**   *************************************************************************
**
**   ****************************
**   *** PROSITE ProRule file ***
**   ****************************
**
**   Release 20.72 of 05-Apr-2011.
**
**   *************************************************************************
**
**   PROSITE is developed by the Swiss Institute of Bioinformatics (SIB) under
**   the responsability of Amos Bairoch and Nicolas Hulo.
**
**   This release was prepared by: Amos Bairoch, Nicolas Hulo, Virginie
**   Buillard, Petra Langendijk-Genevaux and Christian Sigrist with the
**   help of Edouard De Castro, Lorenzo Cerutti and Corinne Lachaize.
**
**   See: http://www.expasy.org/prosite/prorule.html
**   Email: prosite@expasy.org
**
**   *************************************************************************
**
**   PROSITE is copyright.   It  is  produced  by  the  Swiss  Institute   of
**   Bioinformatics (SIB). There are no restrictions on its use by non-profit
**   institutions as long as its  content is in no way modified. Usage by and
**   for commercial  entities requires a license agreement.   For information
**   about  the  licensing  scheme   send  an  email to license@isb-sib.ch or
**   see: http://www.expasy.org/prosite/prosite_license.htm.
**
**   *************************************************************************
//
AC   PRU00001;
DC   Domain;
TR   PROSITE; PS50310; ALA_RICH; 1; level=0
XX
Names: Alanine-rich domain
Function: Unknown
XX
FT   From: PS50310
FT   COMPBIAS   from     to       Ala-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00002;
DC   Domain;
TR   PROSITE; PS50323; ARG_RICH; 1; level=0
XX
Names: Arginine-rich domain
Function: Unknown
XX
FT   From: PS50323
FT   COMPBIAS   from     to       Arg-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00003;
DC   Domain;
TR   PROSITE; PS50321; ASN_RICH; 1; level=0
XX
Names: Asparagine-rich domain
Function: Unknown
XX
FT   From: PS50321
FT   COMPBIAS   from     to       Asn-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00004;
DC   Domain;
TR   PROSITE; PS50312; ASP_RICH; 1; level=0
XX
Names: Aspartate-rich domain
Function: Unknown
XX
FT   From: PS50312
FT   COMPBIAS   from     to       Asp-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00005;
DC   Domain;
TR   PROSITE; PS50311; CYS_RICH; 1; level=0
XX
Names: Cysteine-rich domain
Function: Unknown
XX
FT   From: PS50311
FT   COMPBIAS   from     to       Cys-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00006;
DC   Domain;
TR   PROSITE; PS50322; GLN_RICH; 1; level=0
XX
Names: Glutamine-rich domain
Function: Unknown
XX
FT   From: PS50322
FT   COMPBIAS   from     to       Gln-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00007;
DC   Domain;
TR   PROSITE; PS50313; GLU_RICH; 1; level=0
XX
Names: Glutamate-rich domain
Function: Unknown
XX
FT   From: PS50313
FT   COMPBIAS   from     to       Glu-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00008;
DC   Domain;
TR   PROSITE; PS50315; GLY_RICH; 1; level=0
XX
Names: Glycine-rich domain
Function: Unknown
XX
FT   From: PS50315
FT   COMPBIAS   from     to       Gly-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00009;
DC   Domain;
TR   PROSITE; PS50316; HIS_RICH; 1; level=0
XX
Names: Histidine-rich domain
Function: Unknown
XX
FT   From: PS50316
FT   COMPBIAS   from     to       His-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00010;
DC   Domain;
TR   PROSITE; PS50317; ILE_RICH; 1; level=0
XX
Names: Isoleucine-rich domain
Function: Unknown
XX
FT   From: PS50317
FT   COMPBIAS   from     to       Ile-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00011;
DC   Domain;
TR   PROSITE; PS50319; LEU_RICH; 1; level=0
XX
Names: Leucine-rich domain
Function: Unknown
XX
FT   From: PS50319
FT   COMPBIAS   from     to       Leu-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00012;
DC   Domain;
TR   PROSITE; PS50318; LYS_RICH; 1; level=0
XX
Names: Lysine-rich domain
Function: Unknown
XX
FT   From: PS50318
FT   COMPBIAS   from     to       Lys-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00013;
DC   Domain;
TR   PROSITE; PS50320; MET_RICH; 1; level=0
XX
Names: Methionine-rich domain
Function: Unknown
XX
FT   From: PS50320
FT   COMPBIAS   from     to       Met-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00014;
DC   Domain;
TR   PROSITE; PS50314; PHE_RICH; 1; level=0
XX
Names: Phenylalanine-rich domain
Function: Unknown
XX
FT   From: PS50314
FT   COMPBIAS   from     to       Phe-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00015;
DC   Domain;
TR   PROSITE; PS50099; PRO_RICH; 1; level=0
XX
Names: Proline-rich domain
Function: Unknown
XX
FT   From: PS50099
FT   COMPBIAS   from     to       Pro-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00016;
DC   Domain;
TR   PROSITE; PS50324; SER_RICH; 1; level=0
XX
Names: Serine-rich domain
Function: Unknown
XX
FT   From: PS50324
FT   COMPBIAS   from     to       Ser-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00017;
DC   Domain;
TR   PROSITE; PS50325; THR_RICH; 1; level=0
XX
Names: Threonine-rich domain
Function: Unknown
XX
FT   From: PS50325
FT   COMPBIAS   from     to       Thr-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00018;
DC   Domain;
TR   PROSITE; PS50328; TYR_RICH; 1; level=0
XX
Names: Tyrosine-rich domain
Function: Unknown
XX
FT   From: PS50328
FT   COMPBIAS   from     to       Tyr-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00019;
DC   Domain;
TR   PROSITE; PS50327; TRP_RICH; 1; level=0
XX
Names: Tryptophan-rich domain
Function: Unknown
XX
FT   From: PS50327
FT   COMPBIAS   from     to       Trp-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00020;
DC   Domain;
TR   PROSITE; PS50326; VAL_RICH; 1; level=0
XX
Names: Valine-rich domain
Function: Unknown
XX
FT   From: PS50326
FT   COMPBIAS   from     to       Val-rich.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: unlimited; no keyword;
Topology: Unknown;
Example: Undefined;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
 Plastid
 Mitochondrion
Comments: None
XX
# Revision 1.4  2005/04/18
//
AC   PRU00021;
DC   Domain;
TR   PROSITE; PS50844; AFP_LIKE; 1; level=0
XX
Names: AFP-like domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # AFP-like domain.
FT   From: PS50844
FT   DOMAIN     from     to       AFP-like #.
XX
Chop: Nter=0; Cter=0;
Size: 59-63;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q58465;
Scope:
 Eukaryota; Euteleostomi
 Bacteria; Bacillus
 Archaea; Methanocaldococcus
Comments: None
XX
# Revision 1.3  2005/05/09
//
AC   PRU00022;
DC   Domain;
TR   PROSITE; PS01178; ANAPHYLATOXIN_2; 1; level=0
XX
Names: Anaphylatoxin-like domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # anaphylatoxin-like domain.
DR   PROSITE; PS01177; ANAPHYLATOXIN_1; 1; trigger=no
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS01178
FT   DOMAIN     from     to       Anaphylatoxin-like #.
FT   DISULFID      1     26       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      2     33       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     15     34       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 32-43;
Related: None;
Repeats: 1-3;
Topology: Not cytoplasmic;
Example: P01032;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00023;
DC   Domain;
TR   PROSITE; PS50088; ANK_REPEAT; 1; level=0
XX
Names: ANK repeat
Function: Many ankyrin repeat regions are known to function as protein-protein
 interaction domains.
XX
CC   -!- SIMILARITY: Contains # ANK repeat.
XX
DR   PROSITE; PS50297; ANK_REP_REGION; 1; trigger=no
XX
KW   ANK repeat
XX
FT   From: PS50088
FT   REPEAT     from     to       ANK #.
XX
Chop: Nter=0; Cter=0;
Size: 11-51;
Related: RRU00006!!;
Repeats: 1-27;
Topology: Undefined;
Example: P16157;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses; Chordopoxvirinae
Comments: None
XX
# Revision 1.8  2006/03/28
//
AC   PRU00024;
DC   Domain;
TR   PROSITE; PS50119; ZF_BBOX; 1; level=0
XX
Names: Zinc finger B-box-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # B box-type zinc finger.
XX
KW   Zinc-finger
case <Feature:PS50119:6=[CH]> and <Feature:PS50119:9=[CH]> and <Feature:PS50119:29=[CH]> and <Feature:PS50119:35=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50119
case <Feature:PS50119:6=[C]> and <Feature:PS50119:9=[H]> and <Feature:PS50119:29=[C]> and <Feature:PS50119:35=[H]>
FT   ZN_FING    from     to       B box-type #.
else case <Feature:PS50119:6=[CH]> and <Feature:PS50119:9=[CH]> and <Feature:PS50119:29=[CH]> and <Feature:PS50119:35=[CH]>
FT   ZN_FING    from     to       B box-type #; atypical.
else
FT   ZN_FING    from     to       B box-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 31-54;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q92021;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.8  2005/06/28
//
AC   PRU00025;
DC   Domain;
TR   PROSITE; PS50063; BH4_2; 1; level=0
XX
Names: BH4 motif
Function: Undefined
XX
DR   PROSITE; PS01260; BH4_1; 1; trigger=no
XX
GO   GO:0006915; P:apoptosis
XX
KW   Apoptosis
XX
FT   From: PS50063
FT   MOTIF      from     to       BH4 #.
XX
Chop: Nter=0; Cter=0;
Size: 17-21;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P41957;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.6  2006/07/05
//
AC   PRU00026;
DC   Domain;
TR   PROSITE; PS50197; BEACH; 1; level=0
XX
Names: BEACH
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # BEACH domain.
FT   From: PS50197
FT   DOMAIN     from     to       BEACH #.
XX
Chop: Nter=0; Cter=0;
Size: 103-303;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q10122;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00027;
DC   Domain;
TR   PROSITE; PS50808; ZF_BED; 1; level=0
XX
Names: Zinc finger BED-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # BED-type zinc finger.
XX
KW   Zinc-finger
case <Feature:PS50808:26=[CH]> and <Feature:PS50808:29=[CH]> and <Feature:PS50808:46=[CH]> and <Feature:PS50808:51=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50808
case <Feature:PS50808:26=[C]> and <Feature:PS50808:29=[C]> and <Feature:PS50808:46=[H]> and <Feature:PS50808:51=[CH]>
FT   ZN_FING    from     to       BED-type #.
else case <Feature:PS50808:26=[CH]> and <Feature:PS50808:29=[CH]> and <Feature:PS50808:46=[CH]> and <Feature:PS50808:51=[CH]>
FT   ZN_FING    from     to       BED-type #; atypical.
else
FT   ZN_FING    from     to       BED-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 49-62;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: P34478;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2006/07/17
//
AC   PRU00028;
DC   Domain;
TR   PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 1; level=0
XX
Names: Beta/gamma crystallin 'Greek key' motif
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # beta/gamma crystallin 'Greek key' domain.
FT   From: PS50915
FT   DOMAIN     from     to       Beta/gamma crystallin 'Greek key' #.
XX
Chop: Nter=0; Cter=0;
Size: 33-56;
Related: None;
Repeats: 1-12;
Topology: Undefined;
Example: P43320;
Scope:
 Eukaryota
 Bacteria; Myxococcus
Comments: None
XX
# Revision 1.4  2006/12/05
//
AC   PRU00029;
DC   Domain;
TR   PROSITE; PS50143; BIR_REPEAT_2; 1; level=0
XX
Names: BIR
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # BIR repeat.
DR   PROSITE; PS01282; BIR_REPEAT_1; 1; trigger=no
FT   From: PS50143
FT   REPEAT     from     to       BIR #.
XX
Chop: Nter=0; Cter=0;
Size: 64-98;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: O14064;
Scope:
 Eukaryota
 Viruses; dsDNA viruses, no RNA stage
Comments: None
XX
# Revision 1.4  2005/04/29
//
AC   PRU00030;
DC   Domain;
TR   PROSITE; PS50925; BLUF; 1; level=0
XX
Names: BLUF domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # BLUF domain.
FT   From: PS50925
FT   DOMAIN     from     to       BLUF #.
XX
Chop: Nter=0; Cter=0;
Size: 93-93;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P75990;
Scope:
 Bacteria; Escherichia
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00031;
DC   Domain;
TR   PROSITE; PS50279; BPTI_KUNITZ_2; 1; level=0
XX
Names: BPTI/Kunitz inhibitor domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # BPTI/Kunitz inhibitor domain.
XX
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1; trigger=no
XX
GO   GO:0004866; F:endopeptidase inhibitor activity
GO   GO:0004867; F:serine protease inhibitor activity
XX
KW   Protease inhibitor
KW   Serine protease inhibitor
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50279
FT   DOMAIN     from     to       BPTI/Kunitz inhibitor #.
FT   DISULFID      1     51       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     10     34       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     26     47       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 51-76;
Related: None;
Repeats: 1-5;
Topology: Undefined;
Example: Q60495;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00032;
DC   Domain;
TR   PROSITE; PS50138; BRCA2_REPEAT; 1; level=0
XX
Names: BRCA2
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # BRCA2 repeat.
FT   From: PS50138
FT   REPEAT     from     to       BRCA2 #.
XX
Chop: Nter=0; Cter=0;
Size: 18-35;
Related: None;
Repeats: 1-8;
Topology: Undefined;
Example: P51587;
Scope:
 Eukaryota; Eutheria
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00033;
DC   Domain;
TR   PROSITE; PS50172; BRCT; 1; level=0
XX
Names: BRCT
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # BRCT domain.
FT   From: PS50172
FT   DOMAIN     from     to       BRCT #.
XX
Chop: Nter=0; Cter=0;
Size: 24-129;
Related: None;
Repeats: 1-5;
Topology: Undefined;
Example: P41882;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.4  2005/06/02
//
AC   PRU00034;
DC   Domain;
TR   PROSITE; PS50833; BRIX; 1; level=0
XX
Names: Brix domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # Brix domain.
FT   From: PS50833
FT   DOMAIN     from     to       Brix #.
XX
Chop: Nter=0; Cter=0;
Size: 152-323;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8TDN6;
Scope:
 Eukaryota
 Archaea
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00035;
DC   Domain;
TR   PROSITE; PS50014; BROMODOMAIN_2; 1; level=0
XX
Names: Bromodomain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # bromo domain.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1; trigger=no
XX
KW   Bromodomain
XX
FT   From: PS50014
FT   DOMAIN     from     to       Bromo #.
XX
Chop: Nter=0; Cter=0;
Size: 23-96;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P54816;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2005/06/09
//
AC   PRU00036;
DC   Domain;
TR   PROSITE; PS50858; BSD; 1; level=0
XX
Names: BSD
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # BSD domain.
FT   From: PS50858
FT   DOMAIN     from     to       BSD #.
XX
Chop: Nter=0; Cter=0;
Size: 52-60;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P54858;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00037;
DC   Domain;
TR   PROSITE; PS50097; BTB; 1; level=0
XX
Names: BTB domain
Function: It is a homodimerization domain.
XX
CC   -!- SIMILARITY: Contains # BTB (POZ) domain.
FT   From: PS50097
FT   DOMAIN     from     to       BTB #.
XX
Chop: Nter=0; Cter=0;
Size: 40-177;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q96DT7;
Scope:
 Eukaryota
 Viruses; Chordopoxvirinae
Comments: None
XX
# Revision 1.4  2005/05/11
//
AC   PRU00038;
DC   Domain;
TR   PROSITE; PS50927; BULB_LECTIN; 1; level=0
XX
Names: Bulb-type lectin
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # bulb-type lectin domain.
XX
GO   GO:0005529; F:sugar binding
XX
KW   Lectin
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50927
FT   DOMAIN     from     to       Bulb-type lectin #.
FT   DISULFID     31     58       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 106-130;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P49329;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00039;
DC   Domain;
TR   PROSITE; PS01225; CTCK_2; 1; level=0
XX
Names: C-terminal cystine knot (CTCK) domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CTCK (C-terminal cystine knot-like) domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS01225
FT   DOMAIN     from     to       CTCK #.
FT   DISULFID      1     51       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     16     65       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     27     81       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     31     83       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      ?     87       By similarity.
FT   Tag: disulf; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 72-106;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O95813;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.9  2009/02/09
//
AC   PRU00040;
DC   Domain;
TR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1; level=0
XX
Names: C-type lectin domain
Function: The C-type lectin domain seems to function as a calcium-dependent
 carbohydrate-recognition domain.
XX
CC   -!- SIMILARITY: Contains # C-type lectin domain.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1; trigger=no
XX
GO   GO:0005529; F:sugar binding
XX
KW   Lectin
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50041
FT   DOMAIN     from     to       C-type lectin #.
FT   DISULFID     22    116       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     95    108       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 71-166;
Related: None;
Repeats: 1-10;
Topology: Undefined;
Example: Q9NNX6;
Scope:
 Eukaryota; Metazoa
 Viruses; Avipoxvirus
Comments: None
XX
# Revision 1.9  2009/02/09
//
AC   PRU00041;
DC   Domain;
TR   PROSITE; PS50004; C2; 1; level=0
XX
Names: C2 domain
Function: The C2 domain is thought to be involved in calcium-dependent
 phospholipid binding.
XX
CC   -!- SIMILARITY: Contains # C2 domain.
FT   From: PS50004
FT   DOMAIN     from     to       C2 #.
XX
Chop: Nter=0; Cter=0;
Size: 16-133;
Related: None;
Repeats: 1-5;
Topology: Undefined;
Example: Q6XYQ8;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.8  2006/12/05
//
AC   PRU00042;
DC   Domain;
TR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1; level=0
XX
Names: Zinc finger C2H2-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # C2H2-type zinc finger.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1; trigger=no
XX
KW   Zinc-finger
case <Feature:PS50157:3=[CH]> and <Feature:PS50157:6=[CH]> and <Feature:PS50157:19=[CH]> and <Feature:PS50157:23=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50157
case <Feature:PS50157:3=[C]> and <Feature:PS50157:6=[C]> and <Feature:PS50157:19=[H]> and <Feature:PS50157:23=[H]>
FT   ZN_FING       1     23       C2H2-type #.
else case <Feature:PS50157:3=[CH]> and <Feature:PS50157:6=[CH]> and <Feature:PS50157:19=[CH]> and <Feature:PS50157:23=[CH]>
FT   ZN_FING       1     23       C2H2-type #; atypical.
else
FT   ZN_FING       1     23       C2H2-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 6-40;
Related: None;
Repeats: 1-37;
Topology: Undefined;
Example: Q8ST83;
Scope:
 Eukaryota
 Bacteria; Proteobacteria
 Archaea; Methanocaldococcus
 Viruses
Comments: None
XX
# Revision 1.8  2006/07/17
//
AC   PRU00043;
DC   Domain;
TR   PROSITE; PS50268; CADHERIN_2; 1; level=0
XX
Names: Cadherin
Function: It is suggested that the calcium-binding region of cadherins is
 located in the cadherin domain.
XX
CC   -!- SIMILARITY: Contains # cadherin domain.
DR   PROSITE; PS00232; CADHERIN_1; 1; trigger=no
XX
GO   GO:0005509; F:calcium ion binding
KW   Calcium
XX
FT   From: PS50268
FT   DOMAIN     from     to       Cadherin #.
XX
Chop: Nter=0; Cter=0;
Size: 11-197;
Related: None;
Repeats: 1-34;
Topology: Not cytoplasmic;
Example: O60245;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.6  2005/08/04
//
AC   PRU00044;
DC   Domain;
TR   PROSITE; PS50021; CH; 1; level=0
XX
Names: Calponin-homology domain (CH) domain
Function: Some but not all CH domains are able to bind actin.
XX
CC   -!- SIMILARITY: Contains # CH (calponin-homology) domain.
FT   From: PS50021
FT   DOMAIN     from     to       CH #.
XX
Chop: Nter=0; Cter=0;
Size: 101-139;
Related: None;
Repeats: 1-4;
Topology: Cytoplasmic;
Example: Q01995;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/04/08
//
AC   PRU00045;
DC   Domain;
TR   PROSITE; PS50245; CAP_GLY_2; 1; level=0
XX
Names: CAP-Gly
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CAP-Gly domain.
DR   PROSITE; PS00845; CAP_GLY_1; 1; trigger=no
FT   From: PS50245
FT   DOMAIN     from     to       CAP-Gly #.
XX
Chop: Nter=0; Cter=0;
Size: 43-51;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P11709;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00046;
DC   Domain;
TR   PROSITE; PS50209; CARD; 1; level=0
XX
Names: CARD
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CARD domain.
FT   From: PS50209
FT   DOMAIN     from     to       CARD #.
XX
Chop: Nter=0; Cter=0;
Size: 67-99;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: O95999;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00047;
DC   Domain;
TR   PROSITE; PS50158; ZF_CCHC; 1; level=0
XX
Names: Zinc finger CCHC-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CCHC-type zinc finger.
XX
KW   Zinc-finger
case <Feature:PS50158:3=[CH]> and <Feature:PS50158:6=[CH]> and <Feature:PS50158:11=[CH]> and <Feature:PS50158:16=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50158
case <Feature:PS50158:3=[C]> and <Feature:PS50158:6=[C]> and <Feature:PS50158:11=[H]> and <Feature:PS50158:16=[C]>
FT   ZN_FING    from     to       CCHC-type #.
else case <Feature:PS50158:3=[CH]> and <Feature:PS50158:6=[CH]> and <Feature:PS50158:11=[CH]> and <Feature:PS50158:16=[CH]>
FT   ZN_FING    from     to       CCHC-type #; atypical.
else
FT   ZN_FING    from     to       CCHC-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 14-20;
Related: None;
Repeats: 1-9;
Topology: Undefined;
Example: P03543;
Scope:
 Eukaryota
 Viruses; Retroid viruses
Comments: None
XX
# Revision 1.6  2006/07/17
//
AC   PRU00048;
DC   Domain;
TR   PROSITE; PS50911; CHAP; 1; level=0
XX
Names: CHAP
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # peptidase C51 domain.
XX
GO   GO:0016787; F:hydrolase activity
XX
KW   Hydrolase
XX
FT   From: PS50911
FT   DOMAIN     from     to       Peptidase C51 #.
XX
Chop: Nter=0; Cter=0;
Size: 130-147;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0AES0;
Scope:
 Eukaryota; Crithidia
 Bacteria
Comments: None
XX
# Revision 1.5  2006/11/07
//
AC   PRU00049;
DC   Domain;
TR   PROSITE; PS50839; CHASE; 1; level=0
XX
Names: CHASE
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CHASE domain.
FT   From: PS50839
FT   DOMAIN     from     to       CHASE #.
XX
Chop: Nter=0; Cter=0;
Size: 232-232;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q03101;
Scope:
 Eukaryota; Dictyostelium
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00050;
DC   Domain;
TR   PROSITE; PS50122; CHEB; 1; level=0
XX
Names: cheB-type methylesterase domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # cheB-type methylesterase domain.
XX
case <FTGroup:1>
GO   GO:0016787; F:hydrolase activity
GO   GO:0006935; P:chemotaxis
KW   Hydrolase
KW   Chemotaxis
end case
XX
FT   From: PS50122
FT   DOMAIN     from     to       CheB-type methylesterase #.
FT   ACT_SITE     13     13       By similarity.
FT   Group: 1; Condition: S
FT   ACT_SITE     40     40       By similarity.
FT   Group: 1; Condition: H
FT   ACT_SITE    136    136       By similarity.
FT   Group: 1; Condition: D
XX
Chop: Nter=0; Cter=0;
Size: 141-197;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q8P7A6;
Scope:
 Bacteria
 Archaea; Euryarchaeota
Comments: None
XX
# Revision 1.5  2006/09/04
//
AC   PRU00051;
DC   Domain;
TR   PROSITE; PS50123; CHER; 1; level=0
XX
Names: cheR-type methyltransferase
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # cheR-type methyltransferase domain.
FT   From: PS50123
FT   DOMAIN     from     to       CheR-type methyltransferase #.
XX
Chop: Nter=0; Cter=0;
Size: 256-280;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9KCB8;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00052;
DC   Domain;
TR   PROSITE; PS50851; CHEW; 1; level=0
XX
Names: cheW-like
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # cheW-like domain.
FT   From: PS50851
FT   DOMAIN     from     to       CheW-like #.
XX
Chop: Nter=0; Cter=0;
Size: 129-145;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0A964;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.4  2005/09/14
//
AC   PRU00053;
DC   Domain;
TR   PROSITE; PS50013; CHROMO_2; 1; level=0
XX
Names: Chromo
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # chromo domain.
DR   PROSITE; PS00598; CHROMO_1; 1; trigger=no
FT   From: PS50013
case <Feature:PS50013:48=Y>
FT   DOMAIN     from     to       Chromo #2; shadow subtype.
else
FT   DOMAIN     from     to       Chromo #.
end case
XX
Chop: Nter=0; Cter=0;
Size: 43-104;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P83916;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.6  2006/03/28
//
AC   PRU00054;
DC   Domain;
TR   PROSITE; PS50263; CN_HYDROLASE; 1; level=0
XX
Names: CN hydrolase domain
 Carbon-nitrogen hydrolase domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CN hydrolase domain.
case <FTGroup:1>
GO   GO:0016787; F:hydrolase activity
KW   Hydrolase
end case
FT   From: PS50263
FT   DOMAIN     from     to       CN hydrolase #.
FT   ACT_SITE     41     41       Proton acceptor (Potential).
FT   Group: 1; Condition: E
FT   ACT_SITE    111    111       Potential.
FT   Group: 1; Condition: [KH]
FT   ACT_SITE    147    147       Nucleophile (By similarity).
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 196-322;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9RQ17;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.5  2006/07/05
//
AC   PRU00055;
DC   Domain;
TR   PROSITE; PS50073; COPPER_FIST_2; 1; level=0
XX
Names: Copper-fist DNA-binding domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # copper-fist DNA-binding domain.
DR   PROSITE; PS01119; COPPER_FIST_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   Copper
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
case <FTGroup:1>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50073
FT   DNA_BIND   from     to       Copper-fist #.
FT   METAL        11     11       Zinc (By similarity).
FT   Group: 1; Condition: C
FT   METAL        14     14       Zinc (By similarity).
FT   Group: 1; Condition: C
FT   METAL        23     23       Zinc (By similarity).
FT   Group: 1; Condition: C
FT   METAL        25     25       Zinc (By similarity).
FT   Group: 1; Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 40-40;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P41772;
Scope:
 Eukaryota; Ascomycota
Comments: None
XX
# Revision 1.4  2006/07/05
//
AC   PRU00056;
DC   Domain;
TR   PROSITE; PS50191; CRAL_TRIO; 1; level=0
XX
Names: CRAL-TRIO
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CRAL-TRIO domain.
FT   From: PS50191
FT   DOMAIN     from     to       CRAL-TRIO #.
XX
Chop: Nter=0; Cter=0;
Size: 88-193;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P21359;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00057;
DC   Domain;
TR   PROSITE; PS50108; CRIB; 1; level=0
XX
Names: CRIB
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CRIB domain.
FT   From: PS50108
FT   DOMAIN     from     to       CRIB #.
XX
Chop: Nter=0; Cter=0;
Size: 13-15;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9H3Q1;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00058;
DC   Domain;
TR   PROSITE; PS50897; CTLH; 1; level=0
XX
Names: CTLH
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CTLH domain.
FT   From: PS50897
FT   DOMAIN     from     to       CTLH #.
XX
Chop: Nter=0; Cter=0;
Size: 53-84;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q96G75;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00059;
DC   Domain;
TR   PROSITE; PS01180; CUB; 1; level=0
XX
Names: CUB
Function: The CUB domain [1,2,E1] is an extracellular domain of approximately
 110 residues which is found in functionally diverse, mostly developmentally
 regulated proteins.
XX
CC   -!- SIMILARITY: Contains # CUB domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS01180
FT   DOMAIN     from     to       CUB #.
FT   DISULFID      1     28       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     58     75       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 101-138;
Related: None;
Repeats: 1-5;
Topology: Undefined;
Example: Q8TDF5;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00060;
DC   Domain;
TR   PROSITE; PS50042; CNMP_BINDING_3; 1; level=0
XX
Names: CNMP
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # cyclic nucleotide-binding domain.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1; trigger=no
DR   PROSITE; PS00888; CNMP_BINDING_1; 1; trigger=no
FT   From: PS50042
FT   NP_BIND    from     to       cNMP #.
XX
Chop: Nter=0; Cter=0;
Size: 101-145;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q96L42;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.4  2005/06/09
//
AC   PRU00061;
DC   Domain;
TR   PROSITE; PS50824; DAPIN; 1; level=0
XX
Names: DAPIN
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # DAPIN domain.
FT   From: PS50824
FT   DOMAIN     from     to       DAPIN #.
XX
Chop: Nter=0; Cter=0;
Size: 87-103;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O15553;
Scope:
 Eukaryota; Euteleostomi
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00062;
DC   Domain;
TR   PROSITE; PS50010; DH_2; 1; level=0
XX
Names: Dbl homology (DH) domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # DH (DBL-homology) domain.
XX
DR   PROSITE; PS00741; DH_1; 1; trigger=no
XX
FT   From: PS50010
FT   DOMAIN     from     to       DH #.
XX
Chop: Nter=0; Cter=0;
Size: 160-215;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q9NR80;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/11
//
AC   PRU00063;
DC   Domain;
TR   PROSITE; PS50827; DDT; 1; level=0
XX
Names: DDT domain
Function: A DNA-binding function for the DDT domain has been proposed.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # DDT domain.
XX
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
XX
FT   From: PS50827
FT   DOMAIN     from     to       DDT #.
XX
Chop: Nter=0; Cter=0;
Size: 61-66;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9NRL2;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.6  2008/04/08
//
AC   PRU00064;
DC   Domain;
TR   PROSITE; PS50017; DEATH_DOMAIN; 1; level=0
XX
Names: Death
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # death domain.
FT   From: PS50017
FT   DOMAIN     from     to       Death #.
XX
Chop: Nter=0; Cter=0;
Size: 27-111;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P16157;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00065;
DC   Domain;
TR   PROSITE; PS50168; DED; 1; level=0
XX
Names: DED
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # DED (death effector) domain.
FT   From: PS50168
FT   DOMAIN     from     to       DED #.
XX
Chop: Nter=0; Cter=0;
Size: 71-81;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q14790;
Scope:
 Eukaryota; Eutheria
 Viruses; dsDNA viruses, no RNA stage
Comments: None
XX
# Revision 1.4  2005/09/14
//
AC   PRU00066;
DC   Domain;
TR   PROSITE; PS50186; DEP; 1; level=0
XX
Names: DEP
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # DEP domain.
FT   From: PS50186
FT   DOMAIN     from     to       DEP #.
XX
Chop: Nter=0; Cter=0;
Size: 75-87;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q9Z2H2;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/11
//
AC   PRU00067;
DC   Domain;
TR   PROSITE; PS50216; ZF_DHHC; 1; level=0
XX
Names: Zinc finger DHHC-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # DHHC-type zinc finger.
XX
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS50216
FT   ZN_FING    from     to       DHHC-type #.
XX
Chop: Nter=0; Cter=0;
Size: 51-54;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P39010;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2006/07/17
//
AC   PRU00068;
DC   Domain;
TR   PROSITE; PS50214; DISINTEGRIN_2; 1; level=0
XX
Names: Disintegrin-like
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # disintegrin domain.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1; trigger=no
DR   PROSITE; PS00016; RGD; 1; trigger=yes
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50214
FT   DOMAIN     from     to       Disintegrin #.
FT   DISULFID     60     80       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 57-98;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8K410;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00069;
DC   Domain;
TR   PROSITE; PS50841; DIX; 1; level=0
XX
Names: DIX domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # DIX domain.
XX
KW   Wnt signaling pathway
XX
FT   From: PS50841
FT   DOMAIN     from     to       DIX #.
XX
Chop: Nter=0; Cter=0;
Size: 82-85;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O15169;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00070;
DC   Domain;
TR   PROSITE; PS50809; DM_2; 1; level=0
XX
Names: DM DNA-binding domain
Function: The DM domain binds DNA as a dimer, allowing the recognition of
 pseudopalindromic sequences.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # DM DNA-binding domain.
XX
DR   PROSITE; PS40000; DM_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   DNA-binding
KW   Metal-binding
KW   Zinc
KW   Nucleus
XX
FT   From: PS50809
FT   DNA_BIND   from     to       DM #.
XX
Chop: Nter=0; Cter=0;
Size: 47-49;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P23023;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.8  2008/04/01
//
AC   PRU00071;
DC   Domain;
TR   PROSITE; PS50884; ZF_DOF_2; 1; level=0
XX
Names: Zinc finger Dof-type
Function: Like other zinc fingers the Dof domain has a dual activity: it binds
 DNA in a sequence-specific manner with the core binding site formed by the
 AAAG sequence and it can also mediates protein-protein interaction.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # Dof-type zinc finger.
XX
DR   PROSITE; PS01361; ZF_DOF_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
KW   DNA-binding
KW   Zinc-finger
case <Feature:PS50884:3=[CH]> and <Feature:PS50884:6=[CH]> and <Feature:PS50884:28=[CH]> and <Feature:PS50884:31=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50884
case <Feature:PS50884:3=[C]> and <Feature:PS50884:6=[C]> and <Feature:PS50884:28=[C]> and <Feature:PS50884:31=[C]>
FT   ZN_FING    from     to       Dof-type #.
else case <Feature:PS50884:3=[CH]> and <Feature:PS50884:6=[CH]> and <Feature:PS50884:28=[CH]> and <Feature:PS50884:31=[CH]>
FT   ZN_FING    from     to       Dof-type #; atypical.
else
FT   ZN_FING    from     to       Dof-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 55-55;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q43385;
Scope:
 Eukaryota; Magnoliophyta
Comments: None
XX
# Revision 1.9  2008/04/01
//
AC   PRU00072;
DC   Domain;
TR   PROSITE; PS50309; DC; 1; level=0
XX
Names: Doublecortin
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # doublecortin domain.
FT   From: PS50309
FT   DOMAIN     from     to       Doublecortin #.
XX
Chop: Nter=0; Cter=0;
Size: 80-87;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q9UHG0;
Scope:
 Eukaryota; Eutheria
Comments: None
XX
# Revision 1.3  2005/05/09
//
AC   PRU00073;
DC   Domain;
TR   PROSITE; PS50139; DRADA_REPEAT; 1; level=0
XX
Names: DRADA
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # DRADA repeat.
FT   From: PS50139
FT   REPEAT     from     to       DRADA #.
XX
Chop: Nter=0; Cter=0;
Size: 66-70;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q99MU3;
Scope:
 Eukaryota; Eutheria
 Viruses; Orthopoxvirus
Comments: None
XX
# Revision 1.3  2005/05/09
//
AC   PRU00074;
DC   Domain;
TR   PROSITE; PS50883; EAL; 1; level=0
XX
Names: EAL
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # EAL domain.
FT   From: PS50883
FT   DOMAIN     from     to       EAL #.
XX
Chop: Nter=0; Cter=0;
Size: 47-261;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P14203;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00075;
DC   Domain;
TR   PROSITE; PS50912; EAR; 1; level=0
XX
Names: EAR
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # EAR repeat.
FT   From: PS50912
FT   REPEAT     from     to       EAR #.
XX
Chop: Nter=0; Cter=0;
Size: 44-58;
Related: None;
Repeats: 3-7;
Topology: Undefined;
Example: Q8N135;
Scope:
 Eukaryota; Eutheria
Comments: None
XX
# Revision 1.4  2005/05/11
//
AC   PRU00076;
DC   Domain;
TR   PROSITE; PS50026; EGF_3; 1; level=0
XX
Names: EGF-like domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # EGF-like domain.
XX
DR   PROSITE; PS00022; EGF_1; 1; trigger=no
DR   PROSITE; PS01186; EGF_2; 1; trigger=no
DR   PROSITE; PS01187; EGF_CA; 0-1; trigger=no
XX
case <Feature:PS50026:1-17=[DEQN]-x-[DEQN](2)-C-x(3,14)-C-x(3,7)-C-x-[DN]>
GO   GO:0005509; F:calcium ion binding
KW   Calcium
end case
KW   EGF-like domain
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50026
case <Feature:PS50026:1-17=[DEQN]-x-[DEQN](2)-C-x(3,14)-C-x(3,7)-C-x-[DN]>
FT   DOMAIN     from     to       EGF-like #; calcium-binding (Potential).
else
FT   DOMAIN     from     to       EGF-like #.
end case
FT   DISULFID      5     15       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      9     26       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     28     37       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 13-99;
Related: None;
Repeats: 1-52;
Topology: Undefined;
Example: P01135;
Scope:
 Eukaryota
 Viruses; Chordopoxvirinae
Comments: None
XX
# Revision 1.16  2009/02/09
//
AC   PRU00077;
DC   Domain;
TR   PROSITE; PS50031; EH; 1; level=0
XX
Names: EH
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # EH domain.
FT   From: PS50031
FT   DOMAIN     from     to       EH #.
XX
Chop: Nter=0; Cter=0;
Size: 89-114;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q9JKC9;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/11
//
AC   PRU00078;
DC   Domain;
TR   PROSITE; PS50843; EXPANSIN_CBD; 1; level=0
XX
Names: Expansin-like CBD
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # expansin-like CBD domain.
FT   From: PS50843
FT   DOMAIN     from     to       Expansin-like CBD #.
XX
Chop: Nter=0; Cter=0;
Size: 80-84;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9LZT4;
Scope:
 Eukaryota; Magnoliophyta
Comments: None
XX
# Revision 1.3  2005/05/11
//
AC   PRU00079;
DC   Domain;
TR   PROSITE; PS50842; EXPANSIN_EG45; 1; level=0
XX
Names: Expansin-like EG45
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # expansin-like EG45 domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50842
FT   DOMAIN     from     to       Expansin-like EG45 #.
FT   DISULFID      4     32       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     35    106       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     40     46       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 100-116;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P58738;
Scope:
 Eukaryota; Magnoliophyta
Comments: None
XX
# Revision 1.6  2009/02/09
//
AC   PRU00080;
DC   Domain;
TR   PROSITE; PS50181; FBOX; 1; level=0
XX
Names: F-box
Function: Undefined
XX
**CC   -!- PATHWAY: Ubiquitin conjugation; third step.
**CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex
**CC       (By similarity).
CC   -!- SIMILARITY: Contains # F-box domain.
**XX
**KW   Ubl conjugation pathway
XX
FT   From: PS50181
FT   DOMAIN     from     to       F-box #.
XX
Chop: Nter=0; Cter=0;
Size: 28-153;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P41002;
Scope:
 Eukaryota
 Viruses; dsDNA viruses, no RNA stage
Comments: None
XX
# Revision 1.6  2006/12/20
//
AC   PRU00081;
DC   Domain;
TR   PROSITE; PS50022; FA58C_3; 1; level=0
XX
Names: F5/8 type C
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # F5/8 type C domain.
DR   PROSITE; PS01286; FA58C_2; 1; trigger=no
DR   PROSITE; PS01285; FA58C_1; 1; trigger=no
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50022
FT   DOMAIN     from     to       F5/8 type C #.
FT   DISULFID      1    150       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    137    141       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 139-173;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q8QFX6;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.4  2009/02/09
//
AC   PRU00082;
DC   Domain;
TR   PROSITE; PS50213; FAS1; 1; level=0
XX
Names: FAS1
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # FAS1 domain.
FT   From: PS50213
FT   DOMAIN     from     to       FAS1 #.
XX
Chop: Nter=0; Cter=0;
Size: 123-155;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: Q9SJ81;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.3  2005/05/11
//
AC   PRU00083;
DC   Domain;
TR   PROSITE; PS50133; FCH; 1; level=0
XX
Names: FCH
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # FCH domain.
FT   From: PS50133
FT   DOMAIN     from     to       FCH #.
XX
Chop: Nter=0; Cter=0;
Size: 36-96;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P98171;
Scope:
 Eukaryota
 Viruses; Retroviridae
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00084;
DC   Domain;
TR   PROSITE; PS50057; FERM_3; 1; level=0
XX
Names: FERM
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # FERM domain.
DR   PROSITE; PS00661; FERM_2; 1; trigger=no
DR   PROSITE; PS00660; FERM_1; 1; trigger=no
FT   From: PS50057
FT   DOMAIN     from     to       FERM #.
XX
Chop: Nter=0; Cter=0;
Size: 282-518;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P11171;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/11
//
AC   PRU00085;
DC   Domain;
TR   PROSITE; PS50905; FERRITIN_LIKE; 1; level=0
XX
Names: Ferritin-like diiron domain
Function: Proteins containing a ferritin-like diiron domain possess the
 ability to catalyze oxidation of Fe(2+) to Fe(3+) by O2, i.e. ferroxidase
 activity.
XX
CC   -!- SIMILARITY: Contains # ferritin-like diiron domain.
case <FTGroup:1> or <FTGroup:2>
KW   Metal-binding
KW   Iron
end case
XX
FT   From: PS50905
FT   DOMAIN     from     to       Ferritin-like diiron #.
FT   METAL        18     18       Iron #1 (By similarity).
FT   Group: 1; Condition: E
FT   METAL        51     51       Iron #1 (By similarity).
FT   Group: 1; Condition: E
FT   METAL        51     51       Iron #2 (By similarity).
FT   Group: 1; Condition: E
FT   METAL        96     96       Iron #2 (By similarity).
FT   Group: 1; Condition: E
FT   METAL        99     99       Iron #1 (By similarity).
FT   Group: 1; Condition: E
FT   METAL       129    129       Iron #1 (By similarity).
FT   Group: 1; Condition: E
FT   METAL       129    129       Iron #2 (By similarity).
FT   Group: 1; Condition: E
FT   METAL       132    132       Iron #2 (By similarity).
FT   Group: 1; Condition: H
XX
FT   METAL        18     18       Iron #1 (By similarity).
FT   Group: 2; Condition: E
FT   METAL        51     51       Iron #1 (By similarity).
FT   Group: 2; Condition: E
FT   METAL        51     51       Iron #2 (By similarity).
FT   Group: 2; Condition: E
FT   METAL        52     52       Iron (heme axial ligand) (By similarity).
FT   Optional; Group: 2; Condition: M
FT   METAL        54     54       Iron #1 (By similarity).
FT   Group: 2; Condition: H
FT   METAL        99     99       Iron #2 (By similarity).
FT   Group: 2; Condition: E
FT   METAL       129    129       Iron #1 (By similarity).
FT   Group: 2; Condition: E
FT   METAL       129    129       Iron #2 (By similarity).
FT   Group: 2; Condition: E
FT   METAL       132    132       Iron #2 (By similarity).
FT   Group: 2; Condition: H
XX
case <FTGroup:1> and <FTGroup:2>
Warn: Both types of iron binding amino acid-groups are present!
end case
Chop: Nter=0; Cter=0;
Size: 124-191;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9AGG3;
Scope:
 Bacteria
 Archaea
 Eukaryota
 Plastid
Comments: None
XX
# Revision 1.5  2007/06/27
//
AC   PRU00086;
DC   Domain;
TR   PROSITE; PS50006; FHA_DOMAIN; 1; level=0
XX
Names: FHA
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # FHA domain.
FT   From: PS50006
FT   DOMAIN     from     to       FHA #.
XX
Chop: Nter=0; Cter=0;
Size: 50-81;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P55196;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00087;
DC   Domain;
TR   PROSITE; PS50194; FILAMIN_REPEAT; 1; level=0
XX
Names: Filamin
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # filamin repeat.
FT   From: PS50194
FT   REPEAT     from     to       Filamin #.
XX
Chop: Nter=0; Cter=0;
Size: 63-110;
Related: None;
Repeats: 1-24;
Topology: Undefined;
Example: O75382;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/09
//
AC   PRU00088;
DC   Domain;
TR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1; level=0
XX
Names: Flavodoxin-like domain
Function: The flavodoxin-like domain is involved in electron transfer
 reactions.
XX
CC   -!- SIMILARITY: Contains # flavodoxin-like domain.
FT   From: PS50902
FT   DOMAIN     from     to       Flavodoxin-like #.
FT   NP_BIND       7     11       FMN (By similarity).
FT   NP_BIND      88    119       FMN (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 136-200;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P57503;
Scope:
 Eukaryota
 Bacteria
 Archaea; Euryarchaeota
Comments: None
XX
# Revision 1.3  2006/09/04
//
AC   PRU00089;
DC   Domain;
TR   PROSITE; PS50039; FORK_HEAD_3; 1; level=0
XX
Names: Fork-head DNA-binding domain
Function: Undefined
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Contains # fork-head DNA-binding domain.
DR   PROSITE; PS00658; FORK_HEAD_2; 1; trigger=no
DR   PROSITE; PS00657; FORK_HEAD_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
KW   DNA-binding
XX
FT   From: PS50039
FT   DNA_BIND   from     to       Fork-head #.
XX
Chop: Nter=0; Cter=0;
Size: 77-100;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q12950;
Scope:
 Eukaryota
 Viruses; Avian type C retroviruses
Comments: None
XX
# Revision 1.7  2008/04/01
//
AC   PRU00090;
DC   Domain;
TR   PROSITE; PS50038; FZ; 1; level=0
XX
Names: FZ
Function: Several fz domains have been shown to be both necessary and
 sufficient for Wg/Wnt ligand binding, strongly suggesting that the fz domain
 is a Wg/Wnt interacting domain.
XX
CC   -!- SIMILARITY: Contains # FZ (frizzled) domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50038
FT   DOMAIN     from     to       FZ #.
FT   DISULFID      6     67       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     14     60       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     51     89       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     78    119       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     82    106       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 76-190;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: P97299;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00091;
DC   Domain;
TR   PROSITE; PS50178; ZF_FYVE; 1; level=0
XX
Names: Zinc finger FYVE/FYVE-related type
Function: The FYVE domain target signal-transducing proteins to cell membranes
 through binding to the membrane lipid phosphatidylinositol-3-phosphate
 (PtdIns(3)P) with high specificity.
XX
CC   -!- SIMILARITY: Contains # FYVE-type zinc finger.
XX
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS50178
FT   ZN_FING    from     to       FYVE-type #.
XX
Chop: Nter=0; Cter=0;
Size: 43-83;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P40343;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2006/07/17
//
AC   PRU00092;
DC   Domain;
TR   PROSITE; PS50174; G_PATCH; 1; level=0
XX
Names: G-patch
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # G-patch domain.
FT   From: PS50174
FT   DOMAIN     from     to       G-patch #.
XX
Chop: Nter=0; Cter=0;
Size: 45-50;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O95872;
Scope:
 Eukaryota
 Viruses; Retroviridae
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00093;
DC   Domain;
TR   PROSITE; PS50180; GAE; 1; level=0
XX
Names: GAE
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # GAE domain.
FT   From: PS50180
FT   DOMAIN     from     to       GAE #.
XX
Chop: Nter=0; Cter=0;
Size: 113-122;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q10410;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/09
//
AC   PRU00094;
DC   Domain;
TR   PROSITE; PS50114; GATA_ZN_FINGER_2; 1; level=0
XX
Names: Zinc finger GATA-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # GATA-type zinc finger.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 1; trigger=no
XX
KW   Zinc-finger
case <Feature:PS50114:7=[CH]> and <Feature:PS50114:10=[CH]> and <Feature:PS50114:28=[CH]> and <Feature:PS50114:31=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50114
case <Feature:PS50114:7=[C]> and <Feature:PS50114:10=[C]> and <Feature:PS50114:28=[C]> and <Feature:PS50114:31=[C]>
FT   ZN_FING       7     31       GATA-type #.
else case <Feature:PS50114:7=[CH]> and <Feature:PS50114:10=[CH]> and <Feature:PS50114:28=[CH]> and <Feature:PS50114:31=[CH]>
FT   ZN_FING       7     31       GATA-type #; atypical.
else
FT   ZN_FING       7     31       GATA-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 25-55;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P15976;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.7  2006/07/17
//
AC   PRU00095;
DC   Domain;
TR   PROSITE; PS50887; GGDEF; 1; level=0
XX
Names: GGDEF
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # GGDEF domain.
FT   From: PS50887
FT   DOMAIN     from     to       GGDEF #.
XX
Chop: Nter=0; Cter=0;
Size: 123-138;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P23842;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.4  2005/05/09
//
AC   PRU00096;
DC   Domain;
TR   PROSITE; PS50866; GOLD; 1; level=0
XX
Names: GOLD
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # GOLD domain.
FT   From: PS50866
FT   DOMAIN     from     to       GOLD #.
XX
Chop: Nter=0; Cter=0;
Size: 82-159;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P27869;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00097;
DC   Domain;
TR   PROSITE; PS50877; GOLOCO; 1; level=0
XX
Names: GoLoco
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # GoLoco domain.
FT   From: PS50877
FT   DOMAIN     from     to       GoLoco #.
XX
Chop: Nter=0; Cter=0;
Size: 17-23;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: Q8IVA1;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2005/09/14
//
AC   PRU00098;
DC   Domain;
TR   PROSITE; PS50221; GPS; 1; level=0
XX
Names: GPS domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # GPS domain.
XX
GO   GO:0016021; C:integral to membrane
GO   GO:0016020; C:membrane
XX
KW   Glycoprotein
KW   Membrane
KW   Transmembrane
XX
FT   From: PS50221
FT   DOMAIN     from     to       GPS #.
XX
Chop: Nter=0; Cter=0;
Size: 47-59;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8IZF7;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.6  2006/12/05
//
AC   PRU00099;
DC   Domain;
TR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1; level=0
XX
Names: Guanylate cyclase domain
Function: Undefined
XX
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
CC   -!- SIMILARITY: Contains # guanylate cyclase domain.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1; trigger=no
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
KW   Magnesium
KW   Metal-binding
end case
FT   From: PS50125
FT   DOMAIN     from     to       Guanylate cyclase #.
FT   METAL         6      6       Magnesium 1 (By similarity).
FT   Group: 1; Condition: D
FT   METAL         6      6       Magnesium 2 (By similarity).
FT   Group: 1; Condition: D
FT   METAL         7      7       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   Group: 1; Condition: I
FT   METAL        50     50       Magnesium 1 (By similarity).
FT   Group: 1; Condition: D
FT   METAL        50     50       Magnesium 2 (By similarity).
FT   Group: 1; Condition: D
XX
Chop: Nter=0; Cter=0;
Size: 108-134;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P32870;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.11  2008/07/29
//
AC   PRU00100;
DC   Domain;
TR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1; level=0
XX
Names: Guanylate kinase-like domain
 GK-like domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # guanylate kinase-like domain.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1; trigger=no
XX
GO   GO:0005524; F:ATP binding
GO   GO:0016301; F:kinase activity
GO   GO:0000166; F:nucleotide binding
GO   GO:0016740; F:transferase activity
KW   Transferase
KW   Kinase
KW   ATP-binding
KW   Nucleotide-binding
XX
FT   From: PS50052
FT   DOMAIN     from     to       Guanylate kinase-like #.
FT   NP_BIND       8     15       ATP (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 101-205;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9BXL7;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.5  2006/07/05
//
AC   PRU00101;
DC   Domain;
TR   PROSITE; PS50829; GYF; 1; level=0
XX
Names: GYF
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # GYF domain.
FT   From: PS50829
FT   DOMAIN     from     to       GYF #.
XX
Chop: Nter=0; Cter=0;
Size: 49-59;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P34520;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00102;
DC   Domain;
TR   PROSITE; PS50885; HAMP; 1; level=0
XX
Names: HAMP
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # HAMP domain.
FT   From: PS50885
FT   DOMAIN     from     to       HAMP #.
XX
Chop: Nter=0; Cter=0;
Size: 48-57;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P59963;
Scope:
 Eukaryota; Porphyra
 Bacteria
 Archaea; Halobacteriaceae
Comments: None
XX
# Revision 1.3  2005/05/09
//
AC   PRU00103;
DC   Domain;
TR   PROSITE; PS50077; HEAT_REPEAT; 1; level=0
XX
Names: HEAT_repeat
Function: It has been noted that many HEAT repeat-containing proteins are
 involved in intracellular transport processes.
XX
CC   -!- SIMILARITY: Contains # HEAT repeat.
FT   From: PS50077
FT   REPEAT     from     to       HEAT #.
XX
Chop: Nter=0; Cter=0;
Size: 20-45;
Related: RRU00005!!;
Repeats: 1-20;
Topology: Undefined;
Example: Q09543;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.8  2009/11/27
//
AC   PRU00104;
DC   Domain;
TR   PROSITE; PS50237; HECT; 1; level=0
XX
Names: HECT domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
XX
KW   Ubl conjugation pathway
XX
FT   From: PS50237
FT   DOMAIN     from     to       HECT #.
FT   ACT_SITE    304    304       Glycyl thioester intermediate (By
FT                                similarity).
FT   Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 100-460;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5RBF2;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2006/07/17
//
AC   PRU00105;
DC   Domain;
TR   PROSITE; PS50910; HEPN; 1; level=0
XX
Names: HEPN
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # HEPN domain.
FT   From: PS50910
FT   DOMAIN     from     to       HEPN #.
XX
Chop: Nter=0; Cter=0;
Size: 117-121;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q58700;
Scope:
 Eukaryota; Eutheria
 Archaea; Methanocaldococcus
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00106;
DC   Domain;
TR   PROSITE; PS50834; HIN_200; 1; level=0
XX
Names: HIN-200 domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # HIN-200 domain.
XX
FT   From: PS50834
FT   DOMAIN     from     to       HIN-200 #.
XX
Chop: Nter=0; Cter=0;
Size: 198-201;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q16666;
Scope:
 Eukaryota; Eutheria
Comments: None
XX
# Revision 1.5  2009/12/15
//
AC   PRU00107;
DC   Domain;
TR   PROSITE; PS50109; HIS_KIN; 1; level=0
XX
Names: Histidine kinase core domain
Function: Autophosphorylates at a histidine residue, creating a high-energy
 phosphoryl group that is subsequently transferred to a phosphoacceptor.
XX
CC   -!- SIMILARITY: Contains # histidine kinase domain.
GO   GO:0016740; F:transferase
GO   GO:0016301; F:kinase
KW   Transferase
KW   Kinase
case <Feature:PS50109:4=H>
KW   Phosphoprotein
end case
FT   From: PS50109
FT   DOMAIN     from     to       Histidine kinase #.
FT   MOD_RES       4      4       Phosphohistidine; by autocatalysis (By
FT                                similarity).
FT   Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 157-356;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P59963;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Plastid
 Mitochondrion
Comments: Mitochondrial pyruvate dehydrogenase kinases (PDKs) (EC 2.7.1.99)
 contain an histidine kinase domain which possess a serine/threonine kinase
 activity.
XX
# Revision 1.7  2007/10/13
//
AC   PRU00108;
DC   Domain;
TR   PROSITE; PS50071; HOMEOBOX_2; 1; level=0
XX
Names: Homeobox DNA-binding domain
Function: The homeobox domain binds DNA through a helix-turn-helix type of
 structure.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # homeobox DNA-binding domain.
XX
DR   PROSITE; PS00027; HOMEOBOX_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   DNA-binding
KW   Homeobox
KW   Nucleus
XX
FT   From: PS50071
case <AnyFeature:PS51213>
FT   DNA_BIND  from+1   to+1       Homeobox; TALE-type #.
else
FT   DNA_BIND  from+2   to+1       Homeobox #.
end case
XX
Chop: Nter=0; Cter=0;
Size: 54-82;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: P56915;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.12  2008/04/01
//
AC   PRU00109;
DC   Domain;
TR   PROSITE; PS50815; HORMA; 1; level=0
XX
Names: HORMA
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # HORMA domain.
FT   From: PS50815
FT   DOMAIN     from     to       HORMA #.
XX
Chop: Nter=0; Cter=0;
Size: 184-231;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P20050;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00110;
DC   Domain;
TR   PROSITE; PS50894; HPT; 1; level=0
XX
Names: HPt domain
 Histidine-containing Phosphotransfer domain
Function: Contains a histidine residue capable of participating in phosphoryl
 transfer reactions.
XX
CC   -!- SIMILARITY: Contains # HPt domain.
case <Feature:PS50894:40=H>
KW   Phosphoprotein
end case
FT   From: PS50894
FT   DOMAIN     from     to       HPt #.
FT   MOD_RES      40     40       Phosphohistidine (By similarity).
FT   Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 84-111;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P0AEC5;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.6  2007/10/13
//
AC   PRU00111;
DC   Domain;
TR   PROSITE; PS50932; HTH_LACI_2; 1; level=0
XX
Names: LacI-type HTH domain
Function: The lacI-type HTH domain is a DNA-binding, helix-turn-helix (HTH)
 domain present in the lacI/galR family of transcriptional regulators involved
 in metabolic regulation in prokaryotes.
XX
CC   -!- SIMILARITY: Contains # HTH lacI-type DNA-binding domain.
XX
DR   PROSITE; PS00356; HTH_LACI_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50932
FT   DOMAIN     from     to       HTH lacI-type #.
FT   DNA_BIND      3     22       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 54-62;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P44329;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.6  2006/09/12
//
AC   PRU00112;
DC   Domain;
TR   PROSITE; PS50930; HTH_LYTTR; 1; level=0
XX
Names: LytTR-type HTH domain
Function: The LytTR ('litter') HTH domain is a DNA-binding, potential winged
 helix-turn-helix (wHTH) domain present in bacterial transcriptional
 regulators of the algR/agrA/lytR family.
XX
CC   -!- SIMILARITY: Contains # HTH LytTR-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50930
FT   DOMAIN     from     to       HTH LytTR-type #.
XX
Chop: Nter=0; Cter=0;
Size: 73-106;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0A0I7;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.4  2005/09/14
//
AC   PRU00113;
DC   Domain;
TR   PROSITE; PS50825; HYR; 1; level=0
XX
Names: HYR domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # HYR domain.
FT   From: PS50825
FT   DOMAIN     from     to       HYR #.
XX
Chop: Nter=0; Cter=0;
Size: 83-85;
Related: None;
Repeats: 1-15;
Topology: Undefined;
Example: P78539;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2006/03/20
//
AC   PRU00114;
DC   Domain;
TR   PROSITE; PS50835; IG_LIKE; 1; level=0
XX
Names: Ig-like domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # Ig-like ??-type (immunoglobulin-like)
CC       domain.
XX
KW   Immunoglobulin domain
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50835
FT   DOMAIN     from     to       Ig-like ??-type #.
FT   DISULFID     22     75       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Warn: Check the type of the Ig-like domain(s)
Chop: Nter=0; Cter=0;
Size: 55-135;
Related: None;
Repeats: 1-7;
Topology: Undefined;
Example: P61769;
Scope:
 Eukaryota; Metazoa
 Bacteria
 Viruses; dsDNA viruses, no RNA stage
Comments: None
XX
# Revision 1.12  2009/02/09
//
AC   PRU00115;
DC   Domain;
TR   PROSITE; PS50166; IMPORTIN_B_NT; 1; level=0
XX
Names: Importin N-terminal
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # importin N-terminal domain.
FT   From: PS50166
FT   DOMAIN     from     to       Importin N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 67-89;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P55060;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00116;
DC   Domain;
TR   PROSITE; PS50096; IQ; 1; level=0
XX
Names: IQ
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # IQ domain.
FT   From: PS50096
FT   DOMAIN     from     to       IQ #.
XX
Chop: Nter=0; Cter=0;
Size: 14-33;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: P46940;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00117;
DC   Domain;
TR   PROSITE; PS50084; KH_TYPE_1; 1; level=0
XX
Names: KH domain
Function: The KH domain has been shown to bind RNA.
XX
CC   -!- SIMILARITY: Contains # KH domain.
XX
GO   GO:0003723; F:RNA binding
XX
KW   RNA-binding
XX
FT   From: PS50084
FT   DOMAIN     from     to       KH #.
XX
Chop: Nter=0; Cter=0;
Size: 27-99;
Related: None;
Repeats: 1-14;
Topology: Undefined;
Example: Q9K6V8;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00118;
DC   Domain;
TR   PROSITE; PS50823; KH_TYPE_2; 1; level=0
XX
Names: KH type-2 domain
Function: The KH type-2 domain has been shown to bind RNA.
XX
CC   -!- SIMILARITY: Contains # KH type-2 domain.
XX
GO   GO:0003723; F:RNA binding
XX
KW   RNA-binding
XX
FT   From: PS50823
FT   DOMAIN     from     to       KH type-2 #.
XX
Chop: Nter=0; Cter=0;
Size: 44-97;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8UGK1;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00119;
DC   Domain;
TR   PROSITE; PS50805; KRAB; 1; level=0
XX
Names: KRAB
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # KRAB domain.
XX
FT   From: PS50805
FT   DOMAIN     from     to       KRAB #.
XX
Chop: Nter=0; Cter=0;
Size: 43-97;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q8IVC4;
Scope:
 Eukaryota; Euteleostomi
Comments: None
XX
# Revision 1.5  2005/05/11
//
AC   PRU00120;
DC   Domain;
TR   PROSITE; PS50806; KRAB_RELATED; 1; level=0
XX
Names: KRAB-related domain
Function: The KRAB-related domain is a weak transcriptional repression domain.
XX
CC   -!- SIMILARITY: Contains # KRAB-related domain.
XX
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50806
FT   DOMAIN     from     to       KRAB-related #.
XX
Chop: Nter=0; Cter=0;
Size: 64-64;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q16384;
Scope:
 Eukaryota; Homo
Comments: None
XX
# Revision 1.4  2006/07/05
//
AC   PRU00121;
DC   Domain;
TR   PROSITE; PS50070; KRINGLE_2; 1; level=0
XX
Names: Kringle domain
Function: Kringle domains are thought to play a role in binding mediators,
 such as membranes, other proteins or phospholipids, and in the regulation of
 proteolytic activity.
XX
CC   -!- SIMILARITY: Contains # kringle domain.
DR   PROSITE; PS00021; KRINGLE_1; 1; trigger=no
KW   Kringle
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50070
FT   DOMAIN     from     to       Kringle #.
FT   DISULFID      2     79       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     23     62       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     51     74       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 73-85;
Related: None;
Repeats: 1-10;
Topology: Undefined;
Example: Q14520;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.6  2009/02/09
//
AC   PRU00122;
DC   Domain;
TR   PROSITE; PS50025; LAM_G_DOMAIN; 1; level=0
XX
Names: Laminin G-like
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # laminin G-like domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50025
FT   DOMAIN     from     to       Laminin G-like #.
FT   DISULFID    147    174       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 126-231;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: Q24298;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00123;
DC   Domain;
TR   PROSITE; PS50820; LCCL; 1; level=0
XX
Names: LCCL
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # LCCL domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50820
FT   DOMAIN     from     to       LCCL #.
FT   DISULFID      7     25       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     29     49       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 94-97;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: O42163;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.4  2009/02/09
//
AC   PRU00124;
DC   Domain;
TR   PROSITE; PS50068; LDLRA_2; 1; level=0
XX
Names: LDL-receptor class A
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # LDL-receptor class A domain.
DR   PROSITE; PS01209; LDLRA_1; 1; trigger=no
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50068
FT   DOMAIN     from     to       LDL-receptor class A #.
FT   DISULFID      2     14       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      9     27       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     21     36       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 28-52;
Related: None;
Repeats: 1-36;
Topology: Not cytoplasmic;
Example: Q14114;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00125;
DC   Domain;
TR   PROSITE; PS50023; LIM_DOMAIN_2; 1; level=0
XX
Names: LIM zinc-binding domain
Function: LIM does not bind DNA, rather it seems to act as interface for
 protein-protein interaction.
XX
CC   -!- SIMILARITY: Contains # LIM zinc-binding domain.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1; trigger=no
XX
KW   LIM domain
KW   Metal-binding
KW   Zinc
XX
FT   From: PS50023
FT   DOMAIN    entry   exit       LIM zinc-binding #.
XX
Chop: Nter=0; Cter=0;
Size: 30-114;
Related: None;
Repeats: 1-5;
Topology: Undefined;
Example: P50479;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.6  2006/07/05
//
AC   PRU00126;
DC   Domain;
TR   PROSITE; PS50896; LISH; 1; level=0
XX
Names: LisH
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # LisH domain.
FT   From: PS50896
FT   DOMAIN     from     to       LisH #.
XX
Chop: Nter=0; Cter=0;
Size: 33-33;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q96G75;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00127;
DC   Domain;
TR   PROSITE; PS50838; MAGE; 1; level=0
XX
Names: MAGE
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # MAGE domain.
FT   From: PS50838
FT   DOMAIN     from     to       MAGE #.
XX
Chop: Nter=0; Cter=0;
Size: 123-202;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y5V3;
Scope:
 Eukaryota; Eutheria
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00128;
DC   Domain;
TR   PROSITE; PS50060; MAM_2; 1; level=0
XX
Names: MAM
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # MAM domain.
DR   PROSITE; PS00740; MAM_1; 1; trigger=no
FT   From: PS50060
FT   DOMAIN     from     to       MAM #.
XX
Chop: Nter=0; Cter=0;
Size: 114-171;
Related: None;
Repeats: 1-6;
Topology: Not cytoplasmic;
Example: Q9Y493;
Scope:
 Eukaryota; Euteleostomi
Comments: None
XX
# Revision 1.3  2005/09/14
//
AC   PRU00129;
DC   Domain;
TR   PROSITE; PS50144; MATH; 1; level=0
XX
Names: MATH
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # MATH domain.
FT   From: PS50144
FT   DOMAIN     from     to       MATH #.
XX
Chop: Nter=0; Cter=0;
Size: 117-162;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O94972;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00130;
DC   Domain;
TR   PROSITE; PS50171; ZF_MATRIN; 1; level=0
XX
Names: Zinc finger matrin-type
Function: Undefined
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # matrin-type zinc finger.
XX
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
KW   Zinc-finger
case <Feature:PS50171:3=[CH]> and <Feature:PS50171:6=[CH]> and <Feature:PS50171:21=[CH]> and <Feature:PS50171:27=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50171
case <Feature:PS50171:3=[C]> and <Feature:PS50171:6=[C]> and <Feature:PS50171:21=[H]> and <Feature:PS50171:27=[H]>
FT   ZN_FING    from     to       Matrin-type #.
else case <Feature:PS50171:3=[CH]> and <Feature:PS50171:6=[CH]> and <Feature:PS50171:21=[CH]> and <Feature:PS50171:27=[CH]>
FT   ZN_FING    from     to       Matrin-type #; atypical.
else
FT   ZN_FING    from     to       Matrin-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 31-33;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q9ULV3;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.9  2008/04/08
//
AC   PRU00131;
DC   Domain;
TR   PROSITE; PS50919; MIR; 1; level=0
XX
Names: MIR
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # MIR domain.
FT   From: PS50919
FT   DOMAIN     from     to       MIR #.
XX
Chop: Nter=0; Cter=0;
Size: 46-80;
Related: None;
Repeats: 1-5;
Topology: Undefined;
Example: Q9Y6A1;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00132;
DC   Domain;
TR   PROSITE; PS50202; MSP; 1; level=0
XX
Names: MSP
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # MSP domain.
FT   From: PS50202
FT   DOMAIN     from     to       MSP #.
XX
Chop: Nter=0; Cter=0;
Size: 109-128;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q10484;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00133;
DC   Domain;
TR   PROSITE; PS50090; MYB_LIKE; 1; level=0
XX
Names: Myb-like domain
 Myb/SANT domain
 Myb-like repeat
Function: The myb-like domain resembles the myb-type HTH domain, which is a
 DNA-binding, helix-turn-helix (HTH) domain of  ~55 amino acids, typically
 occurring in a tandem repeat. Myb-like domains can be involved in different
 functions, such as protein-interactions or DNA-binding. The SANT domain does
 not bind to DNA, despite its resemblance to myb-like domains, but it is a
 protein-protein interaction module that can bind to histone-tails
 (see <PRU00624>).
XX
CC   -!- SIMILARITY: Contains # Myb-like domain.
XX
FT   From: PS50090
FT   DOMAIN    entry   exit       Myb-like #.
XX
Chop: Nter=0; Cter=0;
Size: 40-120;
Related: PRU00625; PRU00624;
Repeats: 1-5;
Topology: Undefined;
Example: O14108;
Scope:
 Eukaryota
 Viruses; Avian type C retroviruses
Comments: None
XX
# Revision 1.8  2007/04/03
//
AC   PRU00134;
DC   Domain;
TR   PROSITE; PS50865; ZF_MYND_2; 1; level=0
XX
Names: Zinc finger MYND-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # MYND-type zinc finger.
DR   PROSITE; PS01360; ZF_MYND_1; 1; trigger=no
XX
KW   Zinc-finger
case (<Feature:PS50865:1=[CH]> and <Feature:PS50865:4=[CH]> and <Feature:PS50865:13=[CH]> and <Feature:PS50865:16=[CH]>) or (<Feature:PS50865:22=[CH]> and <Feature:PS50865:26=[CH]> and <Feature:PS50865:34=[CH]> and <Feature:PS50865:38=[CH]>)
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50865
case <Feature:PS50865:1=[CH]> and <Feature:PS50865:4=[C]> and <Feature:PS50865:13=[C]> and <Feature:PS50865:16=[C]> and <Feature:PS50865:22=[C]> and <Feature:PS50865:26=[CH]> and <Feature:PS50865:34=[H]> and <Feature:PS50865:38=[C]>
FT   ZN_FING    from     to       MYND-type #.
else case <Feature:PS50865:1=[CH]> and <Feature:PS50865:4=[CH]> and <Feature:PS50865:13=[CH]> and <Feature:PS50865:16=[CH]> and <Feature:PS50865:22=[CH]> and <Feature:PS50865:26=[CH]> and <Feature:PS50865:34=[CH]> and <Feature:PS50865:38=[CH]>
FT   ZN_FING    from     to       MYND-type #; atypical.
else
FT   ZN_FING    from     to       MYND-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 35-47;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9P2S6;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.6  2006/07/17
//
AC   PRU00135;
DC   Domain;
TR   PROSITE; PS50212; RASGEF_NTER; 1; level=0
XX
Names: N-terminal Ras-GEF domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # N-terminal Ras-GEF domain.
KW   Guanine-nucleotide releasing factor
FT   From: PS50212
FT   DOMAIN     from     to       N-terminal Ras-GEF #.
XX
Chop: Nter=0; Cter=0;
Size: 114-156;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9NZL6;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/10
//
AC   PRU00136;
DC   Domain;
TR   PROSITE; PS50837; NACHT; 1; level=0
XX
Names: NACHT-NTPase domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # NACHT domain.
XX
GO   GO:0005524; F:ATP binding
GO   GO:0000166; F:nucleotide binding
XX
KW   ATP-binding
KW   Nucleotide-binding
XX
FT   From: PS50837
FT   DOMAIN     from     to       NACHT #.
FT   NP_BIND       7     14       ATP (Potential).
XX
Chop: Nter=0; Cter=0;
Size: 295-336;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y239;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2006/07/17
//
AC   PRU00137;
DC   Domain;
TR   PROSITE; PS50177; NTF2_DOMAIN; 1; level=0
XX
Names: NTF2
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # NTF2 domain.
FT   From: PS50177
FT   DOMAIN     from     to       NTF2 #.
XX
Chop: Nter=0; Cter=0;
Size: 88-188;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P61970;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/09/14
//
AC   PRU00138;
DC   Domain;
TR   PROSITE; PS50803; OAR; 1; level=0
XX
Names: OAR domain
Function: Undefined
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
XX
GO   GO:0003677; F:DNA binding
GO   GO:0007275; P:development
GO   GO:0005634; C:nucleus
XX
KW   Developmental protein
KW   Nucleus
XX
FT   From: PS50803
FT   MOTIF      from     to       OAR #.
XX
Chop: Nter=0; Cter=0;
Size: 14-14;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O75364;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.10  2010/05/27
//
AC   PRU00139;
DC   Domain;
TR   PROSITE; PS50802; OTU; 1; level=0
XX
Names: OTU
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # OTU domain.
FT   From: PS50802
FT   DOMAIN     from     to       OTU #.
XX
Chop: Nter=0; Cter=0;
Size: 90-172;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q66431;
Scope:
 Eukaryota
 Bacteria; Chlamydophila
 Viruses
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00140;
DC   Domain;
TR   PROSITE; PS50112; PAS; 1; level=0
XX
Names: PAS
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PAS (PER-ARNT-SIM) domain.
FT   From: PS50112
FT   DOMAIN     from     to       PAS #.
XX
Chop: Nter=0; Cter=0;
Size: 24-90;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P78714;
Scope:
 Eukaryota
 Bacteria
 Archaea; Halobacterium
Comments: None
XX
# Revision 1.5  2005/06/09
//
AC   PRU00141;
DC   Domain;
TR   PROSITE; PS50113; PAC; 1; level=0
XX
Names: PAC domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PAC (PAS-associated C-terminal) domain.
FT   From: PS50113
FT   DOMAIN     from     to       PAC #.
XX
Chop: Nter=0; Cter=0;
Size: 38-60;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: P35841;
Scope:
 Eukaryota
 Bacteria
 Archaea; Halobacterium
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00142;
DC   Domain;
TR   PROSITE; PS50821; PAZ; 1; level=0
XX
Names: PAZ
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PAZ domain.
FT   From: PS50821
FT   DOMAIN     from     to       PAZ #.
XX
Chop: Nter=0; Cter=0;
Size: 109-157;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UL18;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00143;
DC   Domain;
TR   PROSITE; PS50106; PDZ; 1; level=0
XX
Names: PDZ
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PDZ (DHR) domain.
FT   From: PS50106
FT   DOMAIN     from     to       PDZ #.
XX
Chop: Nter=0; Cter=0;
Size: 46-103;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: P0AEH1;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.5  2006/10/09
//
AC   PRU00144;
DC   Domain;
TR   PROSITE; PS50940; CHIT_BIND_II; 1; level=0
XX
Names: Chitin-binding type-2 domain
Function: Chitin-binding
XX
CC   -!- SIMILARITY: Contains # chitin-binding type-2 domain.
XX
GO   GO:0008061; F:chitin binding
XX
KW   Chitin-binding
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50940
FT   DOMAIN    entry   exit       Chitin-binding type-2 #.
FT   DISULFID     34     47       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 50-84;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: Q13231;
Scope:
 Eukaryota
 Viruses; Nucleopolyhedrovirus
Comments: None
XX
# Revision 1.4  2009/02/09
//
AC   PRU00145;
DC   Domain;
TR   PROSITE; PS50003; PH_DOMAIN; 1; level=0
XX
Names: PH
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PH domain.
FT   From: PS50003
FT   DOMAIN     from     to       PH #.
XX
Chop: Nter=0; Cter=0;
Size: 34-344;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: P39969;
Scope:
 Eukaryota
 Viruses; Gammaretrovirus
Comments: None
XX
# Revision 1.4  2005/05/10
//
AC   PRU00146;
DC   Domain;
TR   PROSITE; PS50016; ZF_PHD_2; 1; level=0
XX
Names: Zinc finger PHD-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PHD-type zinc finger.
DR   PROSITE; PS01359; ZF_PHD_1; 1; trigger=no
XX
KW   Zinc-finger
case (<Feature:PS50016:4=[CH]> and <Feature:PS50016:7=[CH]> and <Feature:PS50016:28=[CH]> and <Feature:PS50016:31=[CH]>) or (<Feature:PS50016:20=[CH]> and <Feature:PS50016:23=[CH]> and <Feature:PS50016:48=[CH]> and <Feature:PS50016:51=[CH]>)
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50016
case <Feature:PS50016:4=[C]> and <Feature:PS50016:7=[C]> and <Feature:PS50016:20=[C]> and <Feature:PS50016:23=[C]> and <Feature:PS50016:28=[H]> and <Feature:PS50016:31=[C]> and <Feature:PS50016:48=[C]> and <Feature:PS50016:51=[C]>
FT   ZN_FING    from     to       PHD-type #.
else case <Feature:PS50016:4=[CH]> and <Feature:PS50016:7=[CH]> and <Feature:PS50016:20=[CH]> and <Feature:PS50016:23=[CH]> and <Feature:PS50016:28=[CH]> and <Feature:PS50016:31=[CH]> and <Feature:PS50016:48=[CH]> and <Feature:PS50016:51=[CH]>
FT   ZN_FING    from     to       PHD-type #; atypical.
else
FT   ZN_FING    from     to       PHD-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 34-89;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: P55197;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.7  2006/07/17
//
AC   PRU00147;
DC   Domain;
TR   PROSITE; PS50195; PX; 1; level=0
XX
Names: PX
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PX (phox homology) domain.
FT   From: PS50195
FT   DOMAIN     from     to       PX #.
XX
Chop: Nter=0; Cter=0;
Size: 109-180;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q13596;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00148;
DC   Domain;
TR   PROSITE; PS01179; PID; 1; level=0
XX
Names: PID
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PID domain.
FT   From: PS01179
FT   DOMAIN     from     to       PID #.
XX
Chop: Nter=0; Cter=0;
Size: 113-188;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P49757;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00149;
DC   Domain;
TR   PROSITE; PS50256; PIR_REPEAT_2; 1; level=0
XX
Names: PIR1/2/3 repeat
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PIR1/2/3 repeat.
DR   PROSITE; PS00929; PIR_REPEAT_1; 1; trigger=no
FT   From: PS50256
FT   REPEAT     from     to       PIR1/2/3 #.
XX
Chop: Nter=0; Cter=0;
Size: 13-24;
Related: None;
Repeats: 1-11;
Topology: Undefined;
Example: P46999;
Scope:
 Eukaryota; Saccharomyces
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00150;
DC   Domain;
TR   PROSITE; PS50822; PIWI; 1; level=0
XX
Names: Piwi
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # Piwi domain.
FT   From: PS50822
FT   DOMAIN     from     to       Piwi #.
XX
Chop: Nter=0; Cter=0;
Size: 274-328;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UL18;
Scope:
 Eukaryota
 Archaea; Methanocaldococcus
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00151;
DC   Domain;
TR   PROSITE; PS50093; PKD; 1; level=0
XX
Names: PKD
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PKD domain.
FT   From: PS50093
FT   DOMAIN     from     to       PKD #.
XX
Chop: Nter=0; Cter=0;
Size: 35-101;
Related: None;
Repeats: 1-16;
Topology: Undefined;
Example: P43154;
Scope:
 Eukaryota; Euteleostomi
 Bacteria
 Archaea; Methanocaldococcus
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00152;
DC   Domain;
TR   PROSITE; PS50095; PLAT; 1; level=0
XX
Names: PLAT
Function: It has been proposed that the PLAT domain may be involved in
 protein-protein and protein-lipid interaction.
XX
CC   -!- SIMILARITY: Contains # PLAT domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50095
FT   DOMAIN     from     to       PLAT #.
FT   DISULFID     99    115       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 111-141;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q09624;
Scope:
 Eukaryota
 Bacteria; Clostridium
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00153;
DC   Domain;
TR   PROSITE; PS50035; PLD; 1; level=0
XX
Names: PLD phosphodiesterase
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PLD phosphodiesterase domain.
FT   From: PS50035
FT   DOMAIN     from     to       PLD phosphodiesterase #.
FT   ACT_SITE      6      6       Potential.
FT   Group: 1; Condition: H
FT   ACT_SITE      8      8       Potential.
FT   Group: 1; Condition: K
FT   ACT_SITE     13     13       Potential.
FT   Group: 1; Condition: D
XX
Chop: Nter=0; Cter=0;
Size: 25-41;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P58766;
Scope:
 Eukaryota
 Bacteria
 Viruses; Chordopoxvirinae
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00154;
DC   Domain;
TR   PROSITE; PS50078; POLO_BOX; 1; level=0
XX
Names: POLO box
Function: Point mutations in the POLO box of the budding yeast CDC5 protein
 abolish the ability of overexpressed CDC5 to interact with the spindle poles
 and to organize cytokinetic structures.
XX
CC   -!- SIMILARITY: Contains # POLO box domain.
XX
FT   From: PS50078
FT   DOMAIN     from     to       POLO box #.
XX
Chop: Nter=0; Cter=0;
Size: 62-74;
Related: None;
Repeats: 2;
Topology: Undefined;
Example: P32562;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/10
//
AC   PRU00155;
DC   Domain;
TR   PROSITE; PS50868; POST_SET; 1; level=0
XX
Names: Post-SET
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # post-SET domain.
FT   From: PS50868
FT   DOMAIN     from     to       Post-SET #.
XX
Chop: Nter=0; Cter=0;
Size: 17-17;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O43463;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00156;
DC   Domain;
TR   PROSITE; PS50072; CSA_PPIASE_2; 1; level=0
XX
Names: PPIase cyclophilin-type domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PPIase cyclophilin-type domain.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1; trigger=no
XX
GO   GO:0016853; F:isomerase activity
XX
KW   Isomerase
KW   Rotamase
XX
FT   From: PS50072
FT   DOMAIN     from     to       PPIase cyclophilin-type #.
XX
Chop: Nter=0; Cter=0;
Size: 147-197;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P23284;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.6  2006/07/05
//
AC   PRU00157;
DC   Domain;
TR   PROSITE; PS50867; PRE_SET; 1; level=0
XX
Names: Pre-SET
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # pre-SET domain.
XX
KW   Zinc
XX
FT   From: PS50867
FT   DOMAIN     from     to       Pre-SET #.
FT   METAL         3      3       Zinc 1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL         3      3       Zinc 2 (By similarity).
FT   Group: 1; Condition: C
FT   METAL         5      5       Zinc 1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL         9      9       Zinc 1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL         9      9       Zinc 3 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        15     15       Zinc 1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        17     17       Zinc 2 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        45     45       Zinc 2 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        45     45       Zinc 3 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        49     49       Zinc 2 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        51     51       Zinc 3 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        55     55       Zinc 3 (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 51-96;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9H9B1;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2007/12/14
//
AC   PRU00158;
DC   Domain;
TR   PROSITE; PS50904; PRELI_MSF1; 1; level=0
XX
Names: PRELI/MSF1
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PRELI/MSF1 domain.
FT   From: PS50904
FT   DOMAIN     from     to       PRELI/MSF1 #.
XX
Chop: Nter=0; Cter=0;
Size: 172-175;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y3B1;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00159;
DC   Domain;
TR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1; level=0
XX
Names: Protein kinase domain
Function: Undefined
XX
case <Feature:PS00108>
DE   + RecName: EC=2.7.11.-;
else case <Feature:PS00109>
DE   + RecName: EC=2.7.10.-;
else case <FT:4>
DE   + RecName: EC=2.7.-.-;
end case
case not <FTTag:active>
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
end case
case <Feature:PS00108>
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
else case <Feature:PS00109>
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family.
end case
CC   -!- SIMILARITY: Contains # protein kinase domain.
XX
case <Feature:PS50011:30=K>
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1; trigger=no
end case
case <Feature:PS00108>
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1; trigger=no
else case <Feature:PS00109>
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1; trigger=no
end case
XX
case <Feature:PS00108>
GO   GO:0016301; F:kinase activity
GO   GO:0016740; F:transferase activity
GO   GO:0004674; F:protein serine/threonine kinase activity
KW   Kinase
KW   Transferase
KW   Serine/threonine-protein kinase
else case <Feature:PS00109>
GO   GO:0016301; F:kinase activity
GO   GO:0016740; F:transferase activity
GO   GO:0004713; F:protein-tyrosine kinase activity
KW   Kinase
KW   Transferase
KW   Tyrosine-protein kinase
end case
case <Feature:PS50011:30=K>
GO   GO:0005524; F:ATP binding
GO   GO:0000166; F:nucleotide binding
KW   ATP-binding
KW   Nucleotide-binding
end case
FT   From: PS50011
FT   DOMAIN     from     to       Protein kinase #.
FT   NP_BIND       7     15       ATP (By similarity).
FT   Group: 1; Condition: x*
FT   BINDING      30     30       ATP (By similarity).
FT   Group: 1; Condition: K
case <FTGroup:1>
FT   ACT_SITE    124    124       Proton acceptor (By similarity).
FT   Tag: active; Condition: D
end case
XX
Chop: Nter=0; Cter=0;
Size: 205-549;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: O54967;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.35  2009/02/27
//
AC   PRU00160;
DC   Domain;
TR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1; level=0
XX
Names: Protein-tyrosine phosphatase domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # tyrosine-protein phosphatase domain.
XX
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1; trigger=no
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1; trigger=no
XX
case <Feature:PS50055:196=C>
GO   GO:0016787; F:hydrolase activity
KW   Hydrolase
end case
XX
FT   From: PS50055
FT   DOMAIN     from     to       Tyrosine-protein phosphatase #.
FT   ACT_SITE    196    196       Phosphocysteine intermediate (By
FT                                similarity).
FT   Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 63-419;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P23469;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.8  2005/05/04
//
AC   PRU00161;
DC   Domain;
TR   PROSITE; PS50890; PUA; 1; level=0
XX
Names: PUA
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PUA domain.
FT   From: PS50890
FT   DOMAIN     from     to       PUA #.
XX
Chop: Nter=0; Cter=0;
Size: 75-92;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q58428;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00162;
DC   Domain;
TR   PROSITE; PS50812; PWWP; 1; level=0
XX
Names: PWWP
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PWWP domain.
FT   From: PS50812
FT   DOMAIN     from     to       PWWP #.
XX
Chop: Nter=0; Cter=0;
Size: 51-84;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q9ULU4;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/09/14
//
AC   PRU00163;
DC   Domain;
TR   PROSITE; PS50086; TBC_RABGAP; 1; level=0
XX
Names: Rab-GAP TBC
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # Rab-GAP TBC domain.
FT   From: PS50086
FT   DOMAIN     from     to       Rab-GAP TBC #.
XX
Chop: Nter=0; Cter=0;
Size: 171-284;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P26448;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00164;
DC   Domain;
TR   PROSITE; PS50196; RANBD1; 1; level=0
XX
Names: RanBD1
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # RanBD1 domain.
FT   From: PS50196
FT   DOMAIN     from     to       RanBD1 #.
XX
Chop: Nter=0; Cter=0;
Size: 134-141;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: P32499;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00165;
DC   Domain;
TR   PROSITE; PS50085; RAPGAP; 1; level=0
XX
Names: Rap-GAP domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # Rap-GAP domain.
XX
GO   GO:0005096; F:GTPase activator activity
XX
KW   GTPase activation
XX
FT   From: PS50085
FT   DOMAIN     from     to       Rap-GAP #.
XX
Chop: Nter=0; Cter=0;
Size: 217-235;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P47736;
Scope:
 Eukaryota; Eutheria
Comments: None
XX
# Revision 1.3  2006/07/05
//
AC   PRU00166;
DC   Domain;
TR   PROSITE; PS50200; RA; 1; level=0
XX
Names: Ras-associating
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # Ras-associating domain.
FT   From: PS50200
FT   DOMAIN     from     to       Ras-associating #.
XX
Chop: Nter=0; Cter=0;
Size: 80-103;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P55196;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00167;
DC   Domain;
TR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1; level=0
XX
Names: Ras-GAP
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # Ras-GAP domain.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1; trigger=no
FT   From: PS50018
FT   DOMAIN     from     to       Ras-GAP #.
XX
Chop: Nter=0; Cter=0;
Size: 190-234;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P21359;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00168;
DC   Domain;
TR   PROSITE; PS50009; RASGEF_CAT; 1; level=0
XX
Names: Ras guanine-nucleotide exchange factors catalytic domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # Ras-GEF domain.
XX
DR   PROSITE; PS00720; RASGEF; 1; trigger=no
XX
KW   Guanine-nucleotide releasing factor
XX
FT   From: PS50009
FT   DOMAIN     from     to       Ras-GEF #.
XX
Chop: Nter=0; Cter=0;
Size: 220-271;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9NZL6;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/10
//
AC   PRU00169;
DC   Domain;
TR   PROSITE; PS50110; RESPONSE_REGULATORY; 1; level=0
XX
Names: Response regulatory domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # response regulatory domain.
XX
case <Feature:PS50110:50=D>
KW   Phosphoprotein
end case
XX
FT   From: PS50110
FT   DOMAIN     from     to       Response regulatory #.
FT   MOD_RES      50     50       4-aspartylphosphate (By similarity).
FT   Condition: D
XX
Chop: Nter=0; Cter=0;
Size: 87-143;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P0AEC5;
Scope:
 Eukaryota
 Bacteria
 Archaea; Euryarchaeota
Comments: None
XX
# Revision 1.8  2007/10/13
//
AC   PRU00170;
DC   Domain;
TR   PROSITE; PS50845; RETICULON; 1; level=0
XX
Names: Reticulon
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # reticulon domain.
FT   From: PS50845
FT   DOMAIN     from     to       Reticulon #.
XX
Chop: Nter=0; Cter=0;
Size: 182-201;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P53694;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00171;
DC   Domain;
TR   PROSITE; PS50132; RGS; 1; level=0
XX
Names: RGS
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # RGS domain.
FT   From: PS50132
FT   DOMAIN     from     to       RGS #.
XX
Chop: Nter=0; Cter=0;
Size: 99-270;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: O15169;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00172;
DC   Domain;
TR   PROSITE; PS50238; RHOGAP; 1; level=0
XX
Names: Rho GTPase-activating proteins domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # Rho-GAP domain.
XX
GO   GO:0005096; F:GTPase activator activity
XX
KW   GTPase activation
XX
FT   From: PS50238
FT   DOMAIN     from     to       Rho-GAP #.
XX
Chop: Nter=0; Cter=0;
Size: 173-260;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q3KRB8;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2006/11/21
//
AC   PRU00173;
DC   Domain;
TR   PROSITE; PS50206; RHODANESE_3; 1; level=0
XX
Names: Rhodanese
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # rhodanese domain.
case <AnyFeature:PS50206>=2>
DR   PROSITE; PS00380; RHODANESE_1; 1; trigger=no
DR   PROSITE; PS00683; RHODANESE_2; 1; trigger=no
else
DR   PROSITE; PS00380; RHODANESE_1; 0-1; trigger=no
DR   PROSITE; PS00683; RHODANESE_2; 0-1; trigger=no
end case
FT   From: PS50206
FT   DOMAIN     from     to       Rhodanese #.
case <Feature:PS50206:78-85=C-X-R-G-G-X-R-S>
FT   ACT_SITE     78     78       S-selanylcysteine intermediate (By
FT                                similarity).
else case <Feature:PS50206:78=C>
FT   ACT_SITE     78     78       Cysteine persulfide intermediate (By
FT                                similarity).
end case
XX
Chop: Nter=0; Cter=0;
Size: 75-141;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P96888;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.10  2006/06/29
//
AC   PRU00174;
DC   Domain;
TR   PROSITE; PS50231; RICIN_B_LECTIN; 1; level=0
XX
Names: Ricin B-type lectin
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # ricin B-type lectin domain.
XX
GO   GO:0005529; F:sugar binding
XX
KW   Lectin
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50231
FT   DOMAIN     from     to       Ricin B-type lectin #.
FT   DISULFID     14     31       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     57     74       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    100    118       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 50-151;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q95ZJ1;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00175;
DC   Domain;
TR   PROSITE; PS50089; ZF_RING_2; 1; level=0
XX
Names: Zinc finger RING-type
Function: It has been shown that several RING fingers act as E3 enzymes in the
 ubiquitination process.
XX
**CC   -!- PATHWAY: Ubiquitin conjugation; third step.
**CC   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
**CC       ubiquitin-conjugating enzyme (By similarity).
CC   -!- SIMILARITY: Contains # RING-type zinc finger.
DR   PROSITE; PS00518; ZF_RING_1; 1; trigger=no
XX
KW   Zinc-finger
**KW   Ubl conjugation pathway
case (<Feature:PS50089:1=[CH]> and <Feature:PS50089:4=[CH]> and <Feature:PS50089:23=[CH]> and <Feature:PS50089:26=[CH]>) or (<Feature:PS50089:18=[CH]> and <Feature:PS50089:20=[CH]> and <Feature:PS50089:39=[CH]> and <Feature:PS50089:42=[CH]>)
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50089
case <Feature:PS50089:1=[C]> and <Feature:PS50089:4=[C]> and <Feature:PS50089:18=[C]> and <Feature:PS50089:20=[H]> and <Feature:PS50089:23=[C]> and <Feature:PS50089:26=[C]> and <Feature:PS50089:39=[C]> and <Feature:PS50089:42=[C]>
FT   ZN_FING    from     to       RING-type #.
else case <Feature:PS50089:1=[CH]> and <Feature:PS50089:4=[CH]> and <Feature:PS50089:18=[CH]> and <Feature:PS50089:20=[CH]> and <Feature:PS50089:23=[CH]> and <Feature:PS50089:26=[CH]> and <Feature:PS50089:39=[CH]> and <Feature:PS50089:42=[CH]>
FT   ZN_FING    from     to       RING-type #; atypical.
else
FT   ZN_FING    from     to       RING-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 10-70;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q9M0R4;
Scope:
 Eukaryota
 Viruses; dsDNA viruses, no RNA stage
Comments: None
XX
# Revision 1.10  2006/12/19
//
AC   PRU00176;
DC   Domain;
TR   PROSITE; PS50102; RRM; 1; level=0
XX
Names: RNA recognition motif (RRM) domain
Function: binding RNA
XX
CC   -!- SIMILARITY: Contains # RRM (RNA recognition motif) domain.
XX
GO   GO:0003723; F:RNA binding
XX
KW   RNA-binding
XX
FT   From: PS50102
FT   DOMAIN     from     to       RRM #.
XX
Chop: Nter=0; Cter=0;
Size: 52-151;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: P52298;
Scope:
 Eukaryota
 Bacteria; Synechocystis
Comments: None
XX
# Revision 1.6  2006/07/17
//
AC   PRU00177;
DC   Domain;
TR   PROSITE; PS50142; RNASE_3_2; 1; level=0
XX
Names: RNase III
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # RNase III domain.
DR   PROSITE; PS00517; RNASE_3_1; 1; trigger=no
FT   From: PS50142
FT   DOMAIN     from     to       RNase III #.
XX
Chop: Nter=0; Cter=0;
Size: 67-209;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P47607;
Scope:
 Eukaryota
 Bacteria
 Viruses; Chlorovirus
Comments: None
XX
# Revision 1.3  2005/05/12
//
AC   PRU00178;
DC   Domain;
TR   PROSITE; PS50826; RUN; 1; level=0
XX
Names: RUN
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # RUN domain.
FT   From: PS50826
FT   DOMAIN     from     to       RUN #.
XX
Chop: Nter=0; Cter=0;
Size: 142-142;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q92622;
Scope:
 Eukaryota; Homo
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00179;
DC   Domain;
TR   PROSITE; PS50908; RWD; 1; level=0
XX
Names: RWD
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # RWD domain.
FT   From: PS50908
FT   DOMAIN     from     to       RWD #.
XX
Chop: Nter=0; Cter=0;
Size: 59-151;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P57060;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00180;
DC   Domain;
TR   PROSITE; PS50126; S1; 1; level=0
XX
Names: S1 motif
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # S1 motif domain.
FT   From: PS50126
FT   DOMAIN     from     to       S1 motif #.
XX
Chop: Nter=0; Cter=0;
Size: 33-101;
Related: None;
Repeats: 1-12;
Topology: Undefined;
Example: P05198;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses; Orthopoxvirus
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00181;
DC   Domain;
TR   PROSITE; PS50832; S1_IF1_TYPE; 1; level=0
XX
Names: S1-like domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # S1-like domain.
XX
GO   GO:0006412; P:protein biosynthesis
GO   GO:0003743; F:translation initiation factor activity
XX
KW   Initiation factor
KW   Protein biosynthesis
XX
FT   From: PS50832
FT   DOMAIN     from     to       S1-like #.
XX
Chop: Nter=0; Cter=0;
Size: 57-76;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P47813;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.3  2006/07/05
//
AC   PRU00182;
DC   Domain;
TR   PROSITE; PS50889; S4; 1; level=0
XX
Names: S4 RNA-binding
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # S4 RNA-binding domain.
XX
DR   PROSITE; PS00528; RIBOSOMAL_S4E; 0-1; trigger=no
DR   PROSITE; PS00632; RIBOSOMAL_S4; 0-1; trigger=no
XX
KW   RNA-binding
case <AnyFeature:PS00528> or <AnyFeature:PS00632>
KW   rRNA-binding
end case
XX
FT   From: PS50889
FT   DOMAIN     from     to       S4 RNA-binding #.
XX
Chop: Nter=0; Cter=0;
Size: 53-87;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q44264;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.5  2006/08/29
//
AC   PRU00183;
DC   Domain;
TR   PROSITE; PS50275; SAC; 1; level=0
XX
Names: SAC
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SAC domain.
FT   From: PS50275
FT   DOMAIN     from     to       SAC #.
XX
Chop: Nter=0; Cter=0;
Size: 301-394;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P32368;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/12
//
AC   PRU00184;
DC   Domain;
TR   PROSITE; PS50105; SAM_DOMAIN; 1; level=0
XX
Names: SAM
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SAM (sterile alpha motif) domain.
FT   From: PS50105
FT   DOMAIN     from     to       SAM #.
XX
Chop: Nter=0; Cter=0;
Size: 39-80;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P39969;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2005/05/10
//
AC   PRU00185;
DC   Domain;
TR   PROSITE; PS50864; SAND; 1; level=0
XX
Names: SAND domain
Function: The SAND domain has been proposed to mediate the DNA binding
 activity.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # SAND domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   DNA-binding
KW   Nucleus
XX
FT   From: PS50864
FT   DOMAIN     from     to       SAND #.
XX
Chop: Nter=0; Cter=0;
Size: 81-101;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y692;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.8  2008/04/01
//
AC   PRU00186;
DC   Domain;
TR   PROSITE; PS50800; SAP; 1; level=0
XX
Names: SAP
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SAP domain.
FT   From: PS50800
FT   DOMAIN     from     to       SAP #.
XX
Chop: Nter=0; Cter=0;
Size: 35-35;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P45951;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00187;
DC   Domain;
TR   PROSITE; PS50804; SCAN_BOX; 1; level=0
XX
Names: SCAN box
Function: Undefined
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # SCAN box domain.
XX
KW   Nucleus
XX
GO   GO:0005634; C:nucleus
XX
FT   From: PS50804
FT   DOMAIN     from     to       SCAN box #.
XX
Chop: Nter=0; Cter=0;
Size: 59-95;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P17028;
Scope:
 Eukaryota; Eutheria
Comments: None
XX
# Revision 1.11  2008/04/08
//
AC   PRU00188;
DC   Domain;
TR   PROSITE; PS50024; SEA; 1; level=0
XX
Names: SEA domain
Function: The SEA domain has around 120 residues and its function is not
 known.
XX
CC   -!- SIMILARITY: Contains # SEA domain.
XX
KW   Glycoprotein
FT   From: PS50024
FT   DOMAIN     from     to       SEA #.
XX
Chop: Nter=0; Cter=0;
Size: 111-125;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: Q29435;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.4  2006/07/05
//
AC   PRU00189;
DC   Domain;
TR   PROSITE; PS50190; SEC7; 1; level=0
XX
Names: SEC7
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SEC7 domain.
FT   From: PS50190
FT   DOMAIN     from     to       SEC7 #.
XX
Chop: Nter=0; Cter=0;
Size: 84-206;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UIA0;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/12
//
AC   PRU00190;
DC   Domain;
TR   PROSITE; PS50280; SET; 1; level=0
XX
Names: SET
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SET domain.
FT   From: PS50280
FT   DOMAIN     from     to       SET #.
XX
Chop: Nter=0; Cter=0;
Size: 116-469;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P42124;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00191;
DC   Domain;
TR   PROSITE; PS50001; SH2; 1; level=0
XX
Names: SH2 domain
Function: SH2 domains function as regulatory modules of intracellular
 signalling cascades by interacting with high affinity to phosphotyrosine-
 containing target peptides in a sequence-specific and strictly
 phosphorylation-dependent manner.
XX
CC   -!- SIMILARITY: Contains # SH2 domain.
KW   SH2 domain
FT   From: PS50001
FT   DOMAIN     from     to       SH2 #.
XX
Chop: Nter=0; Cter=0;
Size: 65-129;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q13239;
Scope:
 Eukaryota
 Viruses; Retroviridae
Comments: None
XX
# Revision 1.5  2006/07/17
//
AC   PRU00192;
DC   Domain;
TR   PROSITE; PS50002; SH3; 1; level=0
XX
Names: Src homology 3 (SH3) domain
Function: The function of the SH3 domain is not well understood. The current
 opinion is that they mediate assembly of specific protein complexes via
 binding to proline-rich peptides.
XX
CC   -!- SIMILARITY: Contains # SH3 domain.
XX
KW   SH3 domain
XX
FT   From: PS50002
FT   DOMAIN     from     to       SH3 #.
XX
Chop: Nter=0; Cter=0;
Size: 21-94;
Related: None;
Repeats: 1-5;
Topology: Undefined;
Example: P39969;
Scope:
 Eukaryota
 Viruses; Retroviridae
Comments: None
XX
# Revision 1.5  2007/01/11
//
AC   PRU00193;
DC   Domain;
TR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1; level=0
XX
Names: Sigma-54 factor interaction domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # sigma-54 factor interaction domain.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1; trigger=no
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1; trigger=no
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1; trigger=no
XX
GO   GO:0005524; F:ATP binding
GO   GO:0000166; F:nucleotide binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   ATP-binding
KW   Nucleotide-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50045
FT   DOMAIN     from     to       Sigma-54 factor interaction #.
FT   NP_BIND      29     36       ATP (Potential).
FT   NP_BIND      92    101       ATP (Potential).
XX
Chop: Nter=0; Cter=0;
Size: 200-270;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P41789;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.7  2006/07/17
//
AC   PRU00194;
DC   Domain;
TR   PROSITE; PS50225; SOCS; 1; level=0
XX
Names: SOCS box
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SOCS box domain.
FT   From: PS50225
FT   DOMAIN     from     to       SOCS box #.
XX
Chop: Nter=0; Cter=0;
Size: 47-64;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y576;
Scope:
 Eukaryota; Euteleostomi
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00195;
DC   Domain;
TR   PROSITE; PS50831; SOHO; 1; level=0
XX
Names: SoHo domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SoHo domain.
FT   From: PS50831
FT   DOMAIN     from     to       SoHo #.
XX
Chop: Nter=0; Cter=0;
Size: 46-73;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P28220;
Scope:
 Eukaryota; Eutheria
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00196;
DC   Domain;
TR   PROSITE; PS50287; SRCR_2; 1; level=0
XX
Names: SRCR domain
 Scavenger receptor cysteine-rich domain
Function: Cysteine-rich domains that are likely to mediate protein-protein
 interactions and ligand binding.
XX
CC   -!- SIMILARITY: Contains # SRCR domain.
DR   PROSITE; PS00420; SRCR_1; 1; trigger=no
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50287
FT   DOMAIN     from     to       SRCR #.
FT   DISULFID     26     90       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     39    100       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     70     80       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=28;
Size: 90-130;
Related: None;
Repeats: 1-11;
Topology: Undefined;
Example: Q08380;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.4  2009/02/09
//
AC   PRU00197;
DC   Domain;
TR   PROSITE; PS50848; START; 1; level=0
XX
Names: START
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # START domain.
FT   From: PS50848
FT   DOMAIN     from     to       START #.
XX
Chop: Nter=0; Cter=0;
Size: 202-240;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P46607;
Scope:
 Eukaryota
 Bacteria; Pseudomonas
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00198;
DC   Domain;
TR   PROSITE; PS50801; STAS; 1; level=0
XX
Names: STAS
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # STAS domain.
FT   From: PS50801
FT   DOMAIN     from     to       STAS #.
XX
Chop: Nter=0; Cter=0;
Size: 90-213;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P58743;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00199;
DC   Domain;
TR   PROSITE; PS50156; SSD; 1; level=0
XX
Names: SSD
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SSD (sterol-sensing) domain.
FT   From: PS50156
FT   DOMAIN     from     to       SSD #.
XX
Chop: Nter=0; Cter=0;
Size: 156-182;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q13635;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00200;
DC   Domain;
TR   PROSITE; PS50296; SUI1; 1; level=0
XX
Names: SUI1
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SUI1 domain.
FT   From: PS50296
FT   DOMAIN     from     to       SUI1 #.
XX
Chop: Nter=0; Cter=0;
Size: 60-74;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O43583;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00201;
DC   Domain;
TR   PROSITE; PS50252; TBOX_3; 1; level=0
XX
Names: T-box domain
Function: It probably binds DNA.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # T-box DNA-binding domain.
DR   PROSITE; PS01283; TBOX_1; 1; trigger=no
DR   PROSITE; PS01264; TBOX_2; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
KW   DNA-binding
XX
FT   From: PS50252
FT   DNA_BIND      6    180       T-box #.
XX
Chop: Nter=0; Cter=0;
Size: 64-257;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: O15178;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.6  2008/04/01
//
AC   PRU00202;
DC   Domain;
TR   PROSITE; PS50192; T_SNARE; 1; level=0
XX
Names: t-SNARE coiled-coil homology domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # t-SNARE coiled-coil homology domain.
XX
KW   Coiled coil
XX
FT   From: PS50192
FT   DOMAIN     from     to       t-SNARE coiled-coil homology #.
XX
Chop: Nter=0; Cter=0;
Size: 63-65;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: O15155;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2006/07/05
//
AC   PRU00203;
DC   Domain;
TR   PROSITE; PS50134; ZF_TAZ; 1; level=0
XX
Names: Zinc finger TAZ-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # TAZ-type zinc finger.
XX
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS50134
FT   ZN_FING    from     to       TAZ-type #.
XX
Chop: Nter=0; Cter=0;
Size: 82-107;
Related: None;
Repeats: 2;
Topology: Undefined;
Example: Q92793;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.4  2006/07/17
//
AC   PRU00204;
DC   Domain;
TR   PROSITE; PS50104; TIR; 1; level=0
XX
Names: TIR
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # TIR domain.
FT   From: PS50104
FT   DOMAIN     from     to       TIR #.
XX
Chop: Nter=0; Cter=0;
Size: 132-164;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P08953;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/09/12
//
AC   PRU00205;
DC   Domain;
TR   PROSITE; PS50922; TLC; 1; level=0
XX
Names: TLC domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # TLC (TRAM/LAG1/CLN8) domain.
XX
GO   GO:0016021; C:integral to membrane
GO   GO:0016020; C:membrane
XX
KW   Membrane
KW   Transmembrane
XX
FT   From: PS50922
FT   DOMAIN     from     to       TLC #.
XX
Chop: Nter=0; Cter=0;
Size: 185-217;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P27544;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/12/05
//
AC   PRU00206;
DC   Domain;
TR   PROSITE; PS50050; TNFR_NGFR_2; 1; level=0
XX
Names: TNFR-Cys
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # TNFR-Cys repeat.
DR   PROSITE; PS00652; TNFR_NGFR_1; 1; trigger=no
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50050
FT   REPEAT     from     to       TNFR-Cys #.
FT   DISULFID      2     17       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     20     33       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     23     41       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 18-61;
Related: None;
Repeats: 1-6;
Topology: Not cytoplasmic;
Example: P68637;
Scope:
 Eukaryota
 Viruses; Chordopoxvirinae
Comments: None
XX
# Revision 1.4  2009/02/09
//
AC   PRU00207;
DC   Domain;
TR   PROSITE; PS50145; ZF_TRAF; 1; level=0
XX
Names: Zinc finger TRAF-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # TRAF-type zinc finger.
XX
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS50145
FT   ZN_FING    from     to       TRAF-type #.
XX
Chop: Nter=0; Cter=0;
Size: 53-59;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P11467;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2004/05/06
//
AC   PRU00208;
DC   Domain;
TR   PROSITE; PS50926; TRAM; 1; level=0
XX
Names: TRAM domain
Function: The TRAM domain is predicted to bind tRNA.
XX
CC   -!- SIMILARITY: Contains # TRAM domain.
FT   From: PS50926
FT   DOMAIN     from     to       TRAM #.
XX
Chop: Nter=0; Cter=0;
Size: 55-81;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q96SZ6;
Scope:
 Eukaryota
 Bacteria
 Archaea; Euryarchaeota
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00209;
DC   Domain;
TR   PROSITE; PS50886; TRBD; 1; level=0
XX
Names: tRNA-binding domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # tRNA-binding domain.
XX
GO   GO:0003723; F:RNA binding
GO   GO:0000049; F:tRNA binding
XX
KW   RNA-binding
KW   tRNA-binding
XX
FT   From: PS50886
FT   DOMAIN     from     to       tRNA-binding #.
XX
Chop: Nter=0; Cter=0;
Size: 93-123;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q12904;
Scope:
 Eukaryota
 Bacteria
 Archaea; Euryarchaeota
Comments: None
XX
# Revision 1.5  2006/07/17
//
AC   PRU00210;
DC   Domain;
TR   PROSITE; PS50092; TSP1; 1; level=0
XX
Names: TSP type-1
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # TSP type-1 domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50092
FT   DOMAIN     from     to       TSP type-1 #.
FT   DISULFID     12     47       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID     16     52       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID     26     37       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID      2     37       By similarity.
FT   Tag: disulf; Group: 2; Condition: C-x*-C
FT   DISULFID     12     16       By similarity.
FT   Tag: disulf; Group: 2; Condition: C-x*-C
FT   DISULFID     47     52       By similarity.
FT   Tag: disulf; Group: 2; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 41-84;
Related: None;
Repeats: 1-15;
Topology: Undefined;
Example: Q18206;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2009/02/09
//
AC   PRU00211;
DC   Domain;
TR   PROSITE; PS50304; TUDOR; 1; level=0
XX
Names: Tudor
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # Tudor domain.
FT   From: PS50304
FT   DOMAIN     from     to       Tudor #.
XX
Chop: Nter=0; Cter=0;
Size: 56-64;
Related: None;
Repeats: 1-9;
Topology: Undefined;
Example: Q15047;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00212;
DC   Domain;
TR   PROSITE; PS50030; UBA; 1; level=0
XX
Names: UBA
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # UBA domain.
FT   From: PS50030
FT   DOMAIN     from     to       UBA #.
XX
Chop: Nter=0; Cter=0;
Size: 39-51;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P45974;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00213;
DC   Domain;
TR   PROSITE; PS50330; UIM; 1; level=0
XX
Names: UIM
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # UIM (ubiquitin-interacting motif) repeat.
FT   From: PS50330
FT   REPEAT     from     to       UIM #.
XX
Chop: Nter=0; Cter=0;
Size: 17-20;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P40343;
Scope:
 Eukaryota; Euteleostomi
Comments: None
XX
# Revision 1.3  2005/05/11
//
AC   PRU00214;
DC   Domain;
TR   PROSITE; PS50053; UBIQUITIN_2; 1; level=0
XX
Names: Ubiquitin-like
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # ubiquitin-like domain.
DR   PROSITE; PS00299; UBIQUITIN_1; 1; trigger=no
FT   From: PS50053
FT   DOMAIN     from     to       Ubiquitin-like #.
FT   CROSSLNK     76     76       Glycyl lysine isopeptide (Gly-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins).
FT   Condition: G
XX
Chop: Nter=0; Cter=0;
Size: 39-87;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P63165;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2007/04/20
//
AC   PRU00215;
DC   Domain;
TR   PROSITE; PS50033; UBX; 1; level=0
XX
Names: UBX
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # UBX domain.
FT   From: PS50033
FT   DOMAIN     from     to       UBX #.
XX
Chop: Nter=0; Cter=0;
Size: 77-145;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9BZV1;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00216;
DC   Domain;
TR   PROSITE; PS50173; UMUC; 1; level=0
XX
Names: umuC domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # umuC domain.
XX
case <Feature:PS50173:5=D> or <Feature:PS50173:101=D>
GO   GO:0000287; F:magnesium ion binding
XX
KW   Magnesium
KW   Metal-binding
end case
XX
FT   From: PS50173
FT   DOMAIN     from     to       UmuC #.
FT   METAL         5      5       Magnesium (By similarity).
FT   Condition: D
FT   METAL       101    101       Magnesium (By similarity).
FT   Condition: D
XX
Chop: Nter=0; Cter=0;
Size: 177-257;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P12689;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.5  2006/07/17
//
AC   PRU00217;
DC   Domain;
TR   PROSITE; PS50151; UVR; 1; level=0
XX
Names: UVR
Function: Undefined
XX
CC   -!- SIMILARITY: Contains 1 UVR domain.
FT   From: PS50151
FT   DOMAIN     from     to       UVR #.
XX
Chop: Nter=0; Cter=0;
Size: 35-36;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P46523;
Scope:
 Eukaryota
 Bacteria
 Archaea; Euryarchaeota
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00218;
DC   Domain;
TR   PROSITE; PS50179; VHS; 1; level=0
XX
Names: VHS domain
Function: The VHS domain of Hrs makes both intra- and intermolecular
 interactions with FYVE domains and it has been proposed that it might as well
 interact with other domains.
XX
CC   -!- SIMILARITY: Contains # VHS domain.
FT   From: PS50179
FT   DOMAIN     from     to       VHS #.
XX
Chop: Nter=0; Cter=0;
Size: 131-137;
Related: PRU00243;
Repeats: 1;
Topology: Cytoplasmic;
Example: P40343;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/11
//
AC   PRU00219;
DC   Domain;
TR   PROSITE; PS50234; VWFA; 1; level=0
XX
Names: VWFA
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # VWFA domain.
FT   From: PS50234
FT   DOMAIN     from     to       VWFA #.
XX
Chop: Nter=0; Cter=0;
Size: 123-237;
Related: None;
Repeats: 1-12;
Topology: Undefined;
Example: Q9H6X2;
Scope:
 Eukaryota
 Bacteria
 Archaea; Methanocaldococcus
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00220;
DC   Domain;
TR   PROSITE; PS50184; VWFC_2; 1; level=0
XX
Names: VWFC
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # VWFC domain.
DR   PROSITE; PS01208; VWFC_1; 1; trigger=no
FT   From: PS50184
FT   DOMAIN     from     to       VWFC #.
XX
Chop: Nter=0; Cter=0;
Size: 46-82;
Related: None;
Repeats: 1-5;
Topology: Undefined;
Example: P02452;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.5  2006/03/21
//
AC   PRU00221;
DC   Domain;
TR   PROSITE; PS50082; WD_REPEATS_2; 1; level=0
TR   PROSITE; PS50294; WD_REPEATS_REGION; 1; level=0
XX
Names: WD repeat
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # WD repeat.
DR   PROSITE; PS00678; WD_REPEATS_1; 1; trigger=no
XX
KW   WD repeat
XX
FT   From: PS50082
FT   REPEAT     from     to       WD #.
XX
Chop: Nter=0; Cter=0;
Size: 23-83;
Related: RRU00004!!;
Repeats: 1-16;
Topology: Undefined;
Example: O14576;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.8  2006/07/17
//
AC   PRU00222;
DC   Domain;
TR   PROSITE; PS50814; WIF; 1; level=0
XX
Names: WIF domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # WIF domain.
FT   From: PS50814
FT   DOMAIN     from     to       WIF #.
XX
Chop: Nter=0; Cter=0;
Size: 129-139;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q01887;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00223;
DC   Domain;
TR   PROSITE; PS50811; WRKY; 1; level=0
XX
Names: WRKY DNA-binding domain
Function: The WRKY domain binds specifically to the DNA sequence motif
 (T)(T)TGAC[CT], which is known as the W box.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # WRKY DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50811
FT   DNA_BIND   from     to       WRKY #.
XX
Chop: Nter=0; Cter=0;
Size: 65-71;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q9SI37;
Scope:
 Eukaryota; Arabidopsis
Comments: None
XX
# Revision 1.9  2008/04/08
//
AC   PRU00224;
DC   Domain;
TR   PROSITE; PS50020; WW_DOMAIN_2; 1; level=0
XX
Names: WW/rsp5/WWP domain
Function: It has been shown to bind proteins with particular proline-
 motifs, [AP]-P-P-[AP]-Y.
XX
CC   -!- SIMILARITY: Contains # WW domain.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1; trigger=no
FT   From: PS50020
FT   DOMAIN     from     to       WW #.
XX
Chop: Nter=0; Cter=0;
Size: 26-35;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: Q9H4B6;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00225;
DC   Domain;
TR   PROSITE; PS50882; YTH; 1; level=0
XX
Names: YTH
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # YTH domain.
FT   From: PS50882
FT   DOMAIN     from     to       YTH #.
XX
Chop: Nter=0; Cter=0;
Size: 135-138;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9BYJ9;
Scope:
 Eukaryota; Eutheria
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00226;
DC   Domain;
TR   PROSITE; PS50081; ZF_DAG_PE_2; 1; level=0
XX
Names: Zinc finger phorbol-ester/DAG-type
Function: It is essential for DAG/PE-binding.
XX
CC   -!- SIMILARITY: Contains # phorbol-ester/DAG-type zinc finger.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1; trigger=no
XX
GO   GO:0019992; F:diacylglycerol binding
XX
KW   Metal-binding
KW   Zinc
KW   Zinc-finger
KW   Phorbol-ester binding
XX
FT   From: PS50081
FT   ZN_FING    from     to       Phorbol-ester/DAG-type #.
XX
Chop: Nter=0; Cter=0;
Size: 43-59;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P23743;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.7  2005/05/10
//
AC   PRU00227;
DC   Domain;
TR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1; level=0
XX
Names: Fungal Zn(2)-Cys(6) binuclear cluster domain
Function: It binds DNA in a zinc-dependent fashion.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # Zn(2)-C6 fungal-type DNA-binding domain.
XX
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Metal-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
KW   Zinc
XX
FT   From: PS50048
FT   DNA_BIND      2     29       Zn(2)-C6 fungal-type #.
XX
Chop: Nter=0; Cter=0;
Size: 27-38;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P87000;
Scope:
 Eukaryota; Fungi
Comments: None
XX
# Revision 1.6  2007/06/21
//
AC   PRU00228;
DC   Domain;
TR   PROSITE; PS50135; ZF_ZZ_2; 1; level=0
XX
Names: Zinc finger ZZ-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # ZZ-type zinc finger.
DR   PROSITE; PS01357; ZF_ZZ_1; 1; trigger=no
XX
KW   Zinc-finger
case <Feature:PS50135:7=[CH]> and <Feature:PS50135:10=[CH]> and <Feature:PS50135:31=[CH]> and <Feature:PS50135:34=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50135
case <Feature:PS50135:7=[C]> and <Feature:PS50135:10=[C]> and <Feature:PS50135:31=[C]> and <Feature:PS50135:34=[C]>
FT   ZN_FING    from     to       ZZ-type #.
else case <Feature:PS50135:7=[CH]> and <Feature:PS50135:10=[CH]> and <Feature:PS50135:31=[CH]> and <Feature:PS50135:34=[CH]>
FT   ZN_FING    from     to       ZZ-type #; atypical.
else
FT   ZN_FING    from     to       ZZ-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 42-48;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q92793;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/06/28
//
AC   PRU00229;
DC   Domain;
TR   PROSITE; PS50914; BON; 1; level=0
XX
Names: BON domain
Function: The BON domain is likely to be a phospholipid-binding domain.
XX
CC   -!- SIMILARITY: Contains # BON domain.
FT   From: PS50914
FT   DOMAIN     from     to       BON #.
XX
Chop: Nter=0; Cter=0;
Size: 67-71;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P55702;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00230;
DC   Domain;
TR   PROSITE; PS50933; CHRD; 1; level=0
XX
Names: CHRD domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CHRD domain.
XX
GO   GO:0007275; P:development
XX
KW   Developmental protein
XX
FT   From: PS50933
FT   DOMAIN     from     to       CHRD #.
XX
Chop: Nter=0; Cter=0;
Size: 110-141;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: Q9H2X0;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2005/09/14
//
AC   PRU00231;
DC   Domain;
TR   PROSITE; PS50859; LONGIN; 1; level=0
XX
Names: Longin domain
Function: It has been proposed that the longin domain might be involved in the
 regulation of membrane fusion.
XX
CC   -!- SIMILARITY: Contains # longin domain.
XX
KW   Coiled coil
XX
FT   From: PS50859
FT   DOMAIN     from     to       Longin #.
XX
Chop: Nter=0; Cter=0;
Size: 104-128;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q94AU2;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/07/05
//
AC   PRU00232;
DC   Domain;
TR   PROSITE; PS50906; NIT; 1; level=0
XX
Names: Nitrate and nitrite sensing (NIT) domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # NIT (nitrate and nitrite sensing) domain.
FT   From: PS50906
FT   DOMAIN     from     to       NIT #.
XX
Chop: Nter=0; Cter=0;
Size: 248-248;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q48468;
Scope:
 Bacteria; Klebsiella
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00233;
DC   Domain;
TR   PROSITE; PS50900; PLAC; 1; level=0
XX
Names: PLAC domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # PLAC domain.
XX
FT   From: PS50900
FT   DOMAIN     from     to       PLAC #.
XX
Chop: Nter=0; Cter=0;
Size: 38-45;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P29122;
Scope:
 Eukaryota; Eutheria
Comments: None
XX
# Revision 1.4  2008/02/20
//
AC   PRU00234;
DC   Domain;
TR   PROSITE; PS50916; RABBD; 1; level=0
XX
Names: Rab-binding domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # RabBD (Rab-binding) domain.
FT   From: PS50916
FT   DOMAIN     from     to       RabBD #.
XX
Chop: Nter=0; Cter=0;
Size: 42-184;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q86UR5;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.4  2005/09/14
//
AC   PRU00235;
DC   Domain;
TR   PROSITE; PS50012; RCC1_3; 1; level=0
XX
Names: RCC1 repeat
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # RCC1 repeat.
XX
DR   PROSITE; PS00625; RCC1_1; 1; trigger=no
DR   PROSITE; PS00626; RCC1_2; 1; trigger=no
XX
FT   From: PS50012
FT   REPEAT     from     to       RCC1 #.
XX
Chop: Nter=0; Cter=0;
Size: 39-94;
Related: RRU00003!!;
Repeats: 2-7;
Topology: Undefined;
Example: O74381;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.8  2006/02/07
//
AC   PRU00236;
DC   Domain;
TR   PROSITE; PS50305; SIRTUIN; 1; level=0
XX
Names: Sirtuin catalytic domain
 Sir2 domain
Function: Sirtuins are responsible for a newly classified chemical reaction, NAD-
 dependent protein deacetylation.
XX
CC   -!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
CC       acetyl-ADP-ribose + a protein.
CC   -!- SIMILARITY: Belongs to the sirtuin family.
XX
GO   GO:0016787; F:hydrolase activity
XX
KW   NAD
KW   Hydrolase
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
XX
FT   From: PS50305
FT   DOMAIN     from     to       Deacetylase sirtuin-type #.
FT   ACT_SITE    115    115       Proton acceptor (By similarity).
FT   Condition: H
FT   METAL       123    123       Zinc (By similarity).
FT   Group: 1; Condition: C
FT   METAL       126    126       Zinc (By similarity).
FT   Group: 1; Condition: C
FT   METAL       147    147       Zinc (By similarity).
FT   Group: 1; Condition: C
FT   METAL       150    150       Zinc (By similarity).
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 207-331;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P06700;
Scope:
 Eukaryota
 Archaea
 Bacteria
Comments: None
XX
# Revision 1.4  2006/03/21
//
AC   PRU00237;
DC   Domain;
TR   PROSITE; PS50061; ETS_DOMAIN_3; 1; level=0
XX
Names: ETS domain
Function: Involved in DNA-binding. It seems to recognize purine-rich sequences.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # ETS DNA-binding domain.
XX
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1; trigger=no
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50061
FT   DNA_BIND   from     to       ETS #.
XX
Chop: Nter=0; Cter=0;
Size: 80-83;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P14921;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.6  2007/06/21
//
AC   PRU00238;
DC   Domain;
TR   PROSITE; PS01033; GLOBIN; 1; level=0
XX
Names: Globin domain
Function: Globins are heme-containing proteins involved in binding and/or transporting
 oxygen.
XX
CC   -!- SIMILARITY: Belongs to the globin family.
XX
case <FTGroup:1>
GO   GO:0015671; P:oxygen transport
GO   GO:0006810; P:transport
KW   Heme
KW   Iron
KW   Metal-binding
KW   Oxygen transport
KW   Transport
end case
XX
FT   From: PS01033
FT   METAL        66     66       Iron (heme distal ligand) (By
FT                                similarity).
FT   Group: 1; Condition: H
FT   METAL       100    100       Iron (heme proximal ligand) (By
FT                                similarity).
FT   Group: 1; Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 108-151;
Related: None;
Repeats: 1-9;
Topology: Not cytoplasmic;
Example: Q8WWM9;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.4  2005/04/08
//
AC   PRU00239;
DC   Domain;
TR   PROSITE; PS50203; CALPAIN_CAT; 1; level=0
XX
Names: Cysteine proteinase, calpain-type, catalytic domain
Function: Calpains are a family of cytosolic cysteine proteinases
XX
case <FTGroup:1>
DE   + RecName: EC=3.4.22.-;
end case
XX
CC   -!- SIMILARITY: Contains # calpain catalytic domain.
XX
case <FTGroup:1>
GO   GO:0008234; F:cysteine-type peptidase activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0008233; F:peptidase activity
XX
KW   Hydrolase
KW   Protease
KW   Thiol protease
end case
XX
FT   From: PS50203
FT   DOMAIN     from     to       Calpain catalytic #.
FT   ACT_SITE     61     61       By similarity.
FT   Group: 1; Condition: C
FT   ACT_SITE    222    222       By similarity.
FT   Group: 1; Condition: H
FT   ACT_SITE    243    243       By similarity.
FT   Group: 1; Condition: N
XX
Chop: Nter=0; Cter=0;
Size: 291-344;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9HC96;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.6  2009/02/27
//
AC   PRU00240;
DC   Domain;
TR   PROSITE; PS50141; A_DEAMIN_EDITASE; 1; level=0
XX
Names: Adenosine to inosine editase domain
Function: Enzymes that catalyze the site-selective deamination
 of adenosine residue into inosine within double stranded regions of mRNA.
XX
case <FTGroup:1> and <Feature:PS50141:27=E>
DE   + RecName: EC=3.5.4.-;
end case
XX
CC   -!- SIMILARITY: Contains # A to I editase domain.
XX
case <FTGroup:1> and <Feature:PS50141:27=E>
GO   GO:0016787; F:hydrolase activity
XX
KW   Hydrolase
end case
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
XX
FT   From: PS50141
FT   DOMAIN     from     to       A to I editase #.
FT   METAL        25     25       Zinc (By similarity).
FT   Group: 1; Condition: H
FT   ACT_SITE     27     27       Proton donor (By similarity).
FT   Condition: E
FT   METAL        81     81       Zinc (By similarity).
FT   Group: 1; Condition: C
FT   METAL       149    149       Zinc (By similarity).
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 325-367;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q99MU3;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.8  2009/02/27
//
AC   PRU00241;
DC   Domain;
TR   PROSITE; PS50903; RUBREDOXIN_LIKE; 1; level=0
XX
Names: Rubredoxin-like domain
Function: It is involved in electron transfer processes.
XX
CC   -!- SIMILARITY: Contains # rubredoxin-like domain.
DR   PROSITE; PS00202; RUBREDOXIN; 0-1; trigger=no
case <FTGroup:1>
GO   GO:0009490; F:mononuclear iron electron carrier
GO   GO:0006810; P:transport
GO   GO:0006118; P:electron transport
KW   Transport
KW   Electron transport
KW   Metal-binding
KW   Iron
end case
XX
FT   From: PS50903
FT   DOMAIN     from     to       Rubredoxin-like #.
FT   METAL         6      6       Iron #1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL         9      9       Iron #1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        38     38       Iron #1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        41     41       Iron #1 (By similarity).
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 34-54;
Related: None;
Repeats: 2;
Topology: Cytoplasmic;
Example: P19500;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.6  2006/09/05
//
AC   PRU00242;
DC   Domain;
TR   PROSITE; PS50939; CYTOCHROME_B561; 1; level=0
XX
Names: Cytochrome b561 domain
Function: Cytochromes b561 are di-heme transmembrane electron transport
 proteins.
XX
CC   -!- SIMILARITY: Contains # cytochrome b561 domain.
XX
GO   GO:0006118; P:electron transport
GO   GO:0016020; C:membrane
GO   GO:0016021; C:integral to membrane
GO   GO:0006810; P:transport
XX
KW   Electron transport
KW   Membrane
KW   Transmembrane
KW   Transport
case <FTGroup:1>
KW   Heme
KW   Iron
KW   Metal-binding
end case
XX
FT   From: PS50939
FT   DOMAIN     from     to       Cytochrome b561 #.
FT   METAL        37     37       Iron (heme axial ligand) (Potential).
FT   Group: 1; Condition: H
FT   METAL        73     73       Iron (heme axial ligand) (Potential).
FT   Group: 1; Condition: H
FT   METAL        77     77       Iron (heme axial ligand) (Potential).
FT   Group: 1; Condition: H
FT   METAL        95     95       Iron (heme axial ligand) (Potential).
FT   Group: 1; Condition: H
FT   METAL       107    107       Iron (heme axial ligand) (Potential).
FT   Group: 1; Condition: H
FT   METAL       146    146       Iron (heme axial ligand) (Potential).
FT   Group: 1; Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 198-214;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: P49447;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.6  2006/12/05
//
AC   PRU00243;
DC   Domain;
TR   PROSITE; PS50942; ENTH; 1; level=0
XX
Names: ENTH domain
 Epsin NH2-terminal homology domain
 Epsin N-terminal homology domain
Function: The ENTH domain has been shown to bind to phosphoinositides, as well
 as to interact with proteins.
XX
CC   -!- SIMILARITY: Contains # ENTH (epsin N-terminal homology) domain.
XX
DR   General; Transmembrane; -; 6; trigger=yes
XX
FT   From: PS50942
FT   DOMAIN     from     to       ENTH #.
XX
Chop: Nter=0; Cter=0;
Size: 126-134;
Related: PRU00218;
Repeats: 1;
Topology: Cytoplasmic;
Example: O60641;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/13
//
AC   PRU00244;
DC   Domain;
TR   PROSITE; PS50924; MHYT; 1; level=0
XX
Names: MHYT domain
Function: A predicted transmembrane domain that could serve as a sensor domain
 toward oxygen, CO or NO.
XX
CC   -!- SIMILARITY: Contains # MHYT domain.
XX
DR   General; Transmembrane; -; 6-7; trigger=yes
XX
GO   GO:0016020; C:membrane
GO   GO:0016021; C:integral to membrane
XX
KW   Membrane
KW   Transmembrane
XX
FT   From: PS50924
FT   DOMAIN     from     to       MHYT #.
XX
Chop: Nter=0; Cter=0;
Size: 188-195;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9ABX9;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.10  2006/12/05
//
AC   PRU00245;
DC   Domain;
TR   PROSITE; PS50807; GCM; 1; level=0
XX
Names: GCM domain
Function: The GCM motif has been shown to be a DNA binding domain that
 recognizes preferentially the nonpalindromic octamer 5'-ATGCGGGT-3'.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # GCM DNA-binding domain.
XX
GO   GO:0007275; P:development
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   Developmental protein
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
XX
FT   From: PS50807
FT   DNA_BIND   from     to       GCM #.
XX
FT   METAL        63     63       Zinc #1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        69     69       Zinc #2 (By similarity).
FT   Group: 2; Condition: C
FT   METAL        73     73       Zinc #2 (By similarity).
FT   Group: 2; Condition: C
FT   METAL       100    100       Zinc #2 (By similarity).
FT   Group: 2; Condition: C
FT   METAL       105    105       Zinc #2 (By similarity).
FT   Group: 2; Condition: C
FT   METAL       114    114       Zinc #1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL       141    141       Zinc #1 (By similarity).
FT   Group: 1; Condition: H
FT   METAL       143    143       Zinc #1 (By similarity).
FT   Group: 1; Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 156-160;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9NP62;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.9  2008/04/08
//
AC   PRU00246;
DC   Domain;
TR   PROSITE; PS50836; DOMON; 1; level=0
XX
Names: DOMON domain
Function: The architectures of the DOMON domain proteins strongly suggest a
 function in extracellular adhesion.
XX
CC   -!- SIMILARITY: Contains # DOMON domain.
XX
FT   From: PS50836
FT   DOMAIN     from     to       DOMON #.
XX
Chop: Nter=0; Cter=0;
Size: 117-117;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P09172;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00247;
DC   Domain;
TR   PROSITE; PS50934; SWIRM; 1; level=0
XX
Names: SWIRM domain
Function: The SWIRM domain is predicted to mediate specific protein-protein
 interactions in the assembly of chromatin-protein complexes.
XX
CC   -!- SIMILARITY: Contains # SWIRM domain.
XX
FT   From: PS50934
FT   DOMAIN     from     to       SWIRM #.
XX
Chop: Nter=0; Cter=0;
Size: 86-102;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9XWP6;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00248;
DC   Domain;
TR   PROSITE; PS50918; WWE; 1; level=0
XX
Names: WWE domain
Function: The WWE domain could function in specific interactions with other
 proteins and help in targeting the different kinds of E3-like and
 ADP-ribosylation activities to proteins participating in various signaling
 cascades.
XX
CC   -!- SIMILARITY: Contains # WWE domain.
XX
FT   From: PS50918
FT   DOMAIN     from     to       WWE #.
XX
Chop: Nter=0; Cter=0;
Size: 77-91;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: Q7Z6Z7;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00249;
DC   Domain;
TR   PROSITE; PS50917; SPOC; 1; level=0
XX
Names: SPOC domain
Function: The SPOC domain could mediate interaction with corepressors.
XX
CC   -!- SIMILARITY: Contains # SPOC domain.
XX
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50917
FT   DOMAIN     from     to       SPOC #.
XX
Chop: Nter=0; Cter=0;
Size: 167-180;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q8SX83;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/13
//
AC   PRU00250;
DC   Domain;
TR   PROSITE; PS50913; GRIP; 1; level=0
XX
Names: GRIP domain
Function: The GRIP domain mediates binding to Golgi membranes.
XX
CC   -!- SIMILARITY: Contains # GRIP domain.
XX
KW   Golgi apparatus
XX
FT   From: PS50913
FT   DOMAIN     from     to       GRIP #.
XX
Chop: Nter=0; Cter=0;
Size: 48-52;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q96CN9;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/04/24
//
AC   PRU00251;
DC   Domain;
TR   PROSITE; PS50066; MADS_BOX_2; 1; level=0
XX
Names: MADS-box domain
Function: The MADS-box domain is a DNA-binding domain found in transcriptional
 factors.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # MADS-box domain.
DR   PROSITE; PS00350; MADS_BOX_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50066
FT   DOMAIN     from     to       MADS-box #.
XX
Chop: Nter=0; Cter=0;
Size: 55-61;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q8RVL4;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.7  2007/06/21
//
AC   PRU00252;
DC   Domain;
TR   PROSITE; PS50935; SSB; 1; level=0
XX
Names: SSB domain
Function: The SSB domain is involved in binding to ssDNA.
XX
CC   -!- SIMILARITY: Contains # SSB domain.
XX
GO   GO:0003677; F:DNA binding
XX
KW   DNA-binding
XX
FT   From: PS50935
FT   DOMAIN     from     to       SSB #.
XX
Chop: Nter=0; Cter=0;
Size: 97-113;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: P18022;
Scope:
 Eukaryota
 Bacteria
 Bacteriophage
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00253;
DC   Domain;
TR   PROSITE; PS50931; HTH_LYSR; 1; level=0
XX
Names: LysR-type HTH domain
Function: The lysR-type HTH domain is a DNA-binding, winged helix-turn-helix
 (wHTH) domain present in lysR-type transcriptional regulators.
XX
CC   -!- SIMILARITY: Contains # HTH lysR-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50931
FT   DOMAIN     from     to       HTH lysR-type #.
FT   DNA_BIND     18     37       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 44-61;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P45600;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.6  2006/09/12
//
AC   PRU00254;
DC   Domain;
TR   PROSITE; PS50937; HTH_MERR_2; 1; level=0
XX
Names: MerR-type HTH domain
Function: The merR-type HTH domain is a DNA-binding, winged helix-turn-helix
 (wHTH) domain present in the merR family of transcriptional regulators.
XX
CC   -!- SIMILARITY: Contains # HTH merR-type DNA-binding domain.
DR   PROSITE; PS00552; HTH_MERR_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50937
FT   DOMAIN     from     to       HTH merR-type #.
FT   DNA_BIND      4     23       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 27-75;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P0A2Q8;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.5  2006/09/12
//
AC   PRU00255;
DC   Domain;
TR   PROSITE; PS50869; BRICHOS; 1; level=0
XX
Names: BRICHOS domain
Function: Unknown
XX
CC   -!- SIMILARITY: Contains # BRICHOS domain.
FT   From: PS50869
FT   DOMAIN     from     to       BRICHOS #.
XX
Chop: Nter=0; Cter=0;
Size: 83-104;
Related: None;
Repeats: 1;
Topology: Unknown;
Example: Q9Y287;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00256;
DC   Domain;
TR   PROSITE; PS50816; NAF; 1; level=0
XX
Names: NAF domain
Function: The NAF domain represents a minimum protein interaction module that
 is both necessary and sufficient to mediate the interaction with the CBL
 calcium sensor proteins.
XX
CC   -!- SIMILARITY: Contains # NAF domain.
FT   From: PS50816
FT   DOMAIN     from     to       NAF #.
XX
Chop: Nter=0; Cter=0;
Size: 25-26;
Related: None;
Repeats: 1;
Topology: Unknown;
Example: Q8RWC9;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.3  2005/03/09
//
AC   PRU00257;
DC   Domain;
TR   PROSITE; PS50943; HTH_CROC1; 1; level=0
XX
Names: Cro/C1-type HTH domain
Function: The cro/C1-type HTH domain is a DNA-binding, helix-turn-helix (HTH)
 domain in transcriptional regulators.
XX
CC   -!- SIMILARITY: Contains # HTH cro/C1-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50943
FT   DOMAIN     from     to       HTH cro/C1-type #.
FT   DNA_BIND     12     31       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 53-62;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P14819;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Bacteriophage
Comments: None
XX
# Revision 1.3  2006/09/14
//
AC   PRU00258;
DC   Domain;
TR   PROSITE; PS50075; ACP_DOMAIN; 1; level=0
XX
Names: Phosphopantetheine attachment site
Function: Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic
 group of acyl carrier proteins (ACP) in some multienzyme complexes where it
 serves as a 'swinging arm' for the attachment of activated fatty acid and
 amino-acid groups
XX
CC   -!- SIMILARITY: Contains # acyl carrier domain.
XX
case <Feature:PS50075:34=S>
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1; trigger=no
XX
KW   Phosphopantetheine
end case
XX
FT   From: PS50075
FT   DOMAIN     from     to       Acyl carrier #.
FT   MOD_RES      34     34       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   Condition: S
XX
Chop: Nter=0; Cter=0;
Size: 41-79;
Related: None;
Repeats: 1-5;
Topology: Cytoplasmic;
Example: P19787;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.6  2009/05/25
//
AC   PRU00259;
DC   Domain;
TR   PROSITE; PS50176; ARM_REPEAT; 1; level=0
XX
Names: Armadillo/plakoglobin ARM repeat
Function: Interact with diverse binding partners.
XX
CC   -!- SIMILARITY: Contains # ARM repeat.
FT   From: PS50176
FT   REPEAT     from     to       ARM #.
XX
Chop: Nter=0; Cter=0;
Size: 28-45;
Related: RRU00001!!;
Repeats: 1-9;
Topology: Undefined;
Example: P14923;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.6  2006/02/07
//
AC   PRU00260;
DC   Domain;
TR   PROSITE; PS50228; SUEL_LECTIN; 1; level=0
XX
Names: SUEL-type lectin domain
Function: L-rhamnose and D-galactose binding.
XX
CC   -!- SIMILARITY: Contains # SUEL-type lectin domain.
XX
GO   GO:0005529; F:sugar binding
XX
KW   Lectin
XX
FT   From: PS50228
FT   DOMAIN     from     to       SUEL-type lectin #.
XX
Chop: Nter=0; Cter=0;
Size: 87-93;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P58658;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/11/29
//
AC   PRU00261;
DC   Domain;
TR   PROSITE; PS50941; CHIT_BIND_I_2; 1; level=0
XX
Names: Chitin-binding type-1 domain
Function: Bind chitin.
XX
CC   -!- SIMILARITY: Contains # chitin-binding type-1 domain.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1; trigger=no
XX
GO   GO:0008061; F:chitin binding
XX
KW   Chitin-binding
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50941
FT   DOMAIN     from     to       Chitin-binding type-1 #.
FT   DISULFID      4     19       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     13     25       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     18     32       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     36     40       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 36-57;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: Q9S8M0;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00262;
DC   Domain;
TR   PROSITE; PS50898; RBD; 1; level=0
XX
Names: Ras-binding domain
Function: Ras-binding.
XX
CC   -!- SIMILARITY: Contains # RBD (Ras-binding) domain.
FT   From: PS50898
FT   DOMAIN     from     to       RBD #.
XX
Chop: Nter=0; Cter=0;
Size: 68-77;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: O43566;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/17
//
AC   PRU00263;
DC   Domain;
TR   PROSITE; PS50128; SURP; 1; level=0
XX
Names: SURP motif repeat
Function: Unknown
XX
CC   -!- SIMILARITY: Contains # SURP motif repeat.
XX
GO   GO:0006397; P:mRNA processing
GO   GO:0006371; P:mRNA splicing
XX
KW   mRNA processing
KW   mRNA splicing
XX
FT   From: PS50128
FT   REPEAT     from     to       SURP motif #.
XX
Chop: Nter=0; Cter=0;
Size: 39-44;
Related: None;
Repeats: 2;
Topology: Undefined;
Example: Q8IWZ8;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2006/07/17
//
AC   PRU00264;
DC   Domain;
TR   PROSITE; PS50064; PARP_ZN_FINGER_2; 1; level=0
XX
Names: Zinc finger PARP-type
Function: Bind specifically to single-stranded DNA
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # PARP-type zinc finger.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
KW   DNA-binding
KW   Zinc-finger
case <Feature:PS50064:13=[CH]> and <Feature:PS50064:16=[CH]> and <Feature:PS50064:47=[CH]> and <Feature:PS50064:50=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50064
case <Feature:PS50064:13=[C]> and <Feature:PS50064:16=[C]> and <Feature:PS50064:47=[H]> and <Feature:PS50064:50=[C]>
FT   ZN_FING    from     to       PARP-type #.
else case <Feature:PS50064:13=[CH]> and <Feature:PS50064:16=[CH]> and <Feature:PS50064:47=[CH]> and <Feature:PS50064:50=[CH]>
FT   ZN_FING    from     to       PARP-type #; atypical.
else
FT   ZN_FING    from     to       PARP-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 83-93;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P35875;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.9  2008/04/01
//
AC   PRU00265;
DC   Domain;
TR   PROSITE; PS50254; REL_2; 1; level=0
XX
Names: NF-kappa-B/Rel/dorsal domain
Function: Unknown
XX
CC   -!- SIMILARITY: Contains # RHD (Rel-like) domain.
DR   PROSITE; PS01204; REL_1; 1; trigger=no
FT   From: PS50254
FT   DOMAIN     from     to       RHD #.
XX
Chop: Nter=0; Cter=0;
Size: 274-313;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q94527;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.4  2005/05/17
//
AC   PRU00266;
DC   Domain;
TR   PROSITE; PS50137; DS_RBD; 1; level=0
XX
Names: Double stranded RNA-binding domain
Function: Recognize double-stranded RNAs
XX
CC   -!- SIMILARITY: Contains # DRBM (double-stranded RNA-binding) domain.
XX
GO   GO:0003723; F:RNA binding
XX
KW   RNA-binding
XX
FT   From: PS50137
FT   DOMAIN     from     to       DRBM #.
XX
Chop: Nter=0; Cter=0;
Size: 69-91;
Related: None;
Repeats: 1-5;
Topology: Undefined;
Example: P0A7Y0;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.4  2005/09/14
//
AC   PRU00267;
DC   Domain;
TR   PROSITE; PS50118; HMG_BOX_2; 1; level=0
XX
Names: HMG boxes A and B DNA-binding domains
Function: Bind preferentially to distorted DNAs
XX
c?   not <Triggered>
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # HMG box DNA-binding domain.
DR   PROSITE; PS00353; HMG_BOX_1; 0-1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
KW   DNA-binding
XX
FT   From: PS50118
FT   DNA_BIND   from     to       HMG box #.
XX
case <Feature:PS00353==0>
Warn: If the entry belongs to the HMG1/HMG2 protein family, it should contain DR   PROSITE; PS00353; HMG_BOX_1;
end case
Chop: Nter=0; Cter=0;
Size: 44-81;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: Q24537;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.11  2009/01/30
//
AC   PRU00268;
DC   Domain;
TR   PROSITE; PS50881; S5_DSRBD; 1; level=0
XX
Names: S5 double stranded RNA-binding domain
Function: Interacts with the 16S RNA
XX
CC   -!- SIMILARITY: Contains # S5 DRBM domain.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1; trigger=no
XX
GO   GO:0030529; C:ribonucleoprotein complex
GO   GO:0003735; F:structural constituent of ribosome
XX
KW   Ribonucleoprotein
KW   Ribosomal protein
XX
FT   From: PS50881
FT   DOMAIN     from     to       S5 DRBM #.
XX
Chop: Nter=0; Cter=0;
Size: 60-70;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0A7W1;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.5  2005/09/14
//
AC   PRU00269;
DC   Domain;
TR   PROSITE; PS50290; PI3_4_KINASE_3; 1; level=0
XX
Names: PI3K/PI4K domain
Function: Phosphorylates phosphoinositides on the 3-hydroxyl group of the
 inositol ring.
XX
CC   -!- SIMILARITY: Contains # PI3K/PI4K domain.
XX
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1; trigger=no
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1; trigger=no
XX
GO   GO:0016740; F:transferase activity
GO   GO:0016301; F:kinase activity
XX
KW   Transferase
KW   Kinase
XX
FT   From: PS50290
FT   DOMAIN     from     to       PI3K/PI4K #.
XX
Chop: Nter=0; Cter=0;
Size: 244-381;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P22543;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2006/07/17
//
AC   PRU00270;
DC   Domain;
TR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1; level=0
XX
Names: Phosphatidylinositol-specific phospholipase C X domain
Function: Important for the catalytic activity
XX
CC   -!- SIMILARITY: Contains # PI-PLC X-box domain.
XX
case <FTGroup:1>
GO   GO:0016787; F:hydrolase activity
GO   GO:0016042; P:lipid catabolism
GO   GO:0007165; P:signal transduction
XX
KW   Hydrolase
KW   Lipid degradation
KW   Transducer
end case
XX
FT   From: PS50007
FT   DOMAIN     from     to       PI-PLC X-box #.
FT   ACT_SITE     16     16       By similarity.
FT   Group: 1; Condition: H
FT   ACT_SITE     61     61       By similarity.
FT   Group: 1; Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 100-174;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9NQ66;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/19
//
AC   PRU00271;
DC   Domain;
TR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1; level=0
XX
Names: Phosphatidylinositol-specific phospholipase C Y domain
Function: Important for the catalytic activity.
XX
CC   -!- SIMILARITY: Contains # PI-PLC Y-box domain.
XX
GO   GO:0016787; F:hydrolase activity
GO   GO:0007165; P:signal transduction
GO   GO:0016042; P:lipid catabolism
XX
KW   Transducer
KW   Hydrolase
KW   Lipid degradation
XX
FT   From: PS50008
FT   DOMAIN     from     to       PI-PLC Y-box #.
XX
Chop: Nter=0; Cter=0;
Size: 60-120;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9NQ66;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/19
//
AC   PRU00272;
DC   Domain;
TR   PROSITE; PS50830; TNASE_3; 1; level=0
XX
Names: Thermonuclease domain
Function: catalyzes the hydrolysis of both DNA and RNA at the 5' position of
 the phosphodiester bond yielding 3'-mononucleotides and dinucleotides
XX
case (<OC:Bacteria> or <OC:Archaea>) and <Length<240>
CC   -!- SIMILARITY: Belongs to the thermonuclease family.
else
CC   -!- SIMILARITY: Contains # TNase-like domain.
end case
DR   PROSITE; PS01123; TNASE_1; 1; trigger=no
DR   PROSITE; PS01284; TNASE_2; 1; trigger=no
XX
case <FTGroup:1>
GO   GO:0005509; F:calcium ion binding
end case
case <FTGroup:2>
GO   GO:0016787; F:hydrolase activity
end case
XX
case <FTGroup:1>
KW   Calcium
KW   Metal-binding
end case
case <FTGroup:2>
KW   Hydrolase
KW   Nuclease
KW   Endonuclease
end case
XX
FT   From: PS50830
FT   DOMAIN     from     to       TNase-like #.
FT   METAL        14     14       Calcium (By similarity).
FT   Group: 1; Condition: D
FT   METAL        33     33       Calcium (By similarity).
FT   Group: 1; Condition: D
FT   METAL        34     34       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   Group: 1; Condition: T
FT   ACT_SITE     28     28       By similarity.
FT   Group: 2; Condition: R
FT   ACT_SITE     36     36       By similarity.
FT   Group: 2; Condition: E
FT   ACT_SITE     79     79       By similarity.
FT   Group: 2; Condition: R
XX
Chop: Nter=0; Cter=0;
Size: 119-209;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P22997; Q7KZF4;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.10  2008/07/29
//
AC   PRU00273;
DC   Domain;
TR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1; level=0
XX
Names: Intein DOD homing endonuclease
Function: Homing endonucleases are rare-cutting enzymes encoded by inteins and
 introns.
XX
CC   -!- SIMILARITY: Contains # DOD-type homing endonuclease domain.
FT   From: PS50819
FT   DOMAIN     from     to       DOD-type homing endonuclease #.
XX
Chop: Nter=0; Cter=0;
Size: 80-178;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P21505;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.4  2005/04/22
//
AC   PRU00274;
DC   Domain;
TR   PROSITE; PS50240; TRYPSIN_DOM; 1; level=0
XX
Names: Serine proteases, trypsin domain
Function: Cleaves preferentially: Arg-|-Xaa, Lys-|-Xaa
XX
case <FTGroup:1>
DE   + RecName: EC=3.4.21.-;
end case
XX
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains # peptidase S1 domain.
case <FTGroup:1>
DR   PROSITE; PS00134; TRYPSIN_HIS; 1; trigger=no
DR   PROSITE; PS00135; TRYPSIN_SER; 1; trigger=no
else
DR   PROSITE; PS00134; TRYPSIN_HIS; 0-1; trigger=no
DR   PROSITE; PS00135; TRYPSIN_SER; 0-1; trigger=no
end case
case <FTGroup:1>
GO   GO:0016787; F:hydrolase activity
GO   GO:0008233; F:peptidase activity
GO   GO:0004252; F:serine-type endopeptidase activity
XX
KW   Hydrolase
KW   Protease
KW   Serine protease
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50240
FT   DOMAIN     from     to       Peptidase S1 #.
FT   ACT_SITE     42     42       Charge relay system (By similarity).
FT   Group: 1; Condition: H
FT   ACT_SITE     91     91       Charge relay system (By similarity).
FT   Group: 1; Condition: D
FT   ACT_SITE    186    186       Charge relay system (By similarity).
FT   Group: 1; Condition: S
FT   DISULFID     27     43       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    125    192       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    156    171       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    182    210       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 150-286;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q9BYE2;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.16  2009/02/27
//
AC   PRU00275;
DC   Domain;
TR   PROSITE; PS50175; ASP_PROT_RETROV; 1; level=0
XX
Names: Eukaryotic and viral aspartyl proteases
Function: Belongs to peptidase family A2
XX
case <OS:Human immunodeficiency virus type 1> and <Feature:PS50175:6=D>
DE   + RecName: EC=3.4.23.16;
else case <OS:Human immunodeficiency virus type 2> and <Feature:PS50175:6=D>
DE   + RecName: EC=3.4.23.47;
else case <Feature:PS50175:6=D>
DE   + RecName: EC=3.4.23.-;
end case
XX
case <OS:Human immunodeficiency virus type 1>
CC   -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of
CC       Gag and Gag-Pol polyproteins during or shortly after the release
CC       of the virion from the plasma membrane. Cleavages take place as an
CC       ordered, step-wise cascade to yield mature proteins. This process
CC       is called maturation. Displays maximal activity during the budding
CC       process just prior to particle release from the cell. Also cleaves
CC       Nef and Vif, probably concomitantly with viral structural proteins
CC       on maturation of virus particles (By similarity).
else case <OC:retroviridae>
CC   -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of
CC       Gag and Gag-Pol polyproteins during or shortly after the release
CC       of the virion from the plasma membrane. Cleavages take place as an
CC       ordered, step-wise cascade to yield mature proteins. This process
CC       is called maturation. Displays maximal activity during the budding
CC       process just prior to particle release from the cell (By
CC       similarity).
end case
case <OS:Human immunodeficiency virus type 1> and <Feature:PS50175:6=D>
CC   -!- CATALYTIC ACTIVITY: Specific for a P1 residue that is hydrophobic,
CC       and P1' variable, but often Pro.
else case <OS:Human immunodeficiency virus type 2> and <Feature:PS50175:6=D>
CC   -!- CATALYTIC ACTIVITY: Endopeptidase for which the P1 residue is
CC       preferably hydrophobic.
end case
CC   -!- SIMILARITY: Contains # peptidase A2 domain.
XX
DR   PROSITE; PS00141; ASP_PROTEASE; 1; trigger=no
XX
case <Feature:PS50175:6=D>
GO   GO:0004190; F:aspartic-type endopeptidase activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0008233; F:peptidase activity
XX
KW   Aspartyl protease
KW   Hydrolase
KW   Protease
end case
XX
FT   From: PS50175
FT   DOMAIN     from     to       Peptidase A2 #.
case <OC:retroviridae>
FT   ACT_SITE      6      6       Protease; shared with dimeric partner (By
FT                                similarity).
FT   Condition: D
else
FT   ACT_SITE      6      6       [For protease activity] By similarity.
FT   Condition: D
end case
XX
Chop: Nter=0; Cter=0;
Size: 40-82;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P51518;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.12  2009/02/27
//
AC   PRU00276;
DC   Domain;
TR   PROSITE; PS50215; ADAM_MEPRO; 1; level=0
XX
Names: ADAM type metalloprotease domain
Function: Belongs to peptidase family M12B
XX
CC   -!- SIMILARITY: Contains # peptidase M12B domain.
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50215
FT   DOMAIN     from     to       Peptidase M12B #.
FT   METAL       137    137       Zinc; catalytic (By similarity).
FT   Group: 1; Condition: H
FT   ACT_SITE    138    138       By similarity.
FT   Condition: E
FT   METAL       141    141       Zinc; catalytic (By similarity).
FT   Group: 1; Condition: H
FT   METAL       147    147       Zinc; catalytic (By similarity).
FT   Group: 1; Condition: H
FT   DISULFID    112    192       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    152    176       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    154    159       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 150-252;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P83255;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.8  2009/02/09
//
AC   PRU00277;
DC   Domain;
TR   PROSITE; PS50059; FKBP_PPIASE; 1; level=0
XX
Names: PPIase FKBP-type domain
Function: Peptidyl-prolyl cis-trans isomerase activity (EC 5.2.1.8)
XX
DE   + RecName: EC=5.2.1.8;
XX
CC   -!- SIMILARITY: Contains # PPIase FKBP-type domain.
XX
GO   GO:0016853; F:isomerase activity
XX
KW   Isomerase
KW   Rotamase
XX
FT   From: PS50059
FT   DOMAIN     from     to       PPIase FKBP-type #.
XX
Chop: Nter=0; Cter=0;
Size: 72-130;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q02790;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.8  2009/02/27
//
AC   PRU00278;
DC   Domain;
TR   PROSITE; PS50198; PPIC_PPIASE_2; 1; level=0
XX
Names: PpiC domain
Function: Accelerates protein folding by catalyzing the cis-trans
 isomerization of proline imidic peptide bonds in oligopeptides
XX
CC   -!- SIMILARITY: Contains # PpiC domain.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1; trigger=no
XX
GO   GO:0016853; F:isomerase activity
XX
KW   Isomerase
KW   Rotamase
XX
FT   From: PS50198
FT   DOMAIN     from     to       PpiC #.
XX
Chop: Nter=0; Cter=0;
Size: 72-128;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q13526;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.4  2006/07/05
//
AC   PRU00279;
DC   Domain;
TR   PROSITE; PS50255; CYTOCHROME_B5_2; 1; level=0
XX
Names: Cytochrome b5 family, heme-binding domain
Function: A membrane-bound hemoprotein which acts as an electron carrier for
 several membrane-bound oxygenases
XX
CC   -!- SIMILARITY: Contains # cytochrome b5 heme-binding domain.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1; trigger=no
XX
case <FTGroup:1>
KW   Heme
KW   Iron
KW   Metal-binding
end case
XX
FT   From: PS50255
FT   DOMAIN     from     to       Cytochrome b5 heme-binding #.
FT   METAL        36     36       Iron (heme axial ligand) (By similarity).
FT   Group: 1; Condition: H
FT   METAL        60     60       Iron (heme axial ligand) (By similarity).
FT   Group: 1; Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 76-85;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P00171;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.6  2008/08/14
//
AC   PRU00280;
DC   Domain;
TR   PROSITE; PS50846; HMA_2; 1; level=0
XX
Names: Heavy-metal-associated domain
Function: Found in proteins that transport or detoxify heavy metals. This
 domain contains two conserved cysteines that could be involved in the binding
 of these metals.
XX
CC   -!- SIMILARITY: Contains # HMA domain.
DR   PROSITE; PS01047; HMA_1; 1; trigger=no
XX
case <FTGroup:1>
KW   Metal-binding
end case
XX
FT   From: PS50846
FT   DOMAIN     from     to       HMA #.
FT   METAL        11     11       Potential.
FT   Group: 1; Condition: C
FT   METAL        14     14       Potential.
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 54-75;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: Q47840;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.3  2005/05/19
//
AC   PRU00282;
DC   Domain;
TR   PROSITE; PS50920; SOLCAR; 1; level=0
XX
Names: Solute carrier (Solcar) repeat
Function: Found in substrate carrier proteins involved in energy transfer
XX
CC   -!- SIMILARITY: Contains # Solcar repeat.
XX
GO   GO:0016021; C:integral to membrane
GO   GO:0016020; C:membrane
XX
KW   Membrane
KW   Transmembrane
XX
FT   From: PS50920
FT   REPEAT     from     to       Solcar #.
XX
Chop: Nter=0; Cter=0;
Size: 74-143;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: O43772;
Scope:
 Eukaryota
 Mitochondrion
Comments: None
XX
# Revision 1.3  2006/12/05
//
AC   PRU00283;
DC   Domain;
TR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1; level=0
XX
Names: Kinesin motor domain
Function: A large globular N-terminal domain which is responsible for the
 motor activity of kinesin
XX
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family.
CC   -!- SIMILARITY: Contains # kinesin-motor domain.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1; trigger=no
XX
GO   GO:0005524; F:ATP binding
GO   GO:0003774; F:motor activity
GO   GO:0000166; F:nucleotide binding
XX
KW   ATP-binding
KW   Motor protein
KW   Nucleotide-binding
XX
FT   From: PS50067
FT   DOMAIN     from     to       Kinesin-motor #.
FT   NP_BIND      90     97       ATP (Potential).
FT   Condition: [AG]-x(4)-G-K-[ST]
XX
Chop: Nter=0; Cter=0;
Size: 160-376;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9BVG8;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/06/09
//
AC   PRU00284;
DC   Domain;
TR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1; level=0
XX
Names: Methyl-accepting transducer domain
Function: Respond to changes in the concentration of attractants and
 repellents in the environment, and transduce a signal from the outside to the
 inside of the cell
XX
CC   -!- SIMILARITY: Contains # methyl-accepting transducer domain.
DR   PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1; trigger=no
XX
KW   Transducer
XX
FT   From: PS50111
FT   DOMAIN     from     to       Methyl-accepting transducer #.
XX
Chop: Nter=0; Cter=0;
Size: 221-265;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P02942;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00285;
DC   Domain;
TR   PROSITE; PS01031; HSP20; 1; level=0
XX
Names: Heat shock hsp20 proteins family
Function: Seems to act as chaperones that can protect other proteins against
 heat-induced denaturation and aggregation
XX
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20)
CC       family.
XX
Chop: Nter=0; Cter=0;
Size: 58-158;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q16082;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.4  2006/07/05
//
AC   PRU00286;
DC   Domain;
TR   PROSITE; PS50076; DNAJ_2; 1; level=0
XX
Names: dnaJ domain
Function: Interacts with the chaperone hsp70-like dnaK protein.
XX
CC   -!- SIMILARITY: Contains # J domain.
DR   PROSITE; PS00636; DNAJ_1; 1; trigger=no
FT   From: PS50076
FT   DOMAIN     from     to       J #.
XX
Chop: Nter=0; Cter=0;
Size: 53-88;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Z9E9;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.5  2005/07/06
//
AC   PRU00287;
DC   Domain;
TR   PROSITE; PS50936; ENGC_GTPASE; 1; level=0
XX
Names: EngC GTPase domain
Function: GTPase
XX
CC   -!- SIMILARITY: Contains # engC GTPase domain.
XX
GO   GO:0005525; F:GTP binding
GO   GO:0016787; F:hydrolase activity
GO   GO:0000166; F:nucleotide binding
XX
KW   GTP-binding
KW   Hydrolase
KW   Nucleotide-binding
XX
FT   From: PS50936
FT   DOMAIN     from     to       EngC GTPase #.
FT   NP_BIND      41     44       GTP (By similarity).
FT   NP_BIND      95    103       GTP (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 141-155;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8DVW1;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.4  2010/03/26
//
AC   PRU00288;
DC   Domain;
TR   PROSITE; PS50115; ARFGAP; 1; level=0
XX
Names: ARF GTPase-activating proteins domain
Function: GTPase-activating
XX
CC   -!- SIMILARITY: Contains # Arf-GAP domain.
XX
KW   Zinc-finger
case <Feature:PS50115:16=[CH]> and <Feature:PS50115:19=[CH]> and <Feature:PS50115:36=[CH]> and <Feature:PS50115:39=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50115
FT   DOMAIN     from     to       Arf-GAP #.
case <Feature:PS50115:16=C> and <Feature:PS50115:19=C> and <Feature:PS50115:36=C> and <Feature:PS50115:39=C>
FT   ZN_FING      16     39       C4-type #.
else case <Feature:PS50115:16=[CH]> and <Feature:PS50115:19=[CH]> and <Feature:PS50115:36=[CH]> and <Feature:PS50115:39=[CH]>
FT   ZN_FING      16     39       C4-type #; atypical.
else
FT   ZN_FING      16     39       C4-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 110-144;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8N6T3;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2005/06/28
//
AC   PRU00289;
DC   Domain;
TR   PROSITE; PS50901; FTSK; 1; level=0
XX
Names: FtsK domain
Function: thought to be involved in DNA translocation by coupling ATP
 hydrolysis to movement relative to the long axis of DNA
XX
CC   -!- SIMILARITY: Contains # FtsK domain.
XX
GO   GO:0005524; F:ATP binding
GO   GO:0000166; F:nucleotide binding
XX
KW   ATP-binding
KW   Nucleotide-binding
XX
FT   From: PS50901
FT   DOMAIN     from     to       FtsK #.
FT   NP_BIND      18     25       ATP (Potential).
XX
Chop: Nter=0; Cter=0;
Size: 154-200;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: P46889;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.3  2005/06/09
//
AC   PRU00290;
DC   Domain;
TR   PROSITE; PS50892; V_SNARE; 1; level=0
XX
Names: v-SNARE coiled-coil homology domain
Function: binds t-SNARE
XX
CC   -!- SIMILARITY: Contains # v-SNARE coiled-coil homology domain.
XX
KW   Coiled coil
XX
FT   From: PS50892
FT   DOMAIN     from     to       v-SNARE coiled-coil homology #.
XX
Chop: Nter=0; Cter=0;
Size: 57-70;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P23763;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00291;
DC   Domain;
TR   PROSITE; PS50891; LOB; 1; level=0
XX
Names: LOB domain
Function: Unknown
XX
CC   -!- SIMILARITY: Contains # LOB domain.
FT   From: PS50891
FT   DOMAIN     from     to       LOB #.
XX
Chop: Nter=0; Cter=0;
Size: 101-107;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O64836;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00292;
DC   Domain;
TR   PROSITE; PS50945; I_LWEQ; 1; level=0
XX
Names: I/LWEQ domain
Function: The I/LWEQ domain has been shown to bind to F-actin and to bundle
 actin filaments.
XX
CC   -!- SIMILARITY: Contains # I/LWEQ domain.
FT   From: PS50945
FT   DOMAIN     from     to       I/LWEQ #.
XX
Chop: Nter=0; Cter=0;
Size: 193-199;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9Y490;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00293;
DC   Site;
TR   PROSITE; PS00016; RGD; 1; level=1
XX
Names: Cell attachment sequence
Function: The 'RGD' tripeptide has been shown to play a role in cell adhesion.
XX
GO   GO:0005194; F:cell adhesion molecule activity
GO   GO:0007155; P:cell adhesion
XX
KW   Cell adhesion
XX
FT   From: PS00016
FT   MOTIF      from     to       Cell attachment site (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 3;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P83041;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.3  2005/05/11
//
AC   PRU00294;
DC   Domain;
TR   PROSITE; PS50870; AH; 1; level=1
XX
Names: Arfaptin homology (AH) domain
Function: The AH domain of arfaptin has been shown to dimerize and to bind Arf
 and Rho family GTPases.
XX
CC   -!- SIMILARITY: Contains # AH domain.
FT   From: PS50870
FT   DOMAIN     from     to       AH #.
XX
Chop: Nter=0; Cter=0;
Size: 200-220;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P53367;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00295;
DC   Domain;
TR   PROSITE; PS50189; NTR; 1; level=1
XX
Names: NTR domain
Function: The NTR domain is implicated in inhibition of zinc
 metalloproteinases of the metzincin family.
XX
CC   -!- SIMILARITY: Contains # NTR domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50189
FT   DOMAIN     from     to       NTR #.
FT   DISULFID      1     76       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
case <FTGroup:1>
FT   DISULFID      5     78       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      5    107       By similarity.
FT   Tag: disulf; Condition: C-x*-C
end case
FT   DISULFID     19    134       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 110-200;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P97299;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2009/02/09
//
AC   PRU00296;
DC   Domain;
TR   PROSITE; PS50944; HTH_DTXR; 1; level=0
XX
Names: DtxR-type HTH domain
Function: The dtxR-type HTH domain is a DNA-binding, winged helix-turn-helix
 (wHTH) domain present in metalloregulators of the dtxR/mntR family.
XX
CC   -!- SIMILARITY: Contains # HTH dtxR-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50944
FT   DOMAIN     from     to       HTH dtxR-type #.
XX
Chop: Nter=0; Cter=0;
Size: 60-65;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P0A9F1;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.4  2005/09/14
//
AC   PRU00297;
DC   Domain;
TR   PROSITE; PS50873; PEROXIDASE_4; 1; level=0
XX
Names: Plant heme peroxidase
Function: Removal of H(2)O(2), oxidation of toxic reductants
XX
case <FTGroup:1> and <FTGroup:2> and <FTGroup:3> and <FTGroup:4>
CC   -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC       biosynthesis and degradation of lignin, suberization, auxin
CC       catabolism, response to environmental stresses such as wounding,
CC       pathogen attack and oxidative stress. These functions might be
CC       dependent on each isozyme/isoform in each plant tissue.
CC   -!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per
CC       subunit (By similarity).
CC   -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the peroxidase family. Classical plant
CC       (class III) peroxidase subfamily.
end case
XX
case <Feature:PS50873:168=H>
DR   PROSITE; PS00435; PEROXIDASE_1; 1; trigger=no
end case
case <Feature:PS50873:42=H>
DR   PROSITE; PS00436; PEROXIDASE_2; 1; trigger=no
end case
XX
case <FTGroup:1> and <FTGroup:2> and <FTGroup:3> and <FTGroup:4>
GO   GO:0016491; F:oxidoreductase activity
GO   GO:0004601; F:peroxidase activity
GO   GO:0009055; F:electron carrier activity
GO   GO:0055114; P:oxidation-reduction process
GO   GO:0006979; P:response to oxidative stress
GO   GO:0042744; P:hydrogen peroxide catabolic process
KW   Secreted
KW   Oxidoreductase
KW   Peroxidase
KW   Hydrogen peroxide
end case
case <Feature:PS50873:168=H>
GO   GO:0020037; F:heme binding
GO   GO:0005506; F:iron ion binding
KW   Iron
KW   Heme
end case
case <Feature:PS50873:1=Q>
KW   Pyrrolidone carboxylic acid
end case
case <FTGroup:1> or <FTGroup:2>
GO   GO:0005509; F:calcium ion binding
KW   Calcium
end case
case <Feature:PS50873:168=H> or <FTGroup:1> or <FTGroup:2>
KW   Metal-binding
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50873
FT   METAL        43     43       Calcium #1 (By similarity).
FT   Group: 1; Condition: [DE]
FT   METAL        46     46       Calcium #1; via carbonyl oxygen (By
FT                                similarity).
FT   Group: 1; Condition: [VI]
FT   METAL        48     48       Calcium #1; via carbonyl oxygen (By
FT                                similarity).
FT   Group: 1; Condition: G
FT   METAL        50     50       Calcium #1 (By similarity).
FT   Group: 1; Condition: [DE]
FT   METAL        52     52       Calcium #1 (By similarity).
FT   Group: 1; Condition: [ST]
FT   METAL       169    169       Calcium #2 (By similarity).
FT   Group: 2; Condition: [TS]
FT   METAL       222    222       Calcium #2 (By similarity).
FT   Group: 2; Condition: [DE]
FT   METAL       225    225       Calcium #2 (By similarity).
FT   Group: 2; Condition: [TS]
FT   METAL       230    230       Calcium #2 (By similarity).
FT   Group: 2; Condition: [DE]
FT   SITE         38     38       Transition state stabilizer (By
FT                                similarity).
FT   Group: 3; Condition: R
FT   ACT_SITE     42     42       Proton acceptor (By similarity).
FT   Group: 3; Condition: H
case <FTGroup:4>
FT   BINDING     138    138       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   Condition: P
end case
FT   METAL       168    168       Iron (heme axial ligand) (By similarity).
FT   Group: 3; Condition: H
FT   DISULFID     11     90       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     44     49       By similarity.
FT   Tag: disulf; Group: 4; Condition: C-x*-C
FT   DISULFID     96    298       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    175    207       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   MOD_RES       1      1       Pyrrolidone carboxylic acid (By
FT                                similarity).
FT   Condition: Q
XX
Chop: Nter=0; Cter=0;
Size: 250-384;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q96506;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.25  2010/12/02
//
AC   PRU00298;
DC   Domain;
TR   PROSITE; PS50292; PEROXIDASE_3; 1; level=0
XX
Names: Animal heme peroxidase
Function: Removal of H(2)O(2)
XX
case <FTGroup:1> and <FTGroup:2> and <FTGroup:3>
CC   -!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
CC   -!- COFACTOR: Binds 1 calcium ion per heterodimer (By similarity).
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group covalently
CC       per heterodimer (By similarity).
end case
CC   -!- SIMILARITY: Belongs to the peroxidase family.
XX
case <FTGroup:2>
DR   PROSITE; PS00435; PEROXIDASE_1; 1; trigger=no
DR   PROSITE; PS00436; PEROXIDASE_2; 1; trigger=no
end case
XX
case <FTGroup:1> and <FTGroup:2> and <FTGroup:3>
GO   GO:0016491; F:oxidoreductase activity
GO   GO:0004601; F:peroxidase activity
KW   Oxidoreductase
KW   Peroxidase
end case
case <FTGroup:1>
KW   Iron
KW   Heme
end case
case <FTGroup:3>
KW   Calcium
end case
case <FTGroup:1> or <FTGroup:3>
KW   Metal-binding
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50292
case <Feature:PS50292:4=C> and <Feature:PS50292:111=C>
FT   CHAIN         2    108       <name> light chain.
FT   CHAIN       109   Cter       <name> heavy chain.
** From PMID: 1320128; PMID: 11705390
end case
FT   BINDING      95     95       Heme (covalent) (By similarity).
FT   Group: 1; Condition: D
FT   BINDING     238    238       Heme (covalent) (By similarity).
FT   Group: 1; Condition: E
FT   ACT_SITE     96     96       Proton acceptor (By similarity).
FT   Group: 2; Condition: H
FT   SITE        235    235       Transition state stabilizer (By
FT                                similarity).
FT   Group: 2; Condition: R
FT   METAL        97     97       Calcium (By similarity).
FT   Group: 3; Condition: D
FT   METAL       164    164       Calcium (By similarity).
FT   Group: 3; Condition: [ST]
FT   METAL       166    166       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   Group: 3; Condition: [FY]
FT   METAL       168    168       Calcium (By similarity).
FT   Group: 3; Condition: D
FT   METAL       170    170       Calcium (By similarity).
FT   Group: 3; Condition: [ST]
FT   METAL       332    332       Iron (heme axial ligand) (By similarity).
FT   Condition: H
FT   DISULFID      4     17       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    111    121       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    115    139       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    217    228       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    435    491       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    534    560       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 510-750;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: P11247;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.14  2010/01/12
//
AC   PRU00300;
DC   Domain;
TR   Metamotif; -; PS50021=7,91=PS50021
XX
Names: Actin-binding domain (ABD)
Function: Each single ABD, comprising two CH domains, is able to bind one
 actin monomer in the filament.
XX
CC   -!- SIMILARITY: Contains # actin-binding domain.
XX
DR   PROSITE; PS50021; CH; 2; trigger=yes
DR   PROSITE; PS00019; ACTININ_1; 1-2; trigger=no
DR   PROSITE; PS00020; ACTININ_2; 1-2; trigger=no
XX
GO   GO:0003779; F:actin binding
KW   Actin-binding
XX
FT   From: PS50021=7,91=PS50021
FT   DOMAIN     from     to       Actin-binding #.
XX
Chop: Nter=0; Cter=0;
Size: 225-325;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: O97592;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.9  2009/12/21
//
AC   PRU00302;
DC   Domain;
TR   PROSITE; PS50923; SUSHI; 1; level=0
XX
Names: Sushi domain
Function: involved in many recognition processes, including the binding of
 several complement factors to fragments C3b and C4b.
XX
CC   -!- SIMILARITY: Contains # Sushi (CCP/SCR) domain.
KW   Sushi
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50923
FT   DOMAIN     from     to       Sushi #.
FT   DISULFID      3     46       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     32     59       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 13-77;
Related: None;
Repeats: 1-20;
Topology: Not cytoplasmic;
Example: P20851;
Scope:
 Eukaryota; Metazoa
 Viruses; dsDNA viruses, no RNA stage
Comments: None
XX
# Revision 1.7  2009/02/09
//
AC   PRU00303;
DC   Domain;
c?   <OC:Bacteria> or <OC:Archaea> or <OC:Bacteriophage>
TR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1; level=0
XX
Names: Prokaryotic membrane lipoprotein lipid attachment site
Function: site of signal peptide cleavage and attachment of glyceride-fatty
 acid lipids that anchor proteins in the membrane
XX
DE   + Flags: Precursor;
case not <Triggered>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (Potential).
GO   GO:0005886; C:plasma membrane
end case
XX
case not <Triggered>
KW   Membrane
end case
KW   Palmitate
KW   Signal
KW   Lipoprotein
XX
FT   From: PS51257
FT   SIGNAL        1     34       Potential.
FT   LIPID        35     35       N-palmitoyl cysteine (Potential).
FT   LIPID        35     35       S-diacylglycerol cysteine (Potential).
FT   CHAIN        35   Cter       <name>.
XX
Chop: Nter=0; Cter=0;
Size: 14-35;
Related: ANA00006; ANA00002;
Repeats: 1;
Topology: Membrane;
Example: P23898;
Scope:
 Bacteria
 Archaea
 Bacteriophage
Comments: None
XX
# Revision 1.15  2009/01/26
//
AC   PRU00304;
DC   Domain;
TR   PROSITE; PS50211; DENN; 1; level=0
XX
Names: DENN domain
Function: The function of DENN domain remains to date unclear, although it
 appears to represent a good candidate for a GTP/GDP exchange activity.
XX
CC   -!- SIMILARITY: Contains # DENN domain.
FT   From: PS50211
FT   DOMAIN     from     to       DENN #.
XX
Chop: Nter=0; Cter=0;
Size: 180-230;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: O02626;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2004/05/06
//
AC   PRU00305;
DC   Domain;
TR   PROSITE; PS50946; UDENN; 1; level=0
XX
Names: uDENN domain
Function: It could play a key role in the DENN functions.
XX
CC   -!- SIMILARITY: Contains # uDENN domain.
FT   From: PS50946
FT   DOMAIN     from     to       uDENN #.
XX
Chop: Nter=0; Cter=0;
Size: 90-110;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: O02626;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2004/05/06
//
AC   PRU00306;
DC   Domain;
TR   PROSITE; PS50947; DDENN; 1; level=0
XX
Names: dDENN domain
Function: It could play a key role in the DENN functions.
XX
CC   -!- SIMILARITY: Contains # dDENN domain.
FT   From: PS50947
FT   DOMAIN     from     to       dDENN #.
XX
Chop: Nter=0; Cter=0;
Size: 70-80;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: O02626;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2004/05/06
//
AC   PRU00307;
DC   Domain;
TR   PROSITE; PS50949; HTH_GNTR; 1; level=0
XX
Names: GntR-type HTH domain
Function: The gntR-type HTH domain is a DNA-binding, winged helix-turn-helix
 (wHTH) domain of about 60-70 residues present in transcriptional regulators
 of the gntR family.
XX
CC   -!- SIMILARITY: Contains # HTH gntR-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50949
FT   DOMAIN     from     to       HTH gntR-type #.
FT   DNA_BIND     29     48       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 50-75;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9S470;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.4  2006/09/14
//
AC   PRU00308;
DC   Domain;
TR   PROSITE; PS50921; ANTAR; 1; level=0
XX
Names: ANTAR domain
Function: The ANTAR domain is supposed to be an RNA-binding motif.
XX
CC   -!- SIMILARITY: Contains # ANTAR domain.
XX
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   Transcription
KW   Transcription antitermination
KW   Transcription regulation
XX
FT   From: PS50921
FT   DOMAIN     from     to       ANTAR #.
XX
Chop: Nter=0; Cter=0;
Size: 60-70;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P10932;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.4  2005/02/16
//
AC   PRU00309;
DC   Domain;
TR   PROSITE; PS50950; THAP; 1; level=0
XX
Names: Zinc finger THAP-type
Function: The THAP-type zinc finger is supposed to be a DNA-binding  domain.
XX
CC   -!- SIMILARITY: Contains # THAP-type zinc finger.
XX
GO   GO:0003677; F:DNA binding
XX
KW   Zinc-finger
KW   DNA-binding
case <Feature:PS50950:5=[CH]> and <Feature:PS50950:10=[CH]> and <Feature:PS50950:55=[CH]> and <Feature:PS50950:58=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50950
case <Feature:PS50950:5=C> and <Feature:PS50950:10=C> and <Feature:PS50950:55=C> and <Feature:PS50950:58=H>
FT   ZN_FING       5     58       THAP-type #.
else case <Feature:PS50950:5=[CH]> and <Feature:PS50950:10=[CH]> and <Feature:PS50950:55=[CH]> and <Feature:PS50950:58=[CH]>
FT   ZN_FING       5     58       THAP-type #; atypical.
else
FT   ZN_FING       5     58       THAP-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 70-100;
Related: None;
Repeats: 1-27;
Topology: Cytoplasmic;
Example: Q9NVV9;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.7  2009/02/20
//
AC   PRU00310;
DC   Domain;
TR   PROSITE; PS50951; SARAH; 1; level=0
XX
Names: SARAH domain
Function: The SARAH domain could be a trimerization domain.
XX
CC   -!- SIMILARITY: Contains # SARAH domain.
XX
FT   From: PS50951
FT   DOMAIN     from     to       SARAH #.
XX
Chop: Nter=0; Cter=0;
Size: 45-50;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9H4B6;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/13
//
AC   PRU00311;
DC   Domain;
TR   PROSITE; PS50952; KIX; 1; level=0
XX
Names: KIX domain
Function: The KIX domain appears to be a common docking site on CBP for many
 transcriptional activators.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # KIX domain.
XX
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   Activator
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50952
FT   DOMAIN     from     to       KIX #.
XX
Chop: Nter=0; Cter=0;
Size: 75-85;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: Q92793;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.6  2007/06/21
//
AC   PRU00312;
DC   Domain;
TR   PROSITE; PS50953; KID; 1; level=0
XX
Names: KID domain
Function: Ser-133 phosphorylation of CREB within the KID domain promotes
 target gene activation via complex formation with the KIX domain of the CBP
 and P300 coactivators, whereas concurrent phosphorylation of the CREB KID
 domain at Ser-142 inhibits transcriptional induction.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # KID (kinase-inducible) domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Nucleus
case <Feature:PS50953:33=S> or <Feature:PS50953:42=S>
KW   Phosphoprotein
end case
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50953
FT   DOMAIN     from     to       KID #.
FT   MOD_RES      33     33       Phosphoserine (By similarity).
FT   Condition: S
FT   MOD_RES      42     42       Phosphoserine (By similarity).
FT   Condition: S
XX
Chop: Nter=0; Cter=0;
Size: 55-65;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P16220;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.8  2007/10/13
//
AC   PRU00313;
DC   Domain;
TR   PROSITE; PS50954; LEM; 1; level=0
XX
Names: LEM domain
Function: The LEM domain has been shown to be mediate binding to BAF (barrier-
 to-autointegration factor) and BAF-DNA complexes.
XX
CC   -!- SIMILARITY: Contains # LEM domain.
XX
FT   From: PS50954
FT   DOMAIN     from     to       LEM #.
XX
Chop: Nter=0; Cter=0;
Size: 30-50;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P50402;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00314;
DC   Domain;
TR   PROSITE; PS50955; LEM_LIKE; 1; level=0
XX
Names: LEM-like domain
Function: The LEM-like domain has been shown to bind directly to DNA.
XX
CC   -!- SIMILARITY: Contains # LEM-like domain.
XX
FT   From: PS50955
FT   DOMAIN     from     to       LEM-like #.
XX
Chop: Nter=0; Cter=0;
Size: 40-50;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P42166;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00315;
DC   Domain;
TR   PROSITE; PS50948; PAN; 1; level=0
XX
Names: PAN/Apple domain
Function: The PAN/Apple domain has been shown to bind directly to kininogen,
 factor XIIa, platelets,factor IX and heparin.
XX
case <AnyFeature:PS50948:1={C}> or <AnyFeature:PS50948:78={C}>
CC   -!- SIMILARITY: Contains # PAN domain.
else
CC   -!- SIMILARITY: Contains # apple domain.
XX
DR   PROSITE; PS00495; APPLE; 1; trigger=no
end case
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50948
case <AnyFeature:PS50948:1={C}> or <AnyFeature:PS50948:78={C}>
FT   DOMAIN     from     to       PAN #.
else
FT   DOMAIN     from     to       Apple #.
end case
FT   DISULFID      1     78       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     30     52       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     34     40       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 72-95;
Related: None;
Repeats: 4;
Topology: Not cytoplasmic;
Example: P03951; P14210;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.16  2009/02/09
//
AC   PRU00316;
DC   Domain;
TR   PROSITE; PS50853; FN3; 1; level=0
XX
Names: FN3 domain
Function: The FN3 domain has been shown to be involved in binding substrate.
XX
CC   -!- SIMILARITY: Contains # fibronectin type-III domain.
XX
FT   From: PS50853
FT   DOMAIN     from     to       Fibronectin type-III #.
XX
Chop: Nter=0; Cter=0;
Size: 78-135;
Related: None;
Repeats: 33;
Topology: Not cytoplasmic;
Example: P23352;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.5  2005/05/20
//
AC   PRU00317;
DC   Domain;
TR   PROSITE; PS50302; PUM; 1; level=0
XX
Names: Pumilio repeat
Function: Pumilio repeats have been shown to bind specific RNA
 sequences  mainly  found  in  the 3' UTR of mRNA and repress their translation.
XX
CC   -!- SIMILARITY: Contains # pumilio repeat.
XX
FT   From: PS50302
FT   REPEAT     from     to       Pumilio #.
XX
Chop: Nter=0; Cter=0;
Size: 30-50;
Related: None;
Repeats: 9;
Topology: Not cytoplasmic;
Example: P25822;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2006/04/03
//
AC   PRU00318;
DC   Domain;
TR   PROSITE; PS50303; PUM_HD; 1; level=0
XX
Names: Pumilio homology domain
Function: Pumilio homology domain has been shown to bind specific RNA
 sequences  mainly  found  in  the 3' UTR of mRNA and repress their translation.
XX
CC   -!- SIMILARITY: Contains # PUM-HD domain.
XX
FT   From: PS50303
FT   DOMAIN     from     to       PUM-HD #.
XX
Chop: Nter=0; Cter=0;
Size: 300-450;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P25822;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2006/04/03
//
AC   PRU00319;
DC   Domain;
TR   PROSITE; PS50956; HTH_ASNC_2; 1; level=0
XX
Names: AsnC-type HTH domain
Function: The asnC-type HTH domain is a DNA-binding, helix-turn-helix (HTH)
 domain of about 60 amino acids present in transcription regulators of the
 asnC/lrp family.
XX
CC   -!- SIMILARITY: Contains # HTH asnC-type DNA-binding domain.
XX
DR   PROSITE; PS00519; HTH_ASNC_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50956
FT   DOMAIN     from     to       HTH asnC-type #.
FT   DNA_BIND     20     39       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 40-100;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P0ACJ4;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.8  2006/09/14
//
AC   PRU00320;
DC   Domain;
TR   PROSITE; PS50960; HTH_PSQ; 1; level=0
XX
Names: Psq-type HTH domain
Function: The psq-type HTH domain is a DNA-binding, helix-turn-helix (HTH)
 domain of about 50 amino acids present in eukaryotic proteins of the
 Pipsqueak family.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # HTH psq-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   DNA-binding
KW   Nucleus
XX
FT   From: PS50960
FT   DOMAIN    entry   exit       HTH psq-type #.
FT   DNA_BIND     29     49       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 45-60;
Related: None;
Repeats: 1-4;
Topology: Not cytoplasmic;
Example: P07199;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.10  2008/04/08
//
AC   PRU00321;
DC   Domain;
TR   PROSITE; PS50828; SMR; 1; level=0
XX
Names: Smr domain
Function: It has been proposed that the Smr domain acts as a nicking
 endonuclease.
XX
CC   -!- SIMILARITY: Contains # Smr domain.
FT   From: PS50828
FT   DOMAIN     from     to       Smr #.
XX
Chop: Nter=0; Cter=0;
Size: 70-100;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P76053;
Scope:
 Eukaryota
 Bacteria
 Bacteriophage
Comments: None
XX
# Revision 1.4  2004/05/06
//
AC   PRU00322;
DC   Domain;
TR   PROSITE; PS50199; ZF_RANBP2_2; 1; level=0
XX
Names: Zinc finger RanBP2-type
Function: It has been shown that RanBP2-type zinc fingers bind RanGDP (but not
 RanGTP) and the exportin-1 protein (a receptor of the export pathway).
XX
CC   -!- SIMILARITY: Contains # RanBP2-type zinc finger.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1; trigger=no
KW   Zinc-finger
case <Feature:PS50199:7=[CH]> and <Feature:PS50199:10=[CH]> and <Feature:PS50199:21=[CH]> and <Feature:PS50199:24=[CH]>
KW   Zinc
KW   Metal-binding
end case
FT   From: PS50199
case <Feature:PS50199:7=C> and <Feature:PS50199:10=C> and <Feature:PS50199:21=C> and <Feature:PS50199:24=C>
FT   ZN_FING    from     to       RanBP2-type #.
else case <Feature:PS50199:7=[CH]> and <Feature:PS50199:10=[CH]> and <Feature:PS50199:21=[CH]> and <Feature:PS50199:24=[CH]>
FT   ZN_FING    from     to       RanBP2-type #; atypical.
else
FT   ZN_FING    from     to       RanBP2-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 30-35;
Related: None;
Repeats: 8;
Topology: Cytoplasmic;
Example: P49792;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2005/06/28
//
AC   PRU00323;
DC   Domain;
TR   PROSITE; PS50963; LINK_2; 1; level=0
XX
Names: Link domain
Function: Link domains are hyaluronan(HA)-binding domains found in proteins
 involved in in the assembly of extracellular matrix, cell adhesion, and
 migration.
XX
CC   -!- SIMILARITY: Contains # Link domain.
DR   PROSITE; PS01241; LINK_1; 1; trigger=no
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50963
FT   DOMAIN     from     to       Link #.
FT   DISULFID     23     92       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     47     68       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 80-105;
Related: None;
Repeats: 1-4;
Topology: Not cytoplasmic;
Example: P98066;
Scope:
 Eukaryota; Metazoa; Craniata
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00324;
DC   Domain;
TR   PROSITE; PS50962; IAA_ARF; 1; level=0
XX
Names: Aux/IAA-ARF domain
Function:   This   domain   has   been   shown  to  mediate  both  homo-  and
 heterodimerization between members of ARF and Aux/IAA proteins.
XX
CC   -!- SIMILARITY: Contains # Aux/IAA-ARF domain.
FT   From: PS50962
FT   DOMAIN     from     to       Aux/IAA-ARF #.
XX
Chop: Nter=0; Cter=0;
Size: 80-110;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q8L7G0;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.3  2005/05/23
//
AC   PRU00325;
DC   Domain;
TR   PROSITE; PS50966; ZF_SWIM; 1; level=0
XX
Names: Zinc finger SWIM-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SWIM-type zinc finger.
XX
KW   Zinc-finger
case <Feature:PS50966:16=[CH]> and <Feature:PS50966:18=[CH]> and <Feature:PS50966:27=[CH]> and <Feature:PS50966:29=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50966
case <Feature:PS50966:16=[C]> and <Feature:PS50966:18=[C]> and <Feature:PS50966:27=[C]> and <Feature:PS50966:29=[H]>
FT   ZN_FING    from     to       SWIM-type #.
else case <Feature:PS50966:16=[CH]> and <Feature:PS50966:18=[CH]> and <Feature:PS50966:27=[CH]> and <Feature:PS50966:29=[CH]>
FT   ZN_FING    from     to       SWIM-type #; atypical.
else
FT   ZN_FING    from     to       SWIM-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 25-45;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P33353;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.6  2006/07/17
//
AC   PRU00326;
DC   Domain;
TR   PROSITE; PS50863; B3; 1; level=0
XX
Names: B3 domain
Function: DNA binding domain.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # TF-B3 DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50863
FT   DNA_BIND   from     to       TF-B3 #.
XX
Chop: Nter=0; Cter=0;
Size: 95-110;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q8L7G0;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.5  2007/06/21
//
AC   PRU00327;
DC   Domain;
TR   PROSITE; PS50965; NERD; 1; level=0
XX
Names: NERD domain
Function: The NERD domain is predicted to be connected to DNA processing and
 genomic context and distant homology analysis suggest a nuclease function.
XX
CC   -!- SIMILARITY: Contains # NERD domain.
FT   From: PS50965
FT   DOMAIN     from     to       NERD #.
XX
Chop: Nter=0; Cter=0;
Size: 108-128;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q8KYT4;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.3  2005/09/14
//
AC   PRU00328;
DC   Domain;
TR   PROSITE; PS50967; HRDC; 1; level=0
XX
Names: HRDC domain
Function: The HRDC domain is involved in the binding of DNA to specific DNA
 structures (e.g. long-forked duplexes and Holliday junctions) that are formed
 during replication, recombination or transcription.
XX
CC   -!- SIMILARITY: Contains # HRDC domain.
FT   From: PS50967
FT   DOMAIN     from     to       HRDC #.
XX
Chop: Nter=0; Cter=0;
Size: 70-87;
Related: None;
Repeats: 1-3;
Topology: Cytoplasmic;
Example: Q14191;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00330;
DC   Domain;
TR   PROSITE; PS50069; CULLIN_2; 1; level=0
XX
Names: Cullin
Function: Undefined
XX
CC   -!- SIMILARITY: Belongs to the cullin family.
DR   PROSITE; PS01256; CULLIN_1; 1; trigger=no
XX
Chop: Nter=0; Cter=0;
Size: 150-250;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q13616;
Scope:
 Eukaryota
Comments: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex
XX
# Revision 1.2  2004/05/06
//
AC   PRU00331;
DC   Domain;
TR   PROSITE; PS50957; JOSEPHIN; 1; level=0
XX
Names: Josephin domain
Function: The Josephin domain is believed to be a mainly alpha helical
 cysteine-protease domain predicted to be active against ubiquitin chains or
 related substrates.
XX
CC   -!- SIMILARITY: Contains # Josephin domain.
case <FTGroup:1>
GO   GO:0016787; F:hydrolase activity
KW   Hydrolase
end case
FT   From: PS50957
FT   DOMAIN     from     to       Josephin #.
FT   ACT_SITE     14     14       Potential.
FT   Group: 1; Condition: C
FT   ACT_SITE    117    117       Potential.
FT   Group: 1; Condition: H
FT   ACT_SITE    132    132       Potential.
FT   Group: 1; Condition: [DN]
XX
Chop: Nter=0; Cter=0;
Size: 165-195;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q15040;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/23
//
AC   PRU00332;
DC   Domain;
TR   PROSITE; PS50961; HTH_LA; 1; level=0
XX
Names: La-type HTH domain
Function: The La-type HTH domain is an RNA-binding, winged helix-turn-helix
 (wHTH) domain of about 90 residues present in La proteins and other
 eukaryotic RNA-binding proteins.
XX
CC   -!- SIMILARITY: Contains # HTH La-type RNA-binding domain.
XX
GO   GO:0003723; F:RNA binding
XX
KW   RNA-binding
XX
FT   From: PS50961
FT   DOMAIN     from     to       HTH La-type RNA-binding #.
XX
Chop: Nter=0; Cter=0;
Size: 80-110;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P05455;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/06/22
//
AC   PRU00333;
DC   Domain;
TR   PROSITE; PS50970; HCY; 1; level=0
XX
Names: Homocysteine-binding domain
Function: The homocysteine- (Hcy-)binding domain utilizes a Zn(Cys)3 cluster
 to bind and activate Hcy.
XX
case <FTGroup:1>
CC   -!- COFACTOR: Zinc (Potential).
end case
CC   -!- SIMILARITY: Contains # Hcy-binding domain.
case <FTGroup:1>
GO   GO:0016740; F:transferase activity
GO   GO:0008168; F:methyltransferase activity
KW   Zinc
KW   Metal-binding
KW   Transferase
KW   Methyltransferase
end case
FT   From: PS50970
FT   DOMAIN     from     to       Hcy-binding #.
FT   METAL       215    215       Zinc (Potential).
FT   Group: 1; Condition: C
FT   METAL       281    281       Zinc (Potential).
FT   Group: 1; Condition: C
FT   METAL       282    282       Zinc (Potential).
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 295-330;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9SDL7;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.6  2005/05/23
//
AC   PRU00334;
DC   Domain;
TR   PROSITE; PS50972; PTERIN_BINDING; 1; level=0
XX
Names: Pterin-binding domain
Function: The pterin-binding domain is folded into a (beta/alpha)8 barrel
 which forms a cup for pterin binding.
XX
CC   -!- SIMILARITY: Contains # pterin-binding domain.
FT   From: PS50972
FT   DOMAIN     from     to       Pterin-binding #.
XX
Chop: Nter=0; Cter=0;
Size: 240-320;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P0AC13;
Scope:
 Eukaryota
 Archaea
 Bacteria
Comments: None
XX
# Revision 1.4  2005/11/09
//
AC   PRU00335;
DC   Domain;
TR   PROSITE; PS50977; HTH_TETR_2; 1; level=0
XX
Names: TetR-type HTH domain
Function: The tetR-type HTH domain is a DNA-binding, helix-turn-helix (HTH)
 domain of about 60 residues present in the tetR family of prokaryotic
 transcription regulators.
XX
CC   -!- SIMILARITY: Contains # HTH tetR-type DNA-binding domain.
XX
DR   PROSITE; PS01081; HTH_TETR_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50977
FT   DOMAIN     from     to       HTH tetR-type #.
FT   DNA_BIND     24     43       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 54-67;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: P0ACT4;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.7  2006/09/14
//
AC   PRU00336;
DC   Domain;
TR   PROSITE; PS50969; FCP1; 1; level=0
XX
Names: FCP1 homology domain
Function: The FCP1 homology domain contains a DxDx(T/v) motif preceded by four
 hydrophobic residues characteristic of a large family of metal-dependant
 phosphohydrolases and phosphotransferases.
XX
CC   -!- SIMILARITY: Contains # FCP1 homology domain.
case <Feature:PS50969:11=[D]> and <Feature:PS50969:13=[D]>
GO   GO:0016787; F:hydrolase activity
KW   Hydrolase
end case
FT   From: PS50969
FT   DOMAIN     from     to       FCP1 homology #.
XX
Chop: Nter=0; Cter=0;
Size: 150-200;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q03254;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00337;
DC   Domain;
TR   PROSITE; PS50978; NEAT; 1; level=0
XX
Names: NEAT domain
Function: Given its predicted extracellular location and its close association
 with the components of an iron transport system, one possible function of the
 NEAT domain is to be a receptor of the siderophore-iron complex.
XX
CC   -!- SIMILARITY: Contains # NEAT domain.
FT   From: PS50978
FT   DOMAIN     from     to       NEAT #.
XX
Chop: Nter=0; Cter=0;
Size: 115-135;
Related: None;
Repeats: 1-7;
Topology: Undefined;
Example: Q99TD3;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2004/05/06
//
AC   PRU00338;
DC   Domain;
TR   PROSITE; PS50982; MBD; 1; level=0
XX
Names: Methyl-CpG-binding domain (MBD)
Function: Some MBDs have been shown to mediate binding to DNA and others
 protein-protein interactions.
XX
CC   -!- SIMILARITY: Contains # MBD (methyl-CpG-binding) domain.
FT   From: PS50982
FT   DOMAIN     from     to       MBD #.
XX
Chop: Nter=0; Cter=0;
Size: 65-80;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q15047;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/05/13
//
AC   PRU00339;
DC   Domain;
TR   PROSITE; PS50005; TPR; 1; level=0
XX
Names: TPR repeat
Function: TPR repeats mediate protein-protein interactions and the assembly of
 multiprotein complexes.
XX
CC   -!- SIMILARITY: Contains # TPR repeat.
XX
DR   PROSITE; PS50293; TPR_REGION; 1; trigger=no
XX
KW   TPR repeat
XX
FT   From: PS50005
FT   REPEAT     from     to       TPR #.
XX
Chop: Nter=0; Cter=0;
Size: 30-40;
Related: RRU00002!!;
Repeats: 1-12;
Topology: Undefined;
Example: O15294;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Bacteriophage
Comments: None
XX
# Revision 1.7  2009/12/09
//
AC   PRU00340;
DC   Domain;
TR   PROSITE; PS50987; HTH_ARSR_2; 1; level=0
XX
Names: ArsR-type HTH domain
Function: The arsR-type HTH domain is a DNA-binding, winged helix-turn-helix
 (wHTH) domain present in transcription regulators of the arsR/smtB family,
 involved in stress-response to heavy metal ions. In this domain two distinct
 sites for metal-binding have been identified, one in helix alpha 3 and
 another in helix alpha 5, and other sites occur.
XX
CC   -!- SIMILARITY: Contains # HTH arsR-type DNA-binding domain.
XX
DR   PROSITE; PS00846; HTH_ARSR_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
case <FTGroup:1>
GO   GO:0046872; F:metal ion binding
end case
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
case <FTGroup:1> or <FTGroup:2>
KW   Metal-binding
end case
case <FTGroup:1>
KW   Metal-thiolate cluster
end case
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50987
FT   DOMAIN     from     to       HTH arsR-type #.
FT   DNA_BIND     35     58       H-T-H motif (By similarity).
FT   METAL        34     34       Potential.
FT   Group: 1; Condition: C
FT   METAL        36     36       Potential.
FT   Group: 1; Condition: C
FT   METAL        77     77       Potential.
FT   Group: 2; Condition: D
FT   METAL        79     79       Potential.
FT   Group: 2; Condition: H
FT   METAL        90     90       Potential.
FT   Group: 2; Condition: H
FT   METAL        93     93       Potential.
FT   Group: 2; Condition: [EH]
XX
Chop: Nter=0; Cter=0;
Size: 68-110;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P30340;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.4  2006/09/14
//
AC   PRU00341;
DC   Domain;
TR   PROSITE; PS50986; MANSC; 1; level=0
XX
Names: MANSC domain
Function: It has been proposed that the MANSC domain in HAI-1 might function
 through binding with hepatocyte growth factor activator and matriptase.
XX
CC   -!- SIMILARITY: Contains # MANSC domain.
FT   From: PS50986
FT   DOMAIN     from     to       MANSC #.
XX
Chop: Nter=0; Cter=0;
Size: 80-90;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9H8J5;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2005/05/23
//
AC   PRU00342;
DC   Domain;
TR   PROSITE; PS50984; TRUD; 1; level=0
XX
Names: TRUD domain
Function: The TRUD domain is likely to be involved in substrate recognition
 and may represent a RNA binding module.
XX
CC   -!- SIMILARITY: Contains # TRUD domain.
FT   From: PS50984
FT   DOMAIN     from     to       TRUD #.
XX
Chop: Nter=0; Cter=0;
Size: 120-250;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q57261;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2004/05/24
//
AC   PRU00343;
DC   Domain;
TR   PROSITE; PS50988; TROVE; 1; level=0
XX
Names: TROVE domain
Function: The TROVE domain may be involved in binding the RNA components of
 the three RNPs, which are telomerase RNA, Y RNA and vault RNA.
XX
CC   -!- SIMILARITY: Contains # TROVE domain.
GO   GO:0030529; C:ribonucleoprotein complex
KW   Ribonucleoprotein
FT   From: PS50988
FT   DOMAIN     from     to       TROVE #.
XX
Chop: Nter=0; Cter=0;
Size: 330-490;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P10155;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.1  2004/05/24
//
AC   PRU00344;
DC   Domain;
TR   PROSITE; PS50983; FE_B12_PBP; 1; level=0
XX
Names: Iron siderophore/cobalamin periplasmic-binding domain
Function: The iron siderophore/cobalamin periplasmic-binding domain delivers
 the ligand to the extracellular gate of the transmembrane domains.
XX
CC   -!- SIMILARITY: Contains # Fe/B12 periplasmic-binding domain.
XX
GO   GO:0006810; P:transport
case <AnyFeature:PS51257>
GO   GO:0016020; C:membrane
end case
KW   Transport
KW   Signal
case <AnyFeature:PS51257>
KW   Membrane
KW   Lipoprotein
else
KW   Periplasm
end case
XX
FT   From: PS50983
FT   DOMAIN     from     to       Fe/B12 periplasmic-binding #.
XX
Chop: Nter=0; Cter=0;
Size: 240-285;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P37028; P11460;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.5  2008/10/02
//
AC   PRU00345;
DC   Domain;
TR   PROSITE; PS50995; HTH_MARR_2; 1; level=0
XX
Names: MarR-type HTH domain
Function:  The  marR-type HTH domain is a DNA-binding, winged helix-turn-helix
 (wHTH) domain of about 135 amino acids present in transcription regulators of
 the marR/slyA family, involved in the development of antibiotic resistance.
XX
CC   -!- SIMILARITY: Contains # HTH marR-type DNA-binding domain.
XX
DR   PROSITE; PS01117; HTH_MARR_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50995
FT   DOMAIN     from     to       HTH marR-type #.
FT   DNA_BIND     47     70       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 120-160;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q93CC3;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.5  2006/09/14
//
AC   PRU00346;
DC   Domain;
TR   PROSITE; PS50974; ADOMET_ACTIVATION; 1; level=0
XX
Names: AdoMet activation domain
Function: The AdoMet domain is found in prokaryotic and eukaryotic methione
 synthase (MetH). It binds S-adenosylmethionine and is required for reductive
 activation.
XX
CC   -!- SIMILARITY: Contains # AdoMet activation domain.
GO   GO:0016740; F:transferase activity
KW   Transferase
KW   Methyltransferase
FT   From: PS50974
FT   DOMAIN     from     to       AdoMet activation #.
XX
Chop: Nter=0; Cter=0;
Size: 295-350;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P13009;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2004/06/08
//
AC   PRU00347;
DC   Domain;
TR   PROSITE; PS50856; AMOP; 1; level=0
XX
Names: AMOP domain
Function: The presence of the AMOP domain in cell adhesion molecules could be
 indicative of a role for this domain in adhesion.
XX
CC   -!- SIMILARITY: Contains # AMOP domain.
FT   From: PS50856
FT   DOMAIN     from     to       AMOP #.
XX
Chop: Nter=0; Cter=0;
Size: 155-185;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q20762;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2004/06/08
//
AC   PRU00348;
DC   Domain;
TR   PROSITE; PS50993; NIDOGEN_G2; 1; level=0
XX
Names: Nidogen G2 beta-barrel domain
Function: The nidogen G2 beta-barrel domain contains a large surface patch
 that is involved in the binding of perlecan, and possibly also of collagen
 IV.
XX
CC   -!- SIMILARITY: Contains # nidogen G2 beta-barrel domain.
GO   GO:0005578; C:extracellular matrix
GO   GO:0005604; C:basement membrane
KW   Extracellular matrix
KW   Basement membrane
FT   From: PS50993
FT   DOMAIN     from     to       Nidogen G2 beta-barrel #.
XX
Chop: Nter=0; Cter=0;
Size: 230-240;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: O88322;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2005/05/25
//
AC   PRU00349;
DC   Domain;
TR   PROSITE; PS51000; HTH_DEOR_2; 1; level=0
XX
Names: DeoR-type HTH domain
Function: The deoR-type HTH domain is a DNA-binding, helix-turn-helix (HTH)
 domain of about 50-60 amino acids present in transcription regulators of the
 deoR family, involved in sugar catabolism.
XX
CC   -!- SIMILARITY: Contains # HTH deoR-type DNA-binding domain.
XX
DR   PROSITE; PS00894; HTH_DEOR_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51000
FT   DOMAIN     from     to       HTH deoR-type #.
FT   DNA_BIND     18     37       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 45-70;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P0ACK5;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.6  2006/09/14
//
AC   PRU00350;
DC   Domain;
TR   PROSITE; PS50958; SMB_2; 1; level=0
XX
Names: Somatomedin B (SMB) domain
Function: The SMB domain of vitronectin has been demonstrated to interact with
 both the urokinase receptor and the plasminogen activator inhibitor-1 (PAI-1)
 and the conserved cysteines of the NPP1 somatomedin B-like domain have been
 shown to mediate homodimerization.
XX
CC   -!- SIMILARITY: Contains # SMB (somatomedin B) domain.
XX
DR   PROSITE; PS00524; SMB_1; 1; trigger=no
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50958
FT   DOMAIN     from     to       SMB #.
FT   DISULFID      5      9       Alternate (By similarity).
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      5     21       Alternate (By similarity).
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      9     39       Alternate (By similarity).
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     19     21       Alternate (By similarity).
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     19     32       Alternate (By similarity).
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     25     31       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     32     39       Alternate (By similarity).
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 35-55;
Related: None;
Repeats: 2;
Topology: Not cytoplasmic;
Example: Q9GZM7;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.6  2009/02/09
//
AC   PRU00351;
DC   Domain;
TR   PROSITE; PS51013; PANNEXIN; 1; level=0
XX
Names: Pannexin family
Function: The pannexin family combines invertebrate gap junction proteins
 (innexins) and their vertebrate and viral homologs.
XX
CC   -!- SIMILARITY: Belongs to the pannexin family.
XX
DR   General; Transmembrane; -; 4; trigger=yes
XX
GO   GO:0005921; C:gap junction
GO   GO:0016020; C:membrane
GO   GO:0016021; C:integral to membrane
XX
KW   Gap junction
KW   Membrane
KW   Transmembrane
XX
Chop: Nter=0; Cter=0;
Size: 340-405;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q96RD7;
Scope:
 Eukaryota; Metazoa
 Viruses; Polydnaviridae
Comments: None
XX
# Revision 1.5  2006/10/16
//
AC   PRU00352;
DC   Domain;
TR   PROSITE; PS51004; SEMA; 1; level=0
XX
Names: Sema domain
Function: The 500 amino acid Sema domain is a receptor recognition and binding
 module.
XX
CC   -!- SIMILARITY: Contains # Sema domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS51004
FT   DOMAIN     from     to       Sema #.
FT   DISULFID     74     85       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID    103    112       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID    234    344       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID    258    304       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 400-520;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9H2E6;
Scope:
 Eukaryota; Metazoa
 Viruses
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00353;
DC   Domain;
TR   PROSITE; PS51005; NAC; 1; level=0
XX
Names: NAC domain
Function: The NAC domain has been shown to be a DNA-binding domain (DBD) and a
 dimerization domain.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- DOMAIN: The NAC domain includes a DNA binding domain and a
CC       dimerization domain.
CC   -!- SIMILARITY: Contains # NAC domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51005
FT   DOMAIN     from     to       NAC #.
FT   DNA_BIND    102   to+6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: 145-175;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: Q9ZNU2;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.5  2007/06/07
//
AC   PRU00354;
DC   Domain;
TR   PROSITE; PS51006; SPERMIDINE_SYNTHASE_2; 1; level=0
XX
Names: Spermidine/spermine synthases family
Function: Members of the spermidine/spermine synthases family are polyamine
 biosynthetic enzymes.
XX
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
DR   PROSITE; PS01330; SPERMIDINE_SYNTHASE_1; 1; trigger=no
XX
GO   GO:0006596; P:polyamine biosynthesis
GO   GO:0016740; F:transferase activity
XX
KW   Polyamine biosynthesis
KW   Transferase
XX
Chop: Nter=0; Cter=0;
Size: 240-305;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P70998;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2005/05/25
//
AC   PRU00355;
DC   Domain;
TR   PROSITE; PS51011; ARID; 1; level=0
XX
Names: ARID domain
Function: The AT-rich interaction domain (ARID) is an ~100-amino acid DNA-
 binding module found in a large number of eukaryotic transcription factors
 that regulate cell proliferation, differentiation and development.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # ARID domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
FT   From: PS51011
FT   DOMAIN     from     to       ARID #.
XX
Chop: Nter=0; Cter=0;
Size: 88-95;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q24573;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2007/06/21
//
AC   PRU00356;
DC   Domain;
TR   PROSITE; PS51014; COBK_CBIJ; 1; level=0
XX
Names: Precorrin-6x reductase domain
Function: The precorrin-6x reductase domain catalyzes the NADPH-dependent
 reduction of precorrin-6x to a dihydro derivative named precorrin-6y.
XX
CC   -!- SIMILARITY: Belongs to the precorrin-6x reductase family.
XX
GO   GO:0009236; P:vitamin B12 biosynthesis
GO   GO:0016491; F:oxidoreductase activity
KW   Cobalamin biosynthesis
KW   NADP
KW   Oxidoreductase
XX
Chop: Nter=0; Cter=0;
Size: 240-260;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q10680; Q57972;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2004/09/29
//
AC   PRU00357;
DC   Domain;
TR   PROSITE; PS51017; CCT; 1; level=0
XX
Names: CCT domain
Function: The CCT domain is a plant module that has been shown to be involved
 in nuclear localization and probably also has a role in protein-protein
 interaction.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # CCT domain.
XX
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
XX
FT   From: PS51017
FT   DOMAIN     from     to       CCT #.
XX
Chop: Nter=0; Cter=0;
Size: 40-45;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9LKL2;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.4  2007/06/21
//
AC   PRU00358;
DC   Domain;
TR   PROSITE; PS51015; YDG; 1; level=0
XX
Names: MyTH4 domain
Function: The YDG domain is necessary to direct to the chromatin a number of
 heterogeneous proteins with associated enzymatic activities.
XX
case <OC:Eukaryota>
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
end case
CC   -!- SIMILARITY: Contains # YDG domain.
XX
case <OC:Eukaryota>
GO   GO:0005634; C:nucleus
end case
XX
case <OC:Eukaryota>
KW   Nucleus
end case
XX
FT   From: PS51015
FT   DOMAIN     from     to       YDG #.
XX
Chop: Nter=0; Cter=0;
Size: 135-155;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9FF80;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.4  2008/04/01
//
AC   PRU00359;
DC   Domain;
TR   PROSITE; PS51016; MYTH4; 1; level=0
XX
Names: MyTH4 domain
Function: The function of the MyTH4 domain is presently unknown, although its
 presence in several different putative motor proteins raises the possibility
 that different motor proteins might share similar mechanisms for targeting or
 regulation.
XX
CC   -!- SIMILARITY: Contains # MyTH4 domain.
FT   From: PS51016
FT   DOMAIN     from     to       MyTH4 #.
XX
Chop: Nter=0; Cter=0;
Size: 140-240;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: Q9W5D0;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2005/05/26
//
AC   PRU00361;
DC   Domain;
TR   PROSITE; PS51021; BAR; 1; level=0
XX
Names: BAR domain
Function: BAR domain containing proteins are a unique class of adaptor
 proteins characterized by a common N-terminal fold termed the BAR domain.
XX
CC   -!- SIMILARITY: Contains 1 BAR domain.
KW   Coiled coil
FT   From: PS51021
FT   DOMAIN     from     to       BAR.
XX
Chop: Nter=0; Cter=0;
Size: 222;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P49418;
Scope:
 Eukaryota
Scope:
 Bacteria
 Archaea
Comments: Recent papers, based  on  sequence  and  structural  similarities  have shown that a conserved region  in  more  divergent  families, like oligophrenin, centaurin beta, sorting  nexin, ICA69, pick1 or arfaptins, is related to the BAR domain. These  families  are  however  too  divergent to be detected by the profile.
XX
# Revision 1.4  2006/07/05
//
AC   PRU00362;
DC   Domain;
TR   PROSITE; PS50990; PEPTIDASE_C39; 1; level=0
XX
Names: Peptidase family C39 domain
Function: This domain is a thiol peptidase found in ABC transporters, and
 belongs to the C39 peptidase family.
XX
case (<Feature:PS50990:7=C> and <Feature:PS50990:81=H>)
DE   + RecName: EC=3.4.22.-;
end case
CC   -!- SIMILARITY: Contains # peptidase C39 domain.
XX
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1; trigger=no
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1; trigger=yes
DR   PROSITE; PS50990; PEPTIDASE_C39; 1; trigger=no
DR   PROSITE; PS50929; ABC_TM1F; 1; trigger=no
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Transport
end case
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
KW   Membrane
KW   Cell inner membrane
end case
case <OC:Bacteria> or <OC:Archaea>
KW   Transmembrane
KW   ATP-binding
KW   Nucleotide-binding
end case
case (<Feature:PS50990:7=C> and <Feature:PS50990:81=H>)
KW   Thiol protease
KW   Hydrolase
KW   Protease
end case
FT   From: PS00017
FT   NP_BIND    from     to       ATP # (By similarity).
FT   From: PS50990
FT   DOMAIN     from     to       Peptidase C39 #.
case <Feature:PS50990:7=C>
FT   ACT_SITE      7      7       By similarity.
else case <Feature:PS50990:81=H>
FT   ACT_SITE     81     81       By similarity.
end case
XX
Chop: Nter=0; Cter=0;
Size: 121;
Related: PRU01700;
Repeats: 1;
Topology: Undefined;
Example: P08716;
Scope:
 Bacteria
 Archaea
Comments: A number of the proteins are classified as non-peptidase homologues as they either have been found experimentally  to be  without  peptidase activity,
 or to lack amino acid residues that are believed to be essential for the catalytic
 activity.
XX
# Revision 1.15  2009/02/27
//
AC   PRU00363;
DC   Domain;
TR   PROSITE; PS51019; REELIN; 1; level=0
XX
Names: Reelin domain
Function: The function of the reelin domain is not yet known.
XX
CC   -!- SIMILARITY: Contains # reelin domain.
GO   GO:0005578; C:extracellular matrix
KW   Extracellular matrix
FT   From: PS51019
FT   DOMAIN     from     to       Reelin #.
XX
Chop: Nter=0; Cter=0;
Size: 160-170;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9HCB6;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2004/10/11
//
AC   PRU00364;
DC   Domain;
TR   PROSITE; PS51020; SPONDIN; 1; level=0
XX
Names: Spondin domain
Function: The function of the spondin domain is not known but it might
 interact with other factors.
XX
CC   -!- SIMILARITY: Contains # spondin domain.
GO   GO:0005578; C:extracellular matrix
KW   Extracellular matrix
FT   From: PS51020
FT   DOMAIN     from     to       Spondin #.
XX
Chop: Nter=0; Cter=0;
Size: 190-200;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9HCB6;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2004/10/21
//
AC   PRU00365;
DC   Domain;
TR   PROSITE; PS51022; L27; 1; level=0
XX
Names: L27 domain
Function: The L27 domain is a specific protein-protein interaction module
 capable of forming heteromeric complexes that can integrate multiple scaffold
 proteins into supramolecular assemblies required for establishment and
 maintenance of cell polarity.
XX
CC   -!- SIMILARITY: Contains # L27 domain.
FT   From: PS51022
FT   DOMAIN     from     to       L27 #.
XX
Chop: Nter=0; Cter=0;
Size: 45-70;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: Q9NUP9;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2005/05/26
//
AC   PRU00366;
DC   Domain;
TR   PROSITE; PS51032; AP2_ERF; 1; level=0
XX
Names: AP2/ERF DNA-binding domain
Function: AP2/ERF is a plant DNA binding domain.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Contains # AP2/ERF DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51032
FT   DNA_BIND   from     to       AP2/ERF #.
XX
Chop: Nter=0; Cter=0;
Size: 63-67;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: O82132;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.7  2007/06/07
//
AC   PRU00367;
DC   Domain;
TR   PROSITE; PS51024; ZF_FCS; 1; level=0
XX
Names: Zinc finger FCS-type
Function: This domain can bind RNA in a non-sequence-specific manner.
XX
CC   -!- SIMILARITY: Contains # FCS-type zinc finger.
XX
KW   Zinc-finger
case <Feature:PS51024:10=[CH]> and <Feature:PS51024:13=[CH]> and <Feature:PS51024:30=[CH]> and <Feature:PS51024:34=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS51024
case <Feature:PS51024:10=[C]> and <Feature:PS51024:13=[C]> and <Feature:PS51024:30=[C]> and <Feature:PS51024:34=[C]>
FT   ZN_FING    from     to       FCS-type #.
else case <Feature:PS51024:10=[CH]> and <Feature:PS51024:13=[CH]> and <Feature:PS51024:30=[CH]> and <Feature:PS51024:34=[CH]>
FT   ZN_FING    from     to       FCS-type #; atypical.
else
FT   ZN_FING    from     to       FCS-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 30-50;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P39769;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2006/07/17
//
AC   PRU00368;
DC   Domain;
TR   PROSITE; PS50871; C1Q; 1; level=0
XX
Names: C1q domain
Function: The C-terminal globular domain of the C1q subcomponents and collagen
 types VIII and X is important both for the correct folding and alignment of
 the triple helix and for protein-protein recognition events. For collagen
 type X it has been suggested that the domain is important for initiation and
 maintenance of the correct assembly of the protein.
XX
CC   -!- SIMILARITY: Contains # C1q domain.
FT   From: PS50871
FT   DOMAIN     from     to       C1q #.
XX
Chop: Nter=0; Cter=0;
Size: 125-155;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P02745;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2004/11/23
//
AC   PRU00369;
DC   Domain;
TR   PROSITE; PS51035; BAG; 1; level=0
XX
Names: BAG domain
Function: BAG domain can interact with Hsc70/Hsp70 and can modulate either positively or negatively these chaperone proteins.
XX
CC   -!- SIMILARITY: Contains # BAG domain.
XX
DR   PROSITE; PS51035; BAG; 1; trigger=no
XX
FT   From: PS51035
FT   DOMAIN     from     to       BAG #.
XX
Chop: Nter=0; Cter=0;
Size: 74-95;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: O95816;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2010/03/05
//
AC   PRU00370;
DC   Domain;
TR   PROSITE; PS51038; BAH; 1; level=0
XX
Names: BAH domain
Function: The BAH domain appears to act as a protein-protein interaction
 module specialized in gene silencing.
XX
CC   -!- SIMILARITY: Contains # BAH domain.
XX
DR   PROSITE; PS51038; BAH; 1; trigger=no
XX
FT   From: PS51038
FT   DOMAIN     from     to       BAH #.
XX
Chop: Nter=0; Cter=0;
Size: 119;
Related: none;
Repeats: 1-2;
Topology: Undefined;
Example: P53236;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/26
//
AC   PRU00371;
DC   Domain;
TR   PROSITE; PS51031; BESS; 1; level=0
XX
Names: BESS domain
Function: The BESS domain directs a variety of protein-protein interactions,
 including interactions with itself, with Dorsal, and with a TBP-associated
 factor.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Contains # BESS domain.
GO   GO:0005634; C:nucleus
KW   Nucleus
FT   From: PS51031
FT   DOMAIN     from     to       BESS #.
XX
Chop: Nter=0; Cter=0;
Size: 35-45;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P05552;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.5  2007/06/07
//
AC   PRU00372;
DC   Domain;
TR   PROSITE; PS51029; MADF; 1; level=0
XX
Names: MADF domain
Function: The myb/SANT-like domain in Adf-1 (MADF) is a ~80-amino-acid module
 that directs sequence specific DNA binding to a site consisting of multiple
 trinucleotide repeats.
XX
case not <OC:Viruses>
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
end case
CC   -!- SIMILARITY: Contains # MADF DNA-binding domain.
GO   GO:0003677; F:DNA binding
case not <OC:Viruses>
GO   GO:0005634; C:nucleus
end case
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
KW   DNA-binding
case not <OC:Viruses>
KW   Nucleus
end case
KW   Transcription
KW   Transcription regulation
FT   From: PS51029
FT   DNA_BIND   from     to       MADF #.
XX
Chop: Nter=0; Cter=0;
Size: 75-85;
Related: None;
Repeats: 1-3;
Topology: Not cytoplasmic;
Example: P05552;
Scope:
 Eukaryota; Metazoa
 Viruses
Comments: None
XX
# Revision 1.8  2007/06/07
//
AC   PRU00373;
DC   Domain;
TR   PROSITE; PS50909; GAT; 1; level=0
XX
Names: GAT domain
Function: The GAT domain of GGAs serves as a molecular anchor of GGA to trans-
 Golgi network (TGN) membranes via its interaction with the GTP-bound form of
 a member of the ARF family of small GTPases and can bind specifically to the
 Rab GTPase effector rabaptin5 and to ubiquitin.
XX
CC   -!- SIMILARITY: Contains # GAT domain.
GO   GO:0016020; C:membrane
GO   GO:0015031; P:protein transport
GO   GO:0006810; P:transport
KW   Membrane
KW   Protein transport
KW   Transport
FT   From: PS50909
FT   DOMAIN    entry   exit       GAT #.
XX
Chop: Nter=0; Cter=0;
Size: 85-130;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9UJY5; O60784;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2004/11/23
//
AC   PRU00374;
DC   Domain;
TR   PROSITE; PS51042; CUT; 1; level=0
XX
Names: CUT domain
Function: The CUT domain is a DNA-binding motif which can bind independently or in cooperation  with  the  homeodomain, often found downstream of the CUT domain.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Contains # CUT DNA-binding domain.
XX
DR   PROSITE; PS51042; CUT; 1; trigger=no
XX
GO   GO:0005634; C:nucleus
XX
KW   DNA-binding
KW   Nucleus
XX
FT   From: PS51042
FT   DNA_BIND   from     to       CUT #.
XX
Chop: Nter=0; Cter=0;
Size: 88;
Related: none;
Repeats: 1-3;
Topology: Undefined;
Example: P39880;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.10  2008/04/08
//
AC   PRU00375;
DC   Domain;
TR   PROSITE; PS51034; ZP_2; 1; level=0
XX
Names: ZP domain
Function: The zona pellucida (ZP) domain is a protein polymerization module of
 ~260 amino acid module, which is found at the C-terminus of many secreted
 eukaryotic glycoproteins that play fundamental roles in development, hearing,
 immunity, and cancer.
XX
CC   -!- SIMILARITY: Contains # ZP domain.
XX
DR   PROSITE; PS00682; ZP_1; 1; trigger=no
XX
FT   From: PS51034
FT   DOMAIN     from     to       ZP #.
XX
Chop: Nter=0; Cter=0;
Size: 245-280;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P60852;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2004/12/13
//
AC   PRU00376;
DC   Domain;
TR   PROSITE; PS51037; YEATS; 1; level=0
XX
Names: YEATS domain
Function: The YEATS (for YNL107w, ENL, AF-9, and TFIIF small subunit) domain
 is a ~120-amino acid module of unknown function, which is often found in
 subunits of complexes involved in chromatin modification and transcriptional
 regulation.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Contains # YEATS domain.
XX
GO   GO:0005634; C:nucleus
KW   Nucleus
FT   From: PS51037
FT   DOMAIN     from     to       YEATS #.
XX
Chop: Nter=0; Cter=0;
Size: 100-110;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q99314;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2007/06/07
//
AC   PRU00377;
DC   Domain;
TR   PROSITE; PS51051; DSL; 1; level=0
XX
Names: DSL domain
Function: The DSL domain may mediates oligomerization of DSL proteins to form
 an active ligand and mediates interaction with the extracellular domain of
 Lin-12/Notch proteins.
XX
CC   -!- SIMILARITY: Contains # DSL domain.
XX
DR   PROSITE; PS51051; DSL; 1; trigger=no
XX
FT   From: PS51051
FT   DOMAIN     from     to       DSL #.
XX
Chop: Nter=0; Cter=0;
Size: 45;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P45442;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2005/05/26
//
AC   PRU00378;
DC   Domain;
TR   PROSITE; PS51043; DDHD; 1; level=0
XX
Names: DDHD domain
Function: The DDHD domain  function  is  not  currently  known  but it may be implicated in phospholipid metabolism, membrane turnover, or intracellular trafficking.
XX
CC   -!- SIMILARITY: Contains # DDHD domain.
XX
DR   PROSITE; PS51043; DDHD; 1; trigger=no
XX
FT   From: PS51043
FT   DOMAIN     from     to       DDHD #.
XX
Chop: Nter=0; Cter=0;
Size: 202;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: Q8NEL9;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/04/19
//
AC   PRU00379;
DC   Domain;
c?   <OC:Eukaryota>
TR   PROSITE; PS51055; ITAM_1; 0-1; level=0
c?   <OC:Viruses>
TR   PROSITE; PS51056; ITAM_2; 0-1; level=0
XX
Names: ITAM motif
Function: The ITAM is an immunoreceptor tyrosine-based activation motif. Phosphorylation of the two ITAM tyrosines  is  a critical event in signal transduction. This phosphorylation was found to reflect  activation  of the src family kinase Lyn and Syk.
XX
CC   -!- SIMILARITY: Contains # ITAM domain.
XX
case <OC:Eukaryota>
DR   PROSITE; PS51055; ITAM_1; 1; trigger=no
end case
case <OC:Viruses>
DR   PROSITE; PS51056; ITAM_2; 1; trigger=no
end case
XX
FT   From: PS51055
FT   DOMAIN     from     to       ITAM #.
case <Feature:PS51055:12=Y>
FT   MOD_RES      12     12       Phosphotyrosine (By similarity).
end case
case <Feature:PS51055:23=Y>
FT   MOD_RES      23     23       Phosphotyrosine (By similarity).
end case
FT   From: PS51056
FT   DOMAIN     from     to       ITAM #.
case <Feature:PS51056:5=Y>
FT   MOD_RES       5      5       Phosphotyrosine (By similarity).
end case
case <Feature:PS51056:18=Y>
FT   MOD_RES      18     18       Phosphotyrosine (By similarity).
end case
XX
Chop: Nter=0; Cter=0;
Size: 24-26;
Related: none;
Repeats: 1-3;
Topology: Undefined;
Example: P04234; P28728;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.9  2006/03/29
//
AC   PRU00380;
DC   Domain;
TR   PROSITE; PS51054; ORANGE; 1; level=0
XX
Names: Orange domain
Function: The Orange domain is a ~35 residue domain of unknown function,
 present in eukaryotic DNA-binding transcription repressors which regulate
 cell differentiation, embryonic patterning and other biological processes in
 both vertebrates and invertebrates.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Contains # Orange domain.
XX
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51054
FT   DOMAIN     from     to       Orange #.
XX
Chop: Nter=0; Cter=0;
Size: 20-45;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: O14503;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.4  2007/06/07
//
AC   PRU00381;
DC   Domain;
TR   PROSITE; PS51057; PAIRED_2; 1; level=0
XX
Names: Paired domain
Function: The paired domain is a ~126 amino acid DNA-binding domain, which is
 found in eukaryotic transcription regulatory proteins involved in
 embryogenesis.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # paired domain.
XX
DR   PROSITE; PS00034; PAIRED_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Nucleus
KW   Paired box
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51057
FT   DOMAIN     from     to       Paired #.
XX
Chop: Nter=0; Cter=0;
Size: 120-140;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P63016;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.6  2007/06/07
//
AC   PRU00382;
DC   Domain;
TR   PROSITE; PS51061; R3H; 1; level=0
XX
Names: R3H motif
Function: The  R3H domain is a conserved sequence motif, which  might   be   involved   in polynucleotide-binding, including DNA, RNA and single-stranded DNA
XX
CC   -!- SIMILARITY: Contains # R3H domain.
XX
DR   PROSITE; PS51061; R3H; 1; trigger=no
XX
GO   GO:0003676; F:nucleic acid binding
XX
FT   From: PS51061
FT   DOMAIN     from     to       R3H #.
XX
Chop: Nter=0; Cter=0;
Size: 65;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P38935; Q01620;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.4  2005/04/19
//
AC   PRU00383;
DC   Domain;
TR   PROSITE; PS51046; GON; 1; level=0
XX
Names: GON domain
Function: The GON domain is a ~200-residue module, whose presence is a
 hallmark of a subfamily of structurally and evolutionarily related ADAMTSs,
 called GON-ADAMTSs.
XX
CC   -!- SIMILARITY: Contains # GON domain.
XX
FT   From: PS51046
FT   DOMAIN     from     to       GON #.
XX
Chop: Nter=0; Cter=0;
Size: 195-205;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9P2N4;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/01/18
//
AC   PRU00384;
DC   Domain;
TR   PROSITE; PS51041; EMI; 1; level=0
XX
Names: EMI domain
Function: It has been suggested that the EMI domain could be a protein-protein
 interaction module, as the EMI domain of EMILIN-1 was found to interact with
 the C1q domain of EMILIN-2.
XX
CC   -!- SIMILARITY: Contains # EMI domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51041
FT   DOMAIN     from     to       EMI #.
FT   DISULFID      5     76       Potential.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     34     46       Potential.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     75     90       Potential.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 50-85;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9Y6C2;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2009/02/09
//
AC   PRU00385;
DC   Domain;
TR   PROSITE; PS51049; KASH; 1; level=0
XX
Names: KASH domain
Function: The KASH or KLS domain is a highly hydrophobic nuclear envelope
 localization domain of ~60 amino acids comprising an ~20-amino-acid
 transmembrane region and a 30-35-residue C-terminal region that lies between
 the inner and the outer nuclear membranes.
XX
CC   -!- SIMILARITY: Contains # KASH domain.
XX
DR   General; Transmembrane; -; 1; trigger=no
XX
GO   GO:0016021; C:integral to membrane
GO   GO:0016020; C:membrane
XX
KW   Membrane
KW   Transmembrane
XX
FT   From: PS51049
FT   TOPO_DOM   Nter      9       Cytoplasmic (Potential).
FT   TRANSMEM     10     30       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM     31   Cter       Perinuclear space (Potential).
FT   DOMAIN     from     to       KASH #.
XX
Chop: Nter=0; Cter=0;
Size: 55-65;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q8NF91;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.7  2010/05/10
//
AC   PRU00386;
DC   Domain;
TR   PROSITE; PS51048; SGS; 1; level=0
XX
Names: SGS domain
Function: The SGS domain has been shown to bind to proteins of the S100
 family, which are thought to function as sensors of calcium ion concentration
 in the cell.
XX
CC   -!- SIMILARITY: Contains # SGS domain.
XX
FT   From: PS51048
FT   DOMAIN     from     to       SGS #.
XX
Chop: Nter=0; Cter=0;
Size: 75-95;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q08446;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/01/18
//
AC   PRU00387;
DC   Domain;
TR   PROSITE; PS51063; HTH_CRP_2; 1; level=0
XX
Names: Crp-type HTH domain
Function: The crp-type HTH domain is a DNA-binding, winged helix-turn-helix
 (wHTH) domain of about 70-75 amino acids present in transcription regulators
 of the crp-fnr family, involved in the control of virulence factors, enzymes
 of aromatic ring degradation, nitrogen fixation, photosynthesis, and various
 types of respiration.
XX
CC   -!- SIMILARITY: Contains # HTH crp-type DNA-binding domain.
XX
DR   PROSITE; PS00042; HTH_CRP_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51063
FT   DOMAIN     from     to       HTH crp-type #.
FT   DNA_BIND     43     62       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 40-90;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P27369;
Scope:
 Bacteria
 Plastid
Comments: None
XX
# Revision 1.4  2006/03/23
//
AC   PRU00388;
DC   Domain;
TR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1; level=0
XX
Names: Ubiquitin-conjugating enzyme
Function: Catalyzes the covalent attachment of ubiquitin to target proteins
XX
case <Feature:PS50127:83=C>
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
end case
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
XX
c?   <Feature:PS50127:83=C>
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1; trigger=no
XX
case <Feature:PS50127:83=C>
GO   GO:0016874; F:ligase activity
KW   Ligase
KW   Ubl conjugation pathway
end case
XX
FT   From: PS50127
FT   ACT_SITE     83     83       Glycyl thioester intermediate (By
FT                                similarity).
FT   Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 100-170;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P52484;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.6  2010/06/23
//
AC   PRU00389;
DC   Domain;
TR   PROSITE; PS51064; IRS_PTB; 1; level=0
XX
Names: IRS-type PTB domain
Function: IRS-type  PTB  domain has an average length of about 100 amino acids. It binds to  the  insulin  receptor  through the Asn-Pro-Xaa-Tyr(P) motif found in many tyrosine-phosphorylated proteins.
XX
CC   -!- SIMILARITY: Contains # IRS-type PTB domain.
XX
DR   PROSITE; PS51064; IRS_PTB; 1; trigger=no
XX
FT   From: PS51064
FT   DOMAIN     from     to       IRS-type PTB #.
XX
Chop: Nter=0; Cter=0;
Size: 105;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: Q99704; P35568;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2005/04/19
//
AC   PRU00390;
DC   Domain;
TR   PROSITE; PS51071; HTH_RPIR; 1; level=0
XX
Names: RpiR-type HTH domain
Function: The rpiR-type HTH domain is a DNA-binding, helix-turn-helix (HTH)
 domain of about 75-80 amino acids present in prokaryotic regulators of
 transcription.
XX
CC   -!- SIMILARITY: Contains # HTH rpiR-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51071
FT   DOMAIN     from     to       HTH rpiR-type #.
FT   DNA_BIND     37     56       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 70-90;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P0ACS7;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.4  2006/09/14
//
AC   PRU00391;
DC   Domain;
TR   PROSITE; PS51066; ZF_FPG_2; 1; level=0
XX
Names: Zinc finger FPG-type
Function: Zinc finger specific to Formamidopyrimidine-DNA glycosylase and
 Endonuclease VIII. It binds DNA.
XX
case <Feature:PS51066:10=[C]> and <Feature:PS51066:13=[C]> and <Feature:PS51066:30=[C]> and <Feature:PS51066:33=[C]>
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
end case
CC   -!- SIMILARITY: Contains # FPG-type zinc finger.
DR   PROSITE; PS01242; ZF_FPG_1; 1; trigger=no
XX
KW   Zinc-finger
case <Feature:PS51066:10=[CH]> and <Feature:PS51066:13=[CH]> and <Feature:PS51066:30=[CH]> and <Feature:PS51066:33=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS51066
case <Feature:PS51066:10=[C]> and <Feature:PS51066:13=[C]> and <Feature:PS51066:30=[C]> and <Feature:PS51066:33=[C]>
FT   ZN_FING    from     to       FPG-type #.
else case <Feature:PS51066:10=[CH]> and <Feature:PS51066:13=[CH]> and <Feature:PS51066:30=[CH]> and <Feature:PS51066:33=[CH]>
FT   ZN_FING    from     to       FPG-type #; atypical.
else
FT   ZN_FING    from     to       FPG-type #; degenerate.
FT   ACT_SITE     25     25       Proton donor (in delta-elimination) (By
FT                                similarity).
FT   Condition: R
end case
XX
Chop: Nter=0; Cter=0;
Size: 25-50;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P64159;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.8  2006/07/17
//
AC   PRU00392;
DC   Domain;
TR   PROSITE; PS51068; FPG_CAT; 1; level=0
XX
Names: Formamidopyrimidine-DNA glycosylase catalytic domain
Function: DNA glycosylase
XX
case <FTGroup:1>
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by
CC       oxidation or by mutagenic agents. Acts as DNA glycosylase that
CC       recognizes and removes damaged bases. Has AP
CC       (apurinic/apyrimidinic) lyase activity and introduces nicks in the
CC       DNA strand. Cleaves the DNA backbone by beta-delta elimination to
CC       generate a single-strand break at the site of the removed base
CC       with both 3'- and 5'-phosphates (By similarity).
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate.
CC   -!- SIMILARITY: Belongs to the FPG family.
end case
XX
case <FTGroup:1>
GO   GO:0006974; P:response to DNA damage stimulus
GO   GO:0006281; P:DNA repair
GO   GO:0003677; F:DNA binding
GO   GO:0016798; F:hydrolase activity, acting on glycosyl bonds
GO   GO:0016787; F:hydrolase activity
GO   GO:0016829; F:lyase activity
GO   GO:0003824; F:catalytic activity
KW   DNA damage
KW   DNA repair
KW   DNA-binding
KW   Glycosidase
KW   Hydrolase
KW   Lyase
KW   Multifunctional enzyme
end case
XX
FT   From: PS51068
FT   ACT_SITE      1      1       Schiff-base intermediate with DNA (By
FT                                similarity).
FT   Group: 1; Condition: P
FT   ACT_SITE      2      2       Proton donor (By similarity).
FT   Group: 1; Condition: E
FT   ACT_SITE     57     57       Proton donor (in beta-elimination) (By
FT                                similarity).
FT   Group: 1; Condition: K
XX
Chop: Nter=0; Cter=0;
Size: 70-150;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P05523;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.5  2005/05/27
//
AC   PRU00393;
DC   Domain;
TR   PROSITE; PS51077; HTH_ICLR; 1; level=0
XX
Names: IclR-type HTH domain
Function: The iclR-type HTH domain is a DNA-binding, winged helix-turn-helix
 (wHTH) domain of about 60 amino acids present in transcription regulators of
 the iclR family, involved in carbon metabolism in eubacteria and archaea.
XX
CC   -!- SIMILARITY: Contains # HTH iclR-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51077
FT   DOMAIN     from     to       HTH iclR-type #.
FT   DNA_BIND     23     42       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 50-75;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: P37728;
Scope:
 Bacteria
 Archaea
 Bacteriophage
Comments: None
XX
# Revision 1.4  2006/09/14
//
AC   PRU00394;
DC   Domain;
TR   PROSITE; PS51078; ICLR_ED; 1; level=0
XX
Names: IclR effector binding domain
Function: The iclR effector binding domain is a ~170 residues C-terminal
 regulatory domain, present in transcription regulators of the iclR family,
 involved in carbon metabolism in eubacteria and archaea.
XX
CC   -!- SIMILARITY: Contains # iclR-ED (iclR effector binding) domain.
XX
FT   From: PS51078
FT   DOMAIN       15     to       IclR-ED #.
XX
Chop: Nter=0; Cter=0;
Size: 170-190;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: P16528;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.3  2005/06/28
//
AC   PRU00395;
DC   Domain;
TR   PROSITE; PS51052; CYCLOTIDE; 1; level=0
XX
Names: Cyclotides
Function: Cyclotides (cyclo peptides) are plant peptides of ~30 amino acids
 with a head-to-tail cyclic backbone and six cysteine residues involved in
 three disulfide bonds. They are most likely present as defense molecules.
XX
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC   -!- PTM: This is a cyclic peptide.
case <Feature:PS60008> and not <Feature:PS60009>
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
else case <Feature:PS60009> and not <Feature:PS60008>
CC   -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
else
CC   -!- SIMILARITY: Belongs to the cyclotide family.
end case
CC   -!- CAUTION: This peptide is cyclic. The start position was chosen by
CC       similarity to Oak1 (kalata B1) for which the DNA sequence is
CC       known.
DR   PROSITE; PS60008; CYCLOTIDE_BRACELET; 0-1; trigger=no
DR   PROSITE; PS60009; CYCLOTIDE_MOEBIUS; 0-3; trigger=no
KW   Plant defense
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51052
FT   PEPTIDE    from     to       <name>.
FT   DISULFID      5     19       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      9     21       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     14     26       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 20-35;
Related: None;
Repeats: 1-3;
Topology: Not cytoplasmic;
Example: P58433; P56254;
Scope:
 Eukaryota; Viridiplantae; Embryophyta
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00396;
DC   Domain;
TR   PROSITE; PS51053; SERTA; 1; level=0
XX
Names: SERTA domain
Function: The cyclin-dependent kinase CDK4-interacting segment of TRIP-Br1
 includes most of the SERTA domain.
XX
CC   -!- SIMILARITY: Contains # SERTA domain.
XX
FT   From: PS51053
FT   DOMAIN     from     to       SERTA #.
XX
Chop: Nter=0; Cter=0;
Size: 45-50;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UHV2;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/02/10
//
AC   PRU00397;
DC   Domain;
TR   PROSITE; PS51059; PARP_CATALYTIC; 1; level=0
XX
Names: PARP catalytic domain
Function: Poly(ADP-ribose) polymerase (PARP) transfers the ADP-ribose moiety
 from its substrate, nicotinamide adenine dinucleotide (NAD), to carboxylate
 groups of aspartic and glutamic residues.
XX
DE   + AltName: Full=Poly [ADP-ribose] polymerase;
DE            EC=2.4.2.30;
XX
CC   -!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
CC       nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
CC   -!- SIMILARITY: Contains # PARP catalytic domain.
XX
GO   GO:0016740; F:transferase activity
GO   GO:0016757; F:transferase activity, transferring glycosyl groups
XX
KW   Glycosyltransferase
KW   NAD
KW   Transferase
XX
FT   From: PS51059
FT   DOMAIN     from     to       PARP catalytic #.
XX
Chop: Nter=0; Cter=0;
Size: 185-235;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P35875;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00398;
DC   Domain;
TR   PROSITE; PS51060; PARP_ALPHA_HD; 1; level=0
XX
Names: PARP alpha-helical domain
Function: The poly(ADP-ribose) polymerase (PARP) alpha-helical domain is
 thought to relay the activation signal issued on binding to damaged DNA.
XX
CC   -!- SIMILARITY: Contains # PARP alpha-helical domain.
XX
FT   From: PS51060
FT   DOMAIN     from     to       PARP alpha-helical #.
XX
Chop: Nter=0; Cter=0;
Size: 115-140;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P09874;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/02/11
//
AC   PRU00399;
DC   Domain;
TR   PROSITE; PS51062; RUNT; 1; level=0
XX
Names: Runt domain
Function: The Runt domain confers DNA binding ability to the consensus core
 PyGPyGGT and mediates the interaction of mammalian RUNX proteins with the
 beta-subunit, designated core-binding factor beta (CBFbeta), which increases
 the DNA binding affinity of the heterodimer.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # Runt domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
case <FTGroup:1> or <FTGroup:2>
KW   Chloride
end case
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51062
FT   DOMAIN     from     to       Runt #.
FT   SITE         31     35       Interaction with DNA (By similarity).
FT   SITE         86     94       Interaction with DNA (By similarity).
FT   SITE        119    128       Interaction with DNA (By similarity).
FT   BINDING      63     63       Chloride #1 (By similarity).
FT   Group: 1; Condition: N
FT   BINDING      67     67       Chloride #1 (By similarity).
FT   Group: 1; Condition: E
FT   BINDING      90     90       Chloride #2 (By similarity).
FT   Group: 2; Condition: R
FT   BINDING     121    121       Chloride #2 (By similarity).
FT   Group: 2; Condition: V
XX
Chop: Nter=0; Cter=0;
Size: 125-135;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q01196;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2007/06/21
//
AC   PRU00400;
DC   Domain;
TR   PROSITE; PS51065; NHR; 1; level=0
XX
Names: Neuralized homology repeat (NHR) domain
Function: It has been suggested that the NHR domain is required for the
 localization of neuralized to the plasma membrane and that it might possess a
 microtubule-binding function.
XX
CC   -!- SIMILARITY: Contains # NHR (neuralized homology repeat) domain.
XX
FT   From: PS51065
FT   DOMAIN     from     to       NHR #.
XX
Chop: Nter=0; Cter=0;
Size: 150-225;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: P29503;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2005/12/06
//
AC   PRU00401;
DC   Domain;
TR   PROSITE; PS51073; RPEL; 1; level=0
XX
Names: RPEL repeat
Function: RPEL (RPxxxEL) repeats have been shown to be required for
 unpolymerized actin binding and proteins containing RPEL repeats are able to
 modify cell shape and/or are important in the regulation of gene expression
 by the actin cytoskeleton.
XX
CC   -!- SIMILARITY: Contains # RPEL repeat.
XX
FT   From: PS51073
FT   REPEAT     from     to       RPEL #.
XX
Chop: Nter=0; Cter=0;
Size: 20-30;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: Q8IZQ8;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/02/15
//
AC   PRU00402;
DC   Domain;
TR   PROSITE; PS51069; GBP; 1; level=0
XX
Names: GBP repeat
Function: The GBP repeats have been shown to bind to the erythrocyte receptor
 glycophorin.
XX
CC   -!- SIMILARITY: Contains # GBP repeat.
XX
case <OC:Plasmodium>
KW   Malaria
end case
FT   From: PS51069
FT   REPEAT    entry   exit       GBP #.
XX
Chop: Nter=0; Cter=0;
Size: 40-55;
Related: None;
Repeats: 8-12;
Topology: Undefined;
Example: Q8I6U8;
Scope:
 Eukaryota; Alveolata; Plasmodium
Comments: None
XX
# Revision 1.2  2005/03/09
//
AC   PRU00403;
DC   Domain;
TR   PROSITE; PS51070; SHD; 1; level=0
XX
Names: Stonin homology domain (SHD)
Function: The ~140 amino-acid SHD domain may be unique to members of the
 stonin family, which are supposed to be endocytotic proteins involved in
 clathrin-mediated endocytosis at synapses. Its function is not yet known.
XX
CC   -!- SIMILARITY: Contains # stonin homology (SHD) domain.
XX
GO   GO:0006897; P:endocytosis
GO   GO:0016020; C:membrane
GO   GO:0045202; C:synapse
KW   Endocytosis
KW   Membrane
KW   Synapse
XX
FT   From: PS51070
FT   DOMAIN     from     to       SHD #.
XX
Chop: Nter=0; Cter=0;
Size: 130-180;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q24212;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/02/15
//
AC   PRU00404;
DC   Domain;
TR   PROSITE; PS51072; MHD; 1; level=0
XX
Names: Mu homology domain (MHD)
Function: The MHD domain is found in endocytotic proteins involved in
 clathrin-mediated endocytosis and has been shown to bind to the C2B domain of
 members of the synaptotagmin family.
XX
CC   -!- SIMILARITY: Contains # MHD (mu homology) domain.
XX
GO   GO:0016020; C:membrane
KW   Membrane
XX
FT   From: PS51072
FT   DOMAIN     from     to       MHD #.
XX
Chop: Nter=0; Cter=0;
Size: 240-345;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P38153;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/03/22
//
AC   PRU00405;
DC   Domain;
TR   PROSITE; PS50878; RT_POL; 1; level=0
XX
Names: Reverse transcriptase (RT) catalytic domain
Function: The RT domain exhibits two enzymatic activities: RNA-dependent DNA
 polymerase and DNA-dependent DNA polymerase.
XX
case <FTGroup:1>
DE   + RecName: EC=2.7.7.49;
DE   AltName: EC 2.7.7.7;
end case
case <OS:Human immunodeficiency virus> and <Feature:PS50879>
CC   -!- FUNCTION: RT is a multifunctional enzyme that converts the viral
CC       dimeric RNA genome into dsDNA in the cytoplasm, shortly after
CC       virus entry into the cell. This enzyme displays a DNA polymerase
CC       activity that can copy either DNA or RNA templates, and a
CC       ribonuclease H (RNAse H) activity that cleaves the RNA strand of
CC       RNA-DNA heteroduplexes in a partially processive 3' to 5'
CC       endonucleasic mode. Conversion of viral genomic RNA into dsDNA
CC       requires many steps. A tRNA(3)-Lys binds to the primer-binding
CC       site (PBS) situated at the 5' end of the viral RNA. RT uses the 3'
CC       end of the tRNA primer to perfom a short round of RNA-dependent
CC       minus-strand DNA synthesis. The reading proceeds through the U5
CC       region and ends after the repeated (R) region which is present at
CC       both ends of viral RNA. The portion of the RNA-DNA heteroduplex is
CC       digested by the RNase H, resulting in a ssDNA product attached to
CC       the tRNA primer. This ssDNA/tRNA hybridizes with the identical R
CC       region situated at the 3' end of viral RNA. This template
CC       exchange, known as minus-strand DNA strong stop transfer, can be
CC       either intra- or intermolecular. RT uses the 3' end of this newly
CC       synthetized short ssDNA to perfom the RNA-dependent minus-strand
CC       DNA synthesis of the whole template. RNase H digests the RNA
CC       template except for two polypurine tracts (PPTs) situated at the
CC       5' end and near the center of the genome. It is not clear if both
CC       polymerase and RNase H activities are simultaneous. RNase H
CC       probably can proceed both in a polymerase-dependent (RNA cut into
CC       small fragments by the same RT performing DNA synthesis) and a
CC       polymerase-independent mode (cleavage of remaining RNA fragments
CC       by free RTs). Secondly, RT performs DNA-directed plus-strand DNA
CC       synthesis using the PPTs that have not been removed by RNase H as
CC       primers. PPTs and tRNA primers are then removed by RNAse H. The 3'
CC       and 5' ssDNA PBS regions hybridize to form a circular dsDNA
CC       intermediate. Strand displacement synthesis by RT to the PBS and
CC       PPT ends produces a blunt ended, linear dsDNA copy of the viral
CC       genome that includes long terminal repeats (LTRs) at both ends (By
CC       similarity).
else case <OC:alpharetrovirus> and <Feature:PS50879>
CC   -!- FUNCTION: RT is a multifunctional enzyme that converts the viral
CC       dimeric RNA genome into dsDNA in the cytoplasm, shortly after
CC       virus entry into the cell. This enzyme displays a DNA polymerase
CC       activity that can copy either DNA or RNA templates, and a
CC       ribonuclease H (RNAse H) activity that cleaves the RNA strand of
CC       RNA-DNA heteroduplexes in a partially processive 3' to 5'
CC       endonucleasic mode. Conversion of viral genomic RNA into dsDNA
CC       requires many steps. A tRNA-Trp binds to the primer-binding site
CC       (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end
CC       of the tRNA primer to perfom a short round of RNA-dependent minus-
CC       strand DNA synthesis. The reading proceeds through the U5 region
CC       and ends after the repeated (R) region which is present at both
CC       ends of viral RNA. The portion of the RNA-DNA heteroduplex is
CC       digested by the RNase H, resulting in a ssDNA product attached to
CC       the tRNA primer. This ssDNA/tRNA hybridizes with the identical R
CC       region situated at the 3' end of viral RNA. This template
CC       exchange, known as minus-strand DNA strong stop transfer, can be
CC       either intra- or intermolecular. RT uses the 3' end of this newly
CC       synthetized short ssDNA to perfom the RNA-dependent minus-strand
CC       DNA synthesis of the whole template. RNase H digests the RNA
CC       template except for a polypurine tract (PPT) situated at the 5'
CC       end of the genome. It is not clear if both polymerase and RNase H
CC       activities are simultaneous. RNase H probably can proceed both in
CC       a polymerase-dependent (RNA cut into small fragments by the same
CC       RT performing DNA synthesis) and a polymerase-independent mode
CC       (cleavage of remaining RNA fragments by free RTs). Secondly, RT
CC       performs DNA-directed plus-strand DNA synthesis using the PPT that
CC       has not been removed by RNase H as primers. PPT and tRNA primers
CC       are then removed by RNAse H. The 3' and 5' ssDNA PBS regions
CC       hybridize to form a circular dsDNA intermediate. Strand
CC       displacement synthesis by RT to the PBS and PPT ends produces a
CC       blunt ended, linear dsDNA copy of the viral genome that includes
CC       long terminal repeats (LTRs) at both ends (By similarity).
else case <OC:betaretrovirus> or <OC:gammaretrovirus> or <OC:epsilonretrovirus> or <OC:lentivirus> and <Feature:PS50879>
CC   -!- FUNCTION: RT is a multifunctional enzyme that converts the viral
CC       dimeric RNA genome into dsDNA in the cytoplasm, shortly after
CC       virus entry into the cell. This enzyme displays a DNA polymerase
CC       activity that can copy either DNA or RNA templates, and a
CC       ribonuclease H (RNAse H) activity that cleaves the RNA strand of
CC       RNA-DNA heteroduplexes in a partially processive 3' to 5'
CC       endonucleasic mode. Conversion of viral genomic RNA into dsDNA
CC       requires many steps. A tRNA binds to the primer-binding site (PBS)
CC       situated at the 5' end of the viral RNA. RT uses the 3' end of the
CC       tRNA primer to perfom a short round of RNA-dependent minus-strand
CC       DNA synthesis. The reading proceeds through the U5 region and ends
CC       after the repeated (R) region which is present at both ends of
CC       viral RNA. The portion of the RNA-DNA heteroduplex is digested by
CC       the RNase H, resulting in a ssDNA product attached to the tRNA
CC       primer. This ssDNA/tRNA hybridizes with the identical R region
CC       situated at the 3' end of viral RNA. This template exchange, known
CC       as minus-strand DNA strong stop transfer, can be either intra- or
CC       intermolecular. RT uses the 3' end of this newly synthetized short
CC       ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of
CC       the whole template. RNase H digests the RNA template except for a
CC       polypurine tract (PPT) situated at the 5' end of the genome. It is
CC       not clear if both polymerase and RNase H activities are
CC       simultaneous. RNase H probably can proceed both in a polymerase-
CC       dependent (RNA cut into small fragments by the same RT performing
CC       DNA synthesis) and a polymerase-independent mode (cleavage of
CC       remaining RNA fragments by free RTs). Secondly, RT performs DNA-
CC       directed plus-strand DNA synthesis using the PPT that has not been
CC       removed by RNase H as primers. PPT and tRNA primers are then
CC       removed by RNAse H. The 3' and 5' ssDNA PBS regions hybridize to
CC       form a circular dsDNA intermediate. Strand displacement synthesis
CC       by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA
CC       copy of the viral genome that includes long terminal repeats
CC       (LTRs) at both ends (By similarity).
else case <OC:deltaretrovirus> and <Feature:PS50879>
CC   -!- FUNCTION: RT is a multifunctional enzyme that converts the viral
CC       dimeric RNA genome into dsDNA in the cytoplasm, shortly after
CC       virus entry into the cell. This enzyme displays a DNA polymerase
CC       activity that can copy either DNA or RNA templates, and a
CC       ribonuclease H (RNAse H) activity that cleaves the RNA strand of
CC       RNA-DNA heteroduplexes in a partially processive 3' to 5'
CC       endonucleasic mode. Conversion of viral genomic RNA into dsDNA
CC       requires many steps. A tRNA-Pro binds to the primer-binding site
CC       (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end
CC       of the tRNA primer to perfom a short round of RNA-dependent minus-
CC       strand DNA synthesis. The reading proceeds through the U5 region
CC       and ends after the repeated (R) region which is present at both
CC       ends of viral RNA. The portion of the RNA-DNA heteroduplex is
CC       digested by the RNase H, resulting in a ssDNA product attached to
CC       the tRNA primer. This ssDNA/tRNA hybridizes with the identical R
CC       region situated at the 3' end of viral RNA. This template
CC       exchange, known as minus-strand DNA strong stop transfer, can be
CC       either intra- or intermolecular. RT uses the 3' end of this newly
CC       synthetized short ssDNA to perfom the RNA-dependent minus-strand
CC       DNA synthesis of the whole template. RNase H digests the RNA
CC       template except for a polypurine tract (PPT) situated at the 5'
CC       end of the genome. It is not clear if both polymerase and RNase H
CC       activities are simultaneous. RNase H probably can proceed both in
CC       a polymerase-dependent (RNA cut into small fragments by the same
CC       RT performing DNA synthesis) and a polymerase-independent mode
CC       (cleavage of remaining RNA fragments by free RTs). Secondly, RT
CC       performs DNA-directed plus-strand DNA synthesis using the PPT that
CC       has not been removed by RNase H as primers. PPT and tRNA primers
CC       are then removed by RNAse H. The 3' and 5' ssDNA PBS regions
CC       hybridize to form a circular dsDNA intermediate. Strand
CC       displacement synthesis by RT to the PBS and PPT ends produces a
CC       blunt ended, linear dsDNA copy of the viral genome that includes
CC       long terminal repeats (LTRs) at both ends (By similarity).
end case
XX
case <FTGroup:1>
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1).
end case
XX
case <OC:retroviridae>
CC   -!- COFACTOR: The RT polymerase active site binds 2 magnesium ions (By
CC       similarity).
end case
XX
case <OC:lentivirus>
CC   -!- SUBUNIT: The reverse transcriptase is a heterodimer of p66 RT and
CC       p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA
CC       polymerase activity. Despite the sequence identities, p66 RT and
CC       p51 RT have distinct folding (By similarity).
else case <OC:alpharetrovirus>
CC   -!- SUBUNIT: The reverse transcriptase forms a heterodimer of alpha
CC       and beta subunits (By similarity).
else case <OC:gammaretrovirus>
CC   -!- SUBUNIT: The reverse transcriptase is a monomer (By similarity).
end case
XX
case <OC:lentivirus>
CC   -!- DOMAIN: The p66 RT is structured in five subdomains: finger, palm,
CC       thumb, connection and RNase H. Within the palm subdomain, the
CC       "primer grip" region is thought to be involved in the positioning
CC       of the primer terminus for accomodating the incoming nucleotide.
CC       The RNase H domain stabilizes the association of RT with primer-
CC       template (By similarity).
end case
XX
case <OC:lentivirus>
CC   -!- PTM: Specific enzymatic cleavages by the viral protease yield
CC       mature proteins. The protease is released by autocatalytic
CC       cleavage. The polyprotein is cleaved during and after budding,
CC       this process is termed maturation. Proteolytic cleavage of p66 RT
CC       removes the RNase H domain to yield the p51 RT subunit (By
CC       similarity).
end case
XX
case <OC:retroviridae>
CC   -!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme
CC       that lacks a proof-reading function. High mutations rate is a
CC       direct consequence of this characteristic. RT also displays
CC       frequent template swiching leading to high recombination rate.
CC       Recombination mostly occurs between homologous regions of the two
CC       copackaged RNA genomes. If these two RNA molecules derive from
CC       different viral strains, reverse transcription will give rise to
CC       highly recombinated proviral DNAs (By similarity).
end case
XX
CC   -!- SIMILARITY: Contains 1 reverse transcriptase domain.
XX
GO   GO:0016740; F:transferase activity
GO   GO:0016779; F:nucleotidyltransferase activity
GO   GO:0003964; F:RNA-directed DNA polymerase activity
GO   GO:0003887; F:DNA-directed DNA polymerase activity
XX
KW   Transferase
KW   Nucleotidyltransferase
KW   RNA-directed DNA polymerase
KW   DNA-directed DNA polymerase
KW   Multifunctional enzyme
KW   DNA-binding
KW   RNA-binding
KW   DNA recombination
KW   Metal-binding
KW   Magnesium
XX
FT   From: PS50878
FT   DOMAIN     from     to       Reverse transcriptase #.
FT   METAL        66     66       Magnesium; catalytic (By similarity).
FT   Group: 1; Condition: D
FT   METAL       130    130       Magnesium; catalytic (By similarity).
FT   Group: 1; Condition: D
FT   METAL       131    131       Magnesium; catalytic (By similarity).
FT   Group: 1; Condition: D
XX
Chop: Nter=0; Cter=0;
Size: 140-285;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O14746;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.10  2009/02/27
//
AC   PRU00406;
DC   Domain;
TR   PROSITE; PS51082; WH2; 1; level=0
XX
Names: WH2 domain
 WASP-Homology 2
 Wiskott-Aldrich homology 2
Function: The WH2 (WASP-Homology 2, or Wiskott-Aldrich homology 2) domain is
 an ~18 amino acids actin-binding motif.
XX
CC   -!- SIMILARITY: Contains # WH2 domain.
XX
GO   GO:0003779; F:actin binding
KW   Actin-binding
FT   From: PS51082
FT   DOMAIN     from     to       WH2 #.
XX
Chop: Nter=0; Cter=0;
Size: 10-30;
Related: None;
Repeats: 1-4;
Topology: Cytoplasmic;
Example: O00401;
Scope:
 Eukaryota
 Viruses
 Bacteria
Comments: None
XX
# Revision 1.1  2005/03/01
//
AC   PRU00407;
DC   Domain;
TR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1; level=0
XX
Names: Nuclear hormone receptors DNA-binding domain
Function: Nuclear hormone receptors are ligand-activated transcription factors
 that regulate gene expression by interacting with specific DNA sequences
 upstream of their target genes.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # nuclear receptor DNA-binding domain.
XX
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
GO   GO:0005634; C:nucleus
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
KW   Zinc-finger
case <Feature:PS51030:4=[CH]> and <Feature:PS51030:7=[CH]> and <Feature:PS51030:21=[CH]> and <Feature:PS51030:24=[CH]> or <Feature:PS51030:40=[CH]> and <Feature:PS51030:46=[CH]> and <Feature:PS51030:56=[CH]> and <Feature:PS51030:59=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS51030
FT   DNA_BIND   from     to       Nuclear receptor #.
case <Feature:PS51030:4=[C]> and <Feature:PS51030:7=[C]> and <Feature:PS51030:21=[C]> and <Feature:PS51030:24=[C]>
FT   ZN_FING       4     24       NR C4-type.
else case <Feature:PS51030:4=[CH]> and <Feature:PS51030:7=[CH]> and <Feature:PS51030:21=[CH]> and <Feature:PS51030:24=[CH]>
FT   ZN_FING       4     24       NR C4-type; atypical.
else
FT   ZN_FING       4     24       NR C4-type; degenerate.
end case
case <Feature:PS51030:40=[C]> and <Feature:PS51030:46=[C]> and <Feature:PS51030:56=[C]> and <Feature:PS51030:59=[C]>
FT   ZN_FING      40     59       NR C4-type.
else case <Feature:PS51030:40=[CH]> and <Feature:PS51030:46=[CH]> and <Feature:PS51030:56=[CH]> and <Feature:PS51030:59=[CH]>
FT   ZN_FING      40     59       NR C4-type; atypical.
else
FT   ZN_FING      40     59       NR C4-type; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 30-80;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9W539;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.12  2007/06/21
//
AC   PRU00408;
DC   Domain;
TR   PROSITE; PS50879; RNASE_H; 1; level=0
XX
Names: Ribonuclease H domain
Function: Ribonuclease H (RNase H) (EC 3.1.26.4) recognizes and cleaves the
 RNA strand of RNA-DNA heteroduplexes.
XX
DE   + RecName: EC=3.1.26.4;
XX
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester.
XX
CC   -!- SIMILARITY: Contains 1 RNase H domain.
XX
GO   GO:0004519; F:endonuclease activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0004518; F:nuclease activity
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
XX
KW   Endonuclease
KW   Hydrolase
KW   Nuclease
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
XX
FT   From: PS50879
FT   DOMAIN     from     to       RNase H.
case not <OC:Bacteria> and not <OC:Archaea>
FT   METAL        10     10       Magnesium (By similarity).
FT   Group: 1; Condition: D
FT   METAL        50     50       Magnesium (By similarity).
FT   Group: 1; Condition: E
FT   METAL        74     74       Magnesium (By similarity).
FT   Group: 1; Condition: D
FT   METAL       127    127       Magnesium (By similarity).
FT   Group: 1; Condition: D
end case
XX
Chop: Nter=0; Cter=0;
Size: 101-205;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q08885;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.11  2009/02/27
//
AC   PRU00409;
DC   Domain;
TR   PROSITE; PS50975; ATP_GRASP; 1; level=0
XX
Names: ATP-grasp domain
Function: The  ATP-grasp superfamily currently includes 17 groups of enzymes,
 catalyzing ATP-dependent ligation of a carboxylate containing molecule to an amino
 or thiol group-containing molecule.
XX
case <FTGroup:1> or <FTGroup:2>
CC   -!- COFACTOR: Binds #(magnesium or manganese,ion) per subunit (By
CC       similarity).
end case
CC   -!- SIMILARITY: Contains # ATP-grasp domain.
XX
GO   GO:0005524; F:ATP binding
GO   GO:0000166; F:nucleotide binding
case <FTGroup:1> or <FTGroup:2>
GO   GO:0000287; F:magnesium ion binding
GO   GO:0030145; F:manganese ion binding
end case
XX
KW   ATP-binding
KW   Nucleotide-binding
case <FTGroup:1> or <FTGroup:2>
KW   Magnesium
KW   Manganese
KW   Metal-binding
end case
XX
FT   From: PS50975
FT   DOMAIN     from     to       ATP-grasp #.
FT   NP_BIND      27     84       ATP (By similarity).
FT   METAL       152    152       Magnesium or manganese #1 (By
FT                                similarity).
FT   Group: 1; Condition: [QDE]
FT   METAL       165    165       Magnesium or manganese #1 (By
FT                                similarity).
FT   Group: 1; Condition: E
FT   METAL       165    165       Magnesium or manganese #2 (By
FT                                similarity).
FT   Group: 2; Condition: E
FT   METAL       167    167       Magnesium or manganese #2 (By
FT                                similarity).
FT   Group: 2; Condition: N
XX
case not <FTGroup:1> and not <FTGroup:2>
Warn: one magnesium or manganese binding site was not detected!
end case
Chop: Nter=0; Cter=0;
Size: 140-255;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q75D66;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.9  2008/03/20
//
AC   PRU00410;
DC   Domain;
TR   PROSITE; PS50229; WH1; 1; level=0
XX
Names: WH1 domain
 WASP-Homology 1
 Wiskott-Aldrich homology 1
 EVH1
 Ena/VASP homology 1
 Enabled/Vasodilator-stimulated phosphoprotein homology 1
Function: The WH1 (WASP-Homology 1, or Wiskott-Aldrich homology 1) or EVH1
 (Ena/VASP homology 1, or Enabled/Vasodilator-stimulated phosphoprotein
 homology 1) domain is an ~110 amino acids protein-protein interaction module.
XX
CC   -!- SIMILARITY: Contains # WH1 domain.
XX
FT   From: PS50229
FT   DOMAIN     from     to       WH1 #.
XX
Chop: Nter=0; Cter=0;
Size: 100-130;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: P42768;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/03/03
//
AC   PRU00411;
DC   Domain;
TR   PROSITE; PS50043; HTH_LUXR_2; 1; level=0
XX
Names: LuxR-type HTH domain
Function: The luxR-type HTH domain is a DNA-binding, helix-turn-helix (HTH)
 domain of about 65 amino acids, present in transcription regulators of the
 LuxR/FixJ family of response regulators.
XX
CC   -!- SIMILARITY: Contains # HTH luxR-type DNA-binding domain.
XX
DR   PROSITE; PS00622; HTH_LUXR_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS50043
FT   DOMAIN     from     to       HTH luxR-type #.
FT   DNA_BIND     24     43       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 50-75;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P31802;
Scope:
 Bacteria
 Plastid
Comments: None
XX
# Revision 1.4  2006/09/14
//
AC   PRU00412;
DC   Domain;
TR   PROSITE; PS51087; APAG; 1; level=0
XX
Names: ApaG domain
Function: The apaG domain is a ~125 amino acids domain present in bacterial
 apaG proteins and in eukaryotic F-box proteins.
XX
CC   -!- SIMILARITY: Contains # apaG domain.
XX
FT   From: PS51087
FT   DOMAIN     from     to       ApaG #.
XX
Chop: Nter=0; Cter=0;
Size: 110-140;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q56017;
Scope:
 Bacteria
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/03/15
//
AC   PRU00413;
DC   Domain;
TR   PROSITE; PS51090; CORTACTIN; 1; level=0
XX
Names: Cortactin repeat
 HS1 repeat
Function: The cortactin or HS1 repeat is a tandem repeat of 37-amino acid
 actin-binding domains.
XX
CC   -!- SIMILARITY: Contains # cortactin repeat.
XX
GO   GO:0003779; F:actin binding
KW   Actin-binding
FT   From: PS51090
FT   REPEAT    entry   exit       Cortactin #.
XX
Chop: Nter=0; Cter=0;
Size: 30-50;
Related: None;
Repeats: 1-7;
Topology: Cytoplasmic;
Example: Q14247;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/03/22
//
AC   PRU00414;
DC   Domain;
TR   PROSITE; PS51110; SAP_A; 1; level=0
XX
Names: Saposin A-type domain
Function: The saposin A-type domain is a ~40 amino acid domain present in the
 saposin precursor, prosaposin, in the propeptides that are cleaved off in the
 activation reaction.
XX
CC   -!- SIMILARITY: Contains # saposin A-type domain.
XX
FT   From: PS51110
FT   DOMAIN     from     to       Saposin A-type #.
XX
Chop: Nter=0; Cter=0;
Size: 30-50;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P07602;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/04/06
//
AC   PRU00415;
DC   Domain;
TR   PROSITE; PS50015; SAP_B; 1; level=0
XX
Names: Saposin B-type domain
Function: The saposin B-type domain is a ~80 amino acid domain present in
 saposins and related proteins that interact with lipids. In plant aspartic
 proteinases the two subdomains that are connected by disulfide bridges occur
 in inversed order, these "swapped" halves are called a "swaposin" domain.
XX
CC   -!- SIMILARITY: Contains # saposin B-type domain.
XX
case <Feature:PS50015:22=N>
KW   Glycoprotein
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50015
FT   DOMAIN    entry   exit       Saposin B-type #.
FT   DISULFID      5     79       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID      8     73       By similarity.
FT   Tag: disulf; Group: 2; Condition: C-x*-C
FT   DISULFID     36     48       By similarity.
FT   Tag: disulf; Group: 3; Condition: C-x*-C
FT   CARBOHYD     22     22       N-linked (GlcNAc...) (Potential).
FT   Condition: N
XX
case not <FTGroup:1> and not <FTGroup:2> and not <FTGroup:3>
Warn: In plant aspartic proteinases two half SAP_B subdomains occur in inversed order. Correct the boundaries and check the three disulfide bonds in these "swaposins".
end case
Chop: Nter=0; Cter=0;
Size: 35-160;
Related: None;
Repeats: 1-8;
Topology: Undefined;
Example: P07602;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00416;
DC   Domain;
TR   PROSITE; PS51093; PTS_EIIA_TYPE_1; 1; level=0
XX
Names: PTS EIIA type-1 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
DE   + RecName: EC=2.7.1.-;
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
CC       histidyl residue. Then, it transfers the phosphoryl group to the
CC       EIIB domain.
CC   -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine +
CC       protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine.
CC   -!- SIMILARITY: Contains # PTS EIIA type-1 domain.
end case
XX
DR   PROSITE; PS51093; PTS_EIIA_TYPE_1; 1; trigger=no
XX
GO   GO:0016301; F:kinase activity
GO   GO:0016740; F:transferase activity
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Kinase
KW   Phosphotransferase system
KW   Transferase
end case
FT   From: PS51093
FT   DOMAIN     from     to       PTS EIIA type-1 #.
FT   ACT_SITE     53     53       Tele-phosphohistidine intermediate; for
FT                                EIIA activity (By similarity).
FT   Condition: H
XX
Warn: This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl donor. Check DE, KW and CC DOMAIN.
Chop: Nter=0; Cter=0;
Size: 105;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P09323;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.11  2009/02/27
//
AC   PRU00417;
DC   Domain;
TR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1; level=0
XX
Names: PTS EIIA type-2 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
DE   + RecName: EC=2.7.1.-;
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
CC       histidyl residue. Then, it transfers the phosphoryl group to the
CC       EIIB domain.
CC   -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine +
CC       protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine.
CC   -!- SIMILARITY: Contains # PTS EIIA type-2 domain.
end case
XX
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1; trigger=no
XX
GO   GO:0016740; F:transferase activity
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Phosphoprotein
KW   Phosphotransferase system
KW   Transferase
end case
FT   From: PS51094
FT   DOMAIN     from     to       PTS EIIA type-2 #.
case <AnyFeature:PS51099:7=C> or <AnyFeature:PS51350:15=H>
FT   ACT_SITE     61     61       Tele-phosphohistidine intermediate; for
FT                                EIIA activity (By similarity).
FT   Condition: H
else
FT   ACT_SITE     61     61       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   Condition: H
end case
XX
Warn: This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl. Check DE, KW , FT and CC DOMAIN.
Chop: Nter=0; Cter=0;
Size: 142;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P44715;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.11  2009/02/27
//
AC   PRU00418;
DC   Domain;
TR   PROSITE; PS51095; PTS_EIIA_TYPE_3; 1; level=0
XX
Names: PTS EIIA type-3 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
DE   + RecName: EC=2.7.1.-;
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
CC       histidyl residue. Then, it transfers the phosphoryl group to the
CC       EIIB domain.
CC   -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine +
CC       protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine.
CC   -!- SIMILARITY: Contains # PTS EIIA type-3 domain.
end case
XX
DR   PROSITE; PS51095; PTS_EIIA_TYPE_3; 1; trigger=no
XX
GO   GO:0016740; F:transferase activity
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Phosphoprotein
KW   Phosphotransferase system
KW   Transferase
end case
FT   From: PS51095
FT   DOMAIN     from     to       PTS EIIA type-3 #.
FT   MOD_RES      75     75       Phosphohistidine (by HPr) (By
FT                                similarity).
FT   Condition: H
XX
Warn: This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl. Check DE, KW, FT and CC DOMAIN.
Chop: Nter=0; Cter=0;
Size: 99;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: Q45402;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.12  2009/02/27
//
AC   PRU00419;
DC   Domain;
TR   PROSITE; PS51096; PTS_EIIA_TYPE_4; 1; level=0
XX
Names: PTS EIIA type-4 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS),
 a major carbohydrate active transport system.
XX
DE   + RecName: EC=2.7.1.-;
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- SIMILARITY: Contains # PTS EIIA type-4 domain.
end case
XX
DR   PROSITE; PS51096; PTS_EIIA_TYPE_4; 1; trigger=no
XX
GO   GO:0016301; F:kinase activity
GO   GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system
GO   GO:0016740; F:transferase activity
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Kinase
KW   Phosphotransferase system
KW   Transferase
end case
FT   From: PS51096
FT   DOMAIN     from     to       PTS EIIA type-4 #.
case <AnyFeature:PS51350:15=H> or <AnyFeature:PS51101:16=H>
FT   ACT_SITE      9      9       Tele-phosphohistidine intermediate; for
FT                                EIIA activity.
FT   Condition: H
else
FT   ACT_SITE      9      9       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   Condition: H
end case
XX
Warn: This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl. Check DE, KW, FT and CC DOMAIN.
Chop: Nter=0; Cter=0;
Size: 125;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P26379;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.12  2009/02/27
//
AC   PRU00420;
DC   Domain;
TR   PROSITE; PS51097; PTS_EIIA_TYPE_5; 1; level=0
XX
Names: PTS EIIA type-5 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
DE   + RecName: EC=2.7.1.-;
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
CC       histidyl residue. Then, it transfers the phosphoryl group to the
CC       EIIB domain.
CC   -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine +
CC       protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine.
CC   -!- SIMILARITY: Contains # PTS EIIA type-5 domain.
end case
XX
DR   PROSITE; PS51097; PTS_EIIA_TYPE_5; 1; trigger=no
XX
GO   GO:0016740; F:transferase activity
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Phosphoprotein
KW   Phosphotransferase system
KW   Transferase
end case
FT   From: PS51097
FT   DOMAIN     from     to       PTS EIIA type-5 #.
FT   MOD_RES      41     41       Phosphohistidine (by HPr) (By
FT                                similarity).
FT   Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 114;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P05706;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.10  2009/02/27
//
AC   PRU00421;
DC   Domain;
TR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1; level=0
XX
Names: PTS EIIB type-1 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
DE   + RecName: EC=2.7.1.69;
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- SIMILARITY: Contains # PTS EIIB type-1 domain.
end case
XX
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1; trigger=no
XX
GO   GO:0016301; F:kinase activity
GO   GO:0016740; F:transferase activity
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Kinase
KW   Phosphotransferase system
KW   Transferase
end case
FT   From: PS51098
FT   DOMAIN     from     to       PTS EIIB type-1 #.
FT   ACT_SITE     23     23       Phosphocysteine intermediate; for EIIB
FT                                activity (By similarity).
FT   Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 82;
Related: none;
Repeats: 1-2;
Topology: Undefined;
Example: P69789;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.13  2009/02/27
//
AC   PRU00422;
DC   Domain;
TR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1; level=0
XX
Names: PTS EIIB type-2 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
DE   + RecName: EC=2.7.1.69;
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- SIMILARITY: Contains # PTS EIIB type-2 domain.
end case
XX
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1; trigger=no
XX
GO   GO:0016740; F:transferase activity
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Phosphoprotein
KW   Phosphotransferase system
KW   Transferase
end case
FT   From: PS51099
FT   DOMAIN     from     to       PTS EIIB type-2 #.
FT   MOD_RES       7      7       Phosphocysteine (by EIIA) (By
FT                                similarity).
FT   Condition: C
XX
Warn: This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl. Check DE, KW, CC, FT DOMAIN AND CC CATALYTIC ACTIVITY.
Chop: Nter=0; Cter=0;
Size: 98;
Related: none;
Repeats: 1-2;
Topology: Undefined;
Example: P20966;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.11  2009/02/27
//
AC   PRU00423;
DC   Domain;
TR   PROSITE; PS51100; PTS_EIIB_TYPE_3; 1; level=0
XX
Names: PTS EIIB type-3 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
DE   + RecName: EC=2.7.1.69;
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- SIMILARITY: Contains # PTS EIIB type-3 domain.
end case
XX
DR   PROSITE; PS51100; PTS_EIIB_TYPE_3; 1; trigger=no
XX
GO   GO:0016740; F:transferase activity
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Phosphoprotein
KW   Phosphotransferase system
KW   Transferase
end case
FT   From: PS51100
FT   DOMAIN     from     to       PTS EIIB type-3 #.
FT   MOD_RES       8      8       Phosphocysteine (by EIIA) (By
FT                                similarity).
FT   Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 106;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P55901;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.12  2009/02/27
//
AC   PRU00424;
DC   Domain;
TR   PROSITE; PS51101; PTS_EIIB_TYPE_4; 1; level=0
XX
Names: PTS EIIB type-4 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
DE   + RecName: EC=2.7.1.69;
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- SIMILARITY: Contains # PTS EIIB type-4 domain.
end case
XX
DR   PROSITE; PS51101; PTS_EIIB_TYPE_4; 1; trigger=no
XX
GO   GO:0016740; F:transferase activity
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Phosphoprotein
KW   Phosphotransferase system
KW   Transferase
end case
FT   From: PS51101
FT   DOMAIN     from     to       PTS EIIB type-4 #.
FT   MOD_RES      16     16       Phosphohistidine (by EIIA) (By
FT                                similarity).
FT   Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 166;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P26380;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.11  2009/02/27
//
AC   PRU00425;
DC   Domain;
TR   PROSITE; PS51102; PTS_EIIB_TYPE_5; 1; level=0
XX
Names: PTS_EIIB type-5 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
DE   + RecName: EC=2.7.1.69;
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- SIMILARITY: Contains # PTS EIIB type-5 domain.
end case
XX
DR   PROSITE; PS51102; PTS_EIIB_TYPE_5; 1; trigger=no
XX
GO   GO:0016740; F:transferase activity
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Phosphoprotein
KW   Phosphotransferase system
KW   Transferase
end case
FT   From: PS51102
FT   DOMAIN     from     to       PTS EIIB type-5 #.
FT   MOD_RES      72     72       Phosphocysteine (by EIIA) (Potential).
FT   Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 192;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: O32333;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.14  2009/02/27
//
AC   PRU00426;
DC   Domain;
TR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1; level=0
XX
Names: PTS EIIC type-1 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC       and contains the specific substrate-binding site.
CC   -!- SIMILARITY: Contains # PTS EIIC type-1 domain.
end case
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (Potential).
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else case <OC:Archaea> and defined <Property:Membrane>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
end case
XX
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1; trigger=no
DR   General; Transmembrane; -; 6-10; trigger=yes
XX
GO   GO:0051119; F:sugar transporter activity
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
GO   GO:0005886; C:plasma membrane
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
GO   GO:0005886; C:plasma membrane
else case <OC:Archaea> and defined <Property:Membrane>
GO   GO:0005886; C:plasma membrane
else
GO   GO:0016020; C:membrane
end case
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Phosphotransferase system
KW   Transport
KW   Sugar transport
KW   Transmembrane
KW   Membrane
end case
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
end case
FT   From: PS51103
FT   DOMAIN     from     to       PTS EIIC type-1 #.
XX
Chop: Nter=0; Cter=0;
Size: 369-380;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P09323;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.17  2008/09/29
//
AC   PRU00427;
DC   Domain;
TR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1; level=0
XX
Names: PTS EIIC type-2 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC       and contains the specific substrate-binding site.
CC   -!- SIMILARITY: Contains # PTS EIIC type-2 domain.
end case
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (Potential).
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else case <OC:Archaea> and defined <Property:Membrane>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
end case
XX
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1; trigger=no
DR   General; Transmembrane; -; 6-8; trigger=yes
XX
GO   GO:0051119; F:sugar transporter activity
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
GO   GO:0005886; C:plasma membrane
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
GO   GO:0005886; C:plasma membrane
else case <OC:Archaea> and defined <Property:Membrane>
GO   GO:0005886; C:plasma membrane
else
GO   GO:0016020; C:membrane
end case
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Transport
KW   Sugar transport
KW   Phosphotransferase system
KW   Transmembrane
KW   Membrane
end case
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
end case
FT   From: PS51104
FT   DOMAIN     from     to       PTS EIIC type-2 #.
XX
Chop: Nter=0; Cter=0;
Size: 352;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P42956;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.18  2008/09/29
//
AC   PRU00428;
DC   Domain;
TR   PROSITE; PS51105; PTS_EIIC_TYPE_3; 1; level=0
XX
Names: PTS EIIC type-3 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC       and contains the specific substrate-binding site.
CC   -!- SIMILARITY: Contains # PTS EIIC type-3 domain.
end case
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (Potential).
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else case <OC:Archaea> and defined <Property:Membrane>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
end case
XX
DR   PROSITE; PS51105; PTS_EIIC_TYPE_3; 1; trigger=no
DR   General; Transmembrane; -; 6-8; trigger=yes
XX
GO   GO:0051119; F:sugar transporter activity
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
GO   GO:0005886; C:plasma membrane
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
GO   GO:0005886; C:plasma membrane
else case <OC:Archaea> and defined <Property:Membrane>
GO   GO:0005886; C:plasma membrane
else
GO   GO:0016020; C:membrane
end case
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Transport
KW   Sugar transport
KW   Phosphotransferase system
KW   Transmembrane
KW   Membrane
end case
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
end case
FT   From: PS51105
FT   DOMAIN     from     to       PTS EIIC type-3 #.
XX
Warn: This domain can be found in association with EAL domain, in these cases it may have an other function. Check DE and CC DOMAIN.
Chop: Nter=0; Cter=0;
Size: 407;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: Q45400;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.18  2008/09/29
//
AC   PRU00429;
DC   Domain;
TR   PROSITE; PS51106; PTS_EIIC_TYPE_4; 1; level=0
XX
Names: PTS EIIC type-4 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC       and contains the specific substrate-binding site.
CC   -!- SIMILARITY: Contains # PTS EIIC type-4 domain.
end case
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (Potential).
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else case <OC:Archaea> and defined <Property:Membrane>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
end case
XX
DR   PROSITE; PS51106; PTS_EIIC_TYPE_4; 1; trigger=no
DR   General; Transmembrane; -; 6-8; trigger=yes
XX
GO   GO:0051119; F:sugar transporter activity
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
GO   GO:0005886; C:plasma membrane
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
GO   GO:0005886; C:plasma membrane
else case <OC:Archaea> and defined <Property:Membrane>
GO   GO:0005886; C:plasma membrane
else
GO   GO:0016020; C:membrane
end case
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Transport
KW   Sugar transport
KW   Phosphotransferase system
KW   Transmembrane
KW   Membrane
end case
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
end case
FT   From: PS51106
FT   DOMAIN     from     to       PTS EIIC type-4 #.
XX
Chop: Nter=0; Cter=0;
Size: 234;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P26381;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.17  2008/09/29
//
AC   PRU00430;
DC   Domain;
TR   PROSITE; PS51107; PTS_EIIC_TYPE_5; 1; level=0
XX
Names: PTS EIIC type-5 domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC       and contains the specific substrate-binding site.
CC   -!- SIMILARITY: Contains # PTS EIIC type-5 domain.
end case
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (Potential).
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else case <OC:Archaea> and defined <Property:Membrane>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
end case
XX
DR   PROSITE; PS51107; PTS_EIIC_TYPE_5; 1; trigger=no
DR   General; Transmembrane; -; 6-8; trigger=yes
XX
GO   GO:0051119; F:sugar transporter activity
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
GO   GO:0005886; C:plasma membrane
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
GO   GO:0005886; C:plasma membrane
else case <OC:Archaea> and defined <Property:Membrane>
GO   GO:0005886; C:plasma membrane
else
GO   GO:0016020; C:membrane
end case
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
GO   GO:0005886; C:plasma membrane
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
GO   GO:0005886; C:plasma membrane
else case <OC:Archaea> and defined <Property:Membrane>
GO   GO:0005886; C:plasma membrane
else
GO   GO:0016020; C:membrane
end case
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
GO   GO:0005886; C:plasma membrane
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
GO   GO:0005886; C:plasma membrane
else case <OC:Archaea> and defined <Property:Membrane>
GO   GO:0005886; C:plasma membrane
else
GO   GO:0016020; C:membrane
end case
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Transport
KW   Sugar transport
KW   Phosphotransferase system
KW   Transmembrane
KW   Membrane
end case
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
end case
FT   From: PS51107
FT   DOMAIN     from     to       PTS EIIC type-5 #.
XX
Chop: Nter=0; Cter=0;
Size: 187;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: O32332;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.19  2008/09/29
//
AC   PRU00431;
DC   Domain;
TR   PROSITE; PS51108; PTS_EIID; 1; level=0
XX
Names: PTS EIID domain
Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system.
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- DOMAIN: The EIID domain, with its homologous EIIC domain, forms
CC       the PTS system translocation channel and contains part of its
CC       specific substrate-binding site.
CC   -!- SIMILARITY: Contains # PTS EIID domain.
end case
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (Potential).
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else case <OC:Archaea> and defined <Property:Membrane>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
else
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
end case
XX
DR   PROSITE; PS51108; PTS_EIID; 1; trigger=no
DR   General; Transmembrane; -; 2-6; trigger=yes
XX
GO   GO:0051119; F:sugar transporter activity
case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=2>
GO   GO:0005886; C:plasma membrane
else case <OC:Bacteria> and defined <Property:Membrane> and <Property:Membrane=1>
GO   GO:0005886; C:plasma membrane
else case <OC:Archaea> and defined <Property:Membrane>
GO   GO:0005886; C:plasma membrane
else
GO   GO:0016020; C:membrane
end case
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Phosphotransferase system
KW   Transport
KW   Sugar transport
KW   Transmembrane
KW   Membrane
end case
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
end case
FT   From: PS51108
FT   DOMAIN     from     to       PTS EIID #.
XX
Chop: Nter=0; Cter=0;
Size: 265;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: P26382;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.18  2008/09/29
//
AC   PRU00432;
DC   Domain;
TR   PROSITE; PS51113; ZF_BTK; 1; level=0
XX
Names: Zinc finger Btk-type
 Btk Motif (BM)
Function: The Btk-type zinc finger is a domain of ~37 amino acids present in
 eukaryotic signalling proteins.
XX
CC   -!- SIMILARITY: Contains # Btk-type zinc finger.
XX
KW   Zinc-finger
case <Feature:PS51113:9=[CH]> and <Feature:PS51113:20=[CH]> and <Feature:PS51113:21=[CH]> and <Feature:PS51113:31=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS51113
case <Feature:PS51113:9=[H]> and <Feature:PS51113:20=[C]> and <Feature:PS51113:21=[C]> and <Feature:PS51113:31=[C]>
FT   ZN_FING    from     to       Btk-type #.
else case <Feature:PS51113:9=[CH]> and <Feature:PS51113:20=[CH]> and <Feature:PS51113:21=[CH]> and <Feature:PS51113:31=[CH]>
FT   ZN_FING    from     to       Btk-type #; atypical.
else
FT   ZN_FING    from     to       Btk-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 30-45;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O95294;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2005/06/28
//
AC   PRU00433;
DC   Domain;
TR   PROSITE; PS51007; CYTC; 1; level=0
XX
Names: Cytochrome c domain
Function: Cytochromes c typically function in electron transfer, but c-type cytochrome
 centers are also found in the active sites of many enzymes,
XX
CC   -!- SIMILARITY: Contains # cytochrome c domain.
XX
KW   Heme
KW   Iron
KW   Metal-binding
XX
FT   From: PS51007
FT   DOMAIN     from     to       Cytochrome c #.
FT   METAL        18     18       Iron (heme #1 axial ligand) (By
FT                                similarity).
FT   Condition: H
FT   BINDING      14     14       Heme #1 (covalent) (By similarity).
FT   Group: 1; Condition: C
FT   BINDING      17     17       Heme #1 (covalent) (By similarity).
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 60-120;
Related: None;
Repeats: 3;
Topology: Undefined;
Example: P0A389;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.6  2006/12/05
//
AC   PRU00434;
DC   Domain;
TR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1-2; level=0
XX
Names: ABC transporter family domain
 ATP binding cassette domain
Function: Uses the hydrolysis of ATP to energize diverse biological systems
XX
CC   -!- SIMILARITY: Contains # ABC transporter domain.
XX
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1; trigger=no
XX
GO   GO:0043190; C:ATP-binding cassette (ABC) transporter complex
GO   GO:0006810; P:transport
GO   GO:0005524; F:ATP binding
GO   GO:0000166; F:nucleotide binding
XX
case not (<AnyFeature:MF_00205>)
KW   Transport
end case
KW   ATP-binding
KW   Nucleotide-binding
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2> and not <AnyFeature:MF_00205>
KW   Cell inner membrane
KW   Membrane
end case
case not <AnyFeature:MF_00205>
KW   Membrane
end case
XX
FT   From: PS50893
FT   DOMAIN     from     to       ABC transporter #.
FT   NP_BIND      33     40       ATP (Potential).
FT   Condition: [AG]-x(4)-G-K-[ST]
XX
Chop: Nter=0; Cter=0;
Size: 200-2438;
Related: none;
Repeats: 1-2;
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2> and not <AnyFeature:MF_00205>
Topology: Inner membrane associated;
else
Topology: Membrane associated;
end case
Example: P02915; P60752; P13569;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Plastid
 Bacteriophage
Comments: Contains ABC cassette but lost transport capability in UvrA subfamily.
XX
# Revision 1.16  2008/09/29
//
AC   PRU00435;
DC   Domain;
TR   PROSITE; PS51118; HTH_HXLR; 1; level=0
XX
Names: HxlR-type HTH domain
Function: The hxlR-type HTH domain is a domain of ~90-100 amino acids present
 in  putative transcription regulators with a winged helix-turn-helix (wHTH)
 structure.
XX
CC   -!- SIMILARITY: Contains # HTH hxlR-type DNA-binding domain.
XX
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51118
FT   DOMAIN     from     to       HTH hxlR-type #.
XX
Chop: Nter=0; Cter=0;
Size: 85-110;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: P42406;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2005/05/26
//
AC   PRU00436;
DC   Domain;
TR   PROSITE; PS51080; CTF_NFI_2; 1; level=0
XX
Names: CTF/NF-I DNA-binding domain
Function: The CTF/NF-I DNA-binding domain contains four conserved Cys
 residues, which are required for its DNA-binding activity.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the CTF/NF-I family.
CC   -!- SIMILARITY: Contains # CTF/NF-I DNA-binding domain.
XX
DR   PROSITE; PS00349; CTF_NFI_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006260; P:DNA replication
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
KW   Activator
KW   DNA-binding
KW   DNA replication
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51080
FT   DNA_BIND   from     to       CTF/NF-I #.
XX
Chop: Nter=0; Cter=0;
Size: 190-195;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q12857;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2007/06/07
//
AC   PRU00437;
DC   Domain;
TR   PROSITE; PS51109; G5; 1; level=0
XX
Names: G5 domain
Function: The G5 domain may confer localization or substrate specificity on
 the proteins in which it is found.
XX
CC   -!- SIMILARITY: Contains # G5 domain.
XX
FT   From: PS51109
FT   DOMAIN     from     to       G5 #.
XX
Chop: Nter=0; Cter=0;
Size: 75-90;
Related: None;
Repeats: 1-7;
Topology: Cytoplasmic;
Example: P37546;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.1  2005/05/06
//
AC   PRU00438;
DC   Domain;
TR   PROSITE; PS51075; MH1; 1; level=0
XX
Names: MAD homology domain 1 (MH1)
Function: The MH1 domain has a role in DNA binding and negatively regulates
 the functions of MH2 domain.
XX
CC   -!- SIMILARITY: Contains # MH1 (MAD homology 1) domain.
XX
FT   From: PS51075
FT   DOMAIN     from     to       MH1 #.
XX
Chop: Nter=0; Cter=0;
Size: 120-170;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q99717;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/05/06
//
AC   PRU00439;
DC   Domain;
TR   PROSITE; PS51076; MH2; 1; level=0
XX
Names: MAD homology domain 2 (MH2)
Function: The MH2 domain is responsible for transactivation and mediates
 phosphorylation-triggered heteromeric assembly between Smad4 and R-Smad.
XX
CC   -!- SIMILARITY: Contains # MH2 (MAD homology 2) domain.
XX
case <Feature:PS51076:192-195=S-S-X-S>
KW   Phosphoprotein
end case
FT   From: PS51076
FT   DOMAIN     from     to       MH2 #.
case <Feature:PS51076:192-195=S-S-X-S>
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   MOD_RES     195    195       Phosphoserine (By similarity).
end case
XX
Chop: Nter=0; Cter=0;
Size: 160-235;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q99717;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2007/10/13
//
AC   PRU00440;
DC   Domain;
TR   PROSITE; PS51119; TAFH; 1; level=0
XX
Names: TAFH/NHR1 domain
 TAF homology
 Nervy homology region 1
 domain I
 TAF110 domain
Function: The TAF homology (TAFH) or Nervy homology region 1 (NHR1) domain is
 a domain of 95-100 amino acids present in eukaryotic proteins of the MTG/ETO
 family and whereof the core ~75-80 residues occur in TAF proteins.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # TAFH (NHR1) domain.
XX
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51119
FT   DOMAIN     from     to       TAFH #.
XX
Chop: Nter=0; Cter=0;
Size: 90-110;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q06455;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.7  2008/04/08
//
AC   PRU00441;
DC   Domain;
TR   PROSITE; PS50928; ABC_TM1; 0-1; level=0
TR   PROSITE; PS50929; ABC_TM1F; 0-1; level=0
XX
Names: ABC transporter integral membrane type-1 domain
 ATP binding cassette superfamily
Function:  ABC transporter integral membrane type-1 domain profile
XX
CC   -!- SIMILARITY: Contains # ABC transmembrane type-1 domain.
XX
DR   General; Transmembrane; -; 4-7; trigger=yes
XX
GO   GO:0043190; C:ATP-binding cassette (ABC) transporter complex
GO   GO:0016021; C:integral to membrane
GO   GO:0006810; P:transport
XX
KW   Transmembrane
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
KW   Membrane
end case
XX
FT   From: any
FT   DOMAIN     from     to       ABC transmembrane type-1 #.
XX
Chop: Nter=0; Cter=0;
Size: 200-2438;
Related: none;
Repeats: 1-2;
case <OC:Bacteria> or <OC:Archaea> and defined <Property:Membrane> and <Property:Membrane=2>
Topology: Inner membrane associated;
else
Topology: Membrane associated;
end case
Example: P68183; P02915; P60752; P13569;
Scope:
 Bacteria
 Archaea
 Plastid
 Bacteriophage
Comments: The domain associated with the profile PS50929 TM1F is always found fused to the ABC transporter domain.
XX
# Revision 1.6  2008/09/29
//
AC   PRU00442;
DC   Domain;
TR   PROSITE; PS51012; ABC_TM2; 1; level=0
XX
Names: ABC transporter integral membrane type-2 family domain
 ATP binding cassette superfamily
Function:  ABC transporter integral membrane type-2 domain profile
XX
CC   -!- SIMILARITY: Contains # ABC transmembrane type-2 domain.
XX
GO   GO:0043190; C:ATP-binding cassette (ABC) transporter complex
GO   GO:0016021; C:integral to membrane
GO   GO:0006810; P:transport
XX
KW   Transmembrane
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
KW   Membrane
end case
XX
FT   From: PS51012
FT   DOMAIN     from     to       ABC transmembrane type-2 #.
XX
Chop: Nter=0; Cter=0;
Size: 200-400;
Related: none;
Repeats: 1-2;
case <OC:Bacteria> or <OC:Archaea> and defined <Property:Membrane> and <Property:Membrane=2>
Topology: Inner membrane associated;
else
Topology: Membrane associated;
end case
Example: O52619;
Scope:
 Bacteria
 Archaea
 Plastid
Comments: None.
XX
# Revision 1.8  2009/12/22
//
AC   PRU00443;
DC   Domain;
TR   PROSITE; PS51121; NTA; 1; level=0
XX
Names: NtA (N-terminal agrin) domain
Function: The NtA domain is a region of 135 amino acids required for the
 localization of agrin to synaptic basal lamina and other basement membranes.
XX
CC   -!- SIMILARITY: Contains # NtA (N-terminal agrin) domain.
XX
KW   Alternative splicing
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51121
FT   DOMAIN     from     to       NtA #.
FT   DISULFID      2     74       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 120-150;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O00468;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/09
//
AC   PRU00444;
DC   Domain;
TR   PROSITE; PS51124; PEPTIDASE_C16; 1-2; level=0
XX
Names: Peptidase family C16 domain
Function: Peptidase family C16 contains polyprotein processing endopeptidases from coronaviruses.
XX
case (<Feature:PS51124:39=C> and <Feature:PS51124:198=H>)
DE   + RecName: EC=3.4.22.-;
end case
CC   -!- SIMILARITY: Contains # peptidase C16 domain.
XX
DR   PROSITE; PS51124; PEPTIDASE_C16; 1; trigger=no
XX
case (<Feature:PS51124:39=C> and <Feature:PS51124:198=H>)
KW   Thiol protease
KW   Hydrolase
KW   Protease
end case
FT   From: PS51124
FT   DOMAIN     from     to       Peptidase C16 #.
case <Feature:PS51124:39=C>
FT   ACT_SITE     39     39       For PL#-PRO activity (By similarity).
end case
case <Feature:PS51124:198=H>
FT   ACT_SITE    198    198       For PL#-PRO activity (By similarity).
end case
case (<Feature:PS51124:117=C> and <Feature:PS51124:150=C>)
FT   ZN_FING     117    150       C4-type # (By similarity).
end case
XX
Chop: Nter=0; Cter=0;
Size: 250-260;
Related: none;
Repeats: 1-2;
Topology: Undefined;
Example: P16342;
Scope:
 Viruses
Comments: None
XX
# Revision 1.9  2009/02/27
//
AC   PRU00445;
DC   Domain;
TR   PROSITE; PS51127; BIG1; 1; level=0
XX
Names: Big-1 (Bacterial Ig-like domain 1) domain
Function: The bacterial immunoglobulin-like (Ig) domain 1 or Big-1 domain is a
 domain of ~95 amino acids present in bacterial adhesion molecules of the
 intimin/invasin family, involved in pathogenicity.
XX
CC   -!- SIMILARITY: Contains # Big-1 (Bacterial Ig-like domain 1) domain.
XX
FT   From: PS51127
FT   DOMAIN     from     to       Big-1 #.
XX
Chop: Nter=0; Cter=0;
Size: 80-110;
Related: None;
Repeats: 1-50;
Topology: Undefined;
Example: P19809;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2005/06/09
//
AC   PRU00446;
DC   Domain;
TR   PROSITE; PS51132; OLF; 1; level=0
XX
Names: olfactomedin-like domain
 OLF domain
Function: The olfactomedin-like domain is a module of ~260 residues present in
 metazoan secreted glycoproteins with a characteristic tissue-specific
 expression.
XX
CC   -!- SIMILARITY: Contains # olfactomedin-like domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51132
FT   DOMAIN     from     to       Olfactomedin-like #.
FT   DISULFID      2    184       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 240-280;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q866N2;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2009/02/09
//
AC   PRU00447;
DC   Domain;
TR   PROSITE; PS51135; CIDE_N; 1; level=0
XX
Names: CIDE-N domain
 CIDE domain
 CAD domain
 N-terminal domain (NTD)
Function: The CIDE-N domain is a ~78 amino acid protein-protein interaction
 domain in the N-terminal part of Cell death-Inducing DFF45-like Effector
 (CIDE) proteins, involved in apoptosis.
XX
CC   -!- SIMILARITY: Contains # CIDE-N domain.
XX
GO   GO:0006915; P:apoptosis
KW   Apoptosis
XX
FT   From: PS51135
FT   DOMAIN     from     to       CIDE-N #.
XX
Chop: Nter=0; Cter=0;
Size: 70-90;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O76075;
Scope:
 Eukaryota; Metazoa
 Viruses; Baculoviridae
Comments: None
XX
# Revision 1.1  2005/06/27
//
AC   PRU00448;
DC   Domain;
TR   PROSITE; PS50222; EF_HAND_2; 1; level=0
XX
Names: EF-hand
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # EF-hand domain.
XX
DR   PROSITE; PS00018; EF_HAND_1; 0-1; trigger=no
XX
case <FTGroup:1>
KW   Calcium
end case
XX
FT   From: PS50222
FT   DOMAIN     from     to       EF-hand #.
FT   CA_BIND      14     25       # (Potential).
FT   Group: 1; Condition: D-x-[DNS]-{ILVFYW}-[DENSTG]-[DNQGHRK]-{GP}-[LIVMC]-[DENQSTAGC]-x(2)-[DE]
XX
Chop: Nter=0; Cter=0;
Size: 20-45;
Related: None;
Repeats: 1-8;
Topology: Undefined;
Example: Q5R632;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.6  2006/03/22
//
AC   PRU00449;
DC   Domain;
TR   PROSITE; PS51039; ZF_AN1; 1; level=0
XX
Names: AN1-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # AN1-type zinc finger.
XX
KW   Metal-binding
KW   Zinc
KW   Zinc-finger
XX
FT   From: PS51039
FT   ZN_FING    from     to       AN1-type #.
XX
Chop: Nter=0; Cter=0;
Size: 42-45;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P53899;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/12/05
//
AC   PRU00450;
DC   Domain;
TR   PROSITE; PS50876; ZF_INTEGRASE; 1; level=0
XX
Names: Zinc finger integrase-type
Function: required for integration activity and enhances tetramerization in
 the context of the full-length integrase.
XX
CC   -!- SIMILARITY: Contains # integrase-type zinc finger.
XX
KW   Zinc-finger
case <Feature:PS50876:10=[CH]> and <Feature:PS50876:14=[CH]> and <Feature:PS50876:38=[CH]> and <Feature:PS50876:41=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS50876
case <Feature:PS50876:10=[H]> and <Feature:PS50876:14=[H]> and <Feature:PS50876:38=[C]> and <Feature:PS50876:41=[C]>
FT   ZN_FING    from     to       Integrase-type #.
else case <Feature:PS50876:10=[CH]> and <Feature:PS50876:14=[CH]> and <Feature:PS50876:38=[CH]> and <Feature:PS50876:41=[CH]>
FT   ZN_FING    from     to       Integrase-type #; atypical.
else
FT   ZN_FING    from     to       Integrase-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 30-54;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P51517;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.4  2006/07/17
//
AC   PRU00451;
DC   Domain;
TR   PROSITE; PS51036; ZF_A20; 1; level=0
XX
Names: Zinc finger A20-type
Function: Functions as a ubiquitin ligase by polyubiquitinating RIP with Lys-
 48-linked ubiquitin chains.
XX
CC   -!- SIMILARITY: Contains # A20-type zinc finger.
XX
KW   Zinc-finger
case <Feature:PS51036:7=[CH]> and <Feature:PS51036:11=[CH]> and <Feature:PS51036:23=[CH]> and <Feature:PS51036:26=[CH]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS51036
case <Feature:PS51036:7=[C]> and <Feature:PS51036:11=[C]> and <Feature:PS51036:23=[C]> and <Feature:PS51036:26=[C]>
FT   ZN_FING    from     to       A20-type #.
else case <Feature:PS51036:7=[CH]> and <Feature:PS51036:11=[CH]> and <Feature:PS51036:23=[CH]> and <Feature:PS51036:26=[CH]>
FT   ZN_FING    from     to       A20-type #. atypical.
else
FT   ZN_FING    from     to       A20-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 32-34;
Related: None;
Repeats: 1-7;
Topology: Undefined;
Example: P21580;
Scope:
 Eukaryota; Mammalia
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00452;
DC   Domain;
TR   PROSITE; PS51044; ZF_SP_RING; 1; level=0
XX
Names: Zinc finger SP-RING-type
Function: Like classical RING fingers SP-RINGs function as an E3 enzyme but
 specific for sumoylation.
XX
CC   -!- SIMILARITY: Contains # SP-RING-type zinc finger.
XX
KW   Zinc-finger
case <Feature:PS51044:32=[C]> and <Feature:PS51044:34=[H]> and <Feature:PS51044:55=[C]> and <Feature:PS51044:58=[C]>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS51044
FT   ZN_FING    from     to       SP-RING-type #.
XX
Chop: Nter=0; Cter=0;
Size: 60-85;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O54714;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2009/10/13
//
AC   PRU00453;
DC   Domain;
TR   PROSITE; PS51083; ZF_HIT; 1; level=0
XX
Names: Zinc finger HIT-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # HIT-type zinc finger.
XX
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS51083
FT   ZN_FING    from     to       HIT-type #.
XX
Chop: Nter=0; Cter=0;
Size: 26-40;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P38772;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00454;
DC   Domain;
TR   PROSITE; PS51050; ZF_CW; 1; level=0
XX
Names: Zinc finger CW-type
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # CW-type zinc finger.
XX
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS51050
FT   ZN_FING    from     to       CW-type #.
XX
Chop: Nter=0; Cter=0;
Size: 39-56;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8TE76;
Scope:
 Eukaryota; Mammalia
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00455;
DC   Domain;
TR   PROSITE; PS51081; ZF_SIAH; 1; level=0
XX
Names: Zinc finger SIAH-type
Function: substrate- and cofactor-interaction domain
XX
CC   -!- SIMILARITY: Contains # SIAH-type zinc finger.
KW   Zinc-finger
case (<Feature:PS50089:6=[CH]> and <Feature:PS50089:13=[CH]> and <Feature:PS50089:25=[CH]> and <Feature:PS50089:29=[CH]>) or (<Feature:PS50089:36=[CH]> and <Feature:PS50089:43=[CH]> and <Feature:PS50089:55=[CH]> and <Feature:PS50089:60=[CH]>)
KW   Zinc
KW   Metal-binding
end case
FT   From: PS51081
case <Feature:PS50089:6=[C]> and <Feature:PS50089:13=[C]> and <Feature:PS50089:25=[H]> and <Feature:PS50089:29=[C]> and <Feature:PS50089:36=[C]> and <Feature:PS50089:43=[C]> and <Feature:PS50089:55=[H]> and <Feature:PS50089:60=[H]>
FT   ZN_FING    from     to       SIAH-type #.
else case <Feature:PS50089:6=[CH]> and <Feature:PS50089:13=[CH]> and <Feature:PS50089:25=[CH]> and <Feature:PS50089:29=[CH]> and <Feature:PS50089:36=[CH]> and <Feature:PS50089:43=[CH]> and <Feature:PS50089:55=[CH]> and <Feature:PS50089:60=[CH]>
FT   ZN_FING    from     to       SIAH-type #; atypical.
else
FT   ZN_FING    from     to       SIAH-type #; degenerate.
end case
XX
Chop: Nter=0; Cter=0;
Size: 50-70;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8R4T2;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00456;
DC   Domain;
TR   PROSITE; PS51074; ZF_DPH; 1; level=0
XX
Names: Zinc finger DPH-type
Function: biosynthesis of diphtamide a unique post-translationally modified
 histidine residue found only in translation elongation factor 2 (eEF-2)
XX
CC   -!- SIMILARITY: Contains # DPH-type zinc finger.
XX
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS51074
FT   ZN_FING    from     to       DPH-type #.
XX
Chop: Nter=0; Cter=0;
Size: 50-75;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6VUC1;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00457;
DC   Domain;
TR   PROSITE; PS50994; INTEGRASE; 1; level=0
XX
Names: Integrase catalytic domain
Function: The integrase catalytic domain catalyzes a series of reactions to
 integrate the viral genome into a host chromosome.
XX
CC   -!- SIMILARITY: Contains # integrase catalytic domain.
case <FTGroup:1>
KW   Hydrolase
KW   Nuclease
KW   Endonuclease
KW   DNA integration
KW   DNA recombination
end case
XX
case <FTGroup:1>
GO   GO:0004518; F:nuclease activity
GO   GO:0004519; F:endonuclease activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0006310; F:DNA recombination
GO   GO:0006313; F:DNA transposition
end case
XX
FT   From: PS50994
FT   DOMAIN     from     to       Integrase catalytic #.
FT   METAL        12     12       Magnesium; catalytic (By similarity).
FT   Group: 1; Condition: D
FT   METAL        71     71       Magnesium; catalytic (By similarity).
FT   Group: 1; Condition: D
**FT   ACT_SITE    107    107       Integrase (By similarity).
**FT   Group: 1; Condition: E
XX
Chop: Nter=0; Cter=0;
Size: 43-217;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O92956;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.5  2008/07/29
//
AC   PRU00458;
DC   Domain;
TR   PROSITE; PS51115; LAMININ_IVA; 1; level=0
XX
Names: Laminin IV type A domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # laminin IV type A domain.
FT   From: PS51115
FT   DOMAIN     from     to       Laminin IV type A #.
XX
Chop: Nter=0; Cter=0;
Size: 167-202;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P15215;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/06/29
//
AC   PRU00459;
DC   Domain;
TR   PROSITE; PS51079; MBT; 1; level=0
XX
Names: MBT domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # MBT repeat.
FT   From: PS51079
FT   REPEAT     from     to       MBT #.
XX
Chop: Nter=0; Cter=0;
Size: 94-105;
Related: None;
Repeats: 2-4;
Topology: Undefined;
Example: Q9UHJ3;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/06/29
//
AC   PRU00460;
DC   Domain;
TR   PROSITE; PS50027; EGF_LAM_2; 1; level=0
XX
Names: Laminin EGF-like domain
Function: binding basement membranes proteins
XX
CC   -!- SIMILARITY: Contains # laminin EGF-like domain.
KW   Laminin EGF-like domain
case <FTTag:disulf>
KW   Disulfide bond
end case
FT   From: PS50027
FT   DOMAIN     from     to       Laminin EGF-like #.
FT   DISULFID      1     13       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      3     20       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     22     31       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     34     48       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 3-91;
Related: None;
Repeats: 1-23;
Topology: Undefined;
Example: Q9R1A3;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.4  2009/02/09
//
AC   PRU00461;
DC   Domain;
TR   PROSITE; PS51120; LDLRB; 1; level=0
XX
Names: LDL-receptor class B repeat
Function: important for ligand release and recycling of the receptor
XX
CC   -!- SIMILARITY: Contains # LDL-receptor class B repeat.
FT   From: PS51120
FT   REPEAT     from     to       LDL-receptor class B #.
XX
Chop: Nter=0; Cter=0;
Size: 36-56;
Related: None;
Repeats: 4-37;
Topology: Undefined;
Example: P01133;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/06/30
//
AC   PRU00462;
DC   Domain;
TR   PROSITE; PS51116; LAMININ_IVB; 1; level=0
XX
Names: Laminin IV type B
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # laminin IV type B domain.
FT   From: PS51116
FT   DOMAIN     from     to       Laminin IV type B #.
XX
Chop: Nter=0; Cter=0;
Size: 200-225;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q61292;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/06/30
//
AC   PRU00463;
DC   Domain;
TR   PROSITE; PS50998; GLA_2; 1; level=0
XX
Names: Gla domain
Function: a membrane binding motif which, in the presence of calcium ions, interacts with phospholipid membranes that include phosphatidylserine
XX
case <FTGroup:1>  or <FTGroup:2>
CC   -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K
CC       dependent carboxylation. These residues are essential for the
CC       binding of calcium.
CC   -!- SIMILARITY: Contains # Gla (gamma-carboxy-glutamate) domain.
end case
DR   PROSITE; PS00011; GLA_1; 1; trigger=no
XX
case <FTGroup:1>  or <FTGroup:2>
GO   GO:0005509; F:calcium ion binding
end case
XX
case <FTGroup:1>  or <FTGroup:2>
KW   Calcium
KW   Gamma-carboxyglutamic acid
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50998
FT   DOMAIN     from     to       Gla #.
FT   MOD_RES      21     21       4-carboxyglutamate (By similarity).
FT   Group: 1; Condition: E
FT   MOD_RES      24     24       4-carboxyglutamate (By similarity).
FT   Group: 2; Condition: E
FT   DISULFID     18     23       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     23     29       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 17-45;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P84349;
Scope:
 Eukaryota; Gnathostomata
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00464;
DC   Domain;
TR   PROSITE; PS51084; HIT_2; 1; level=0
XX
Names: HIT
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # HIT domain.
FT   From: PS51084
FT   DOMAIN     from     to       HIT #.
XX
Chop: Nter=0; Cter=0;
Size: 26-132;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9BGQ0;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2005/06/30
//
AC   PRU00465;
DC   Domain;
TR   PROSITE; PS51085; 2FE2S_FER_2; 1; level=0
XX
Names: 2Fe-2S ferredoxin-type domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # 2Fe-2S ferredoxin-type domain.
XX
case <FTGroup:1>
KW   2Fe-2S
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
end case
XX
FT   From: PS51085
FT   DOMAIN     from     to       2Fe-2S ferredoxin-type #.
FT   METAL        37     37       Iron-sulfur (2Fe-2S) (By similarity).
FT   Group: 1; Condition: C
FT   METAL        42     42       Iron-sulfur (2Fe-2S) (By similarity).
FT   Group: 1; Condition: C
FT   METAL        45     45       Iron-sulfur (2Fe-2S) (By similarity).
FT   Group: 1; Condition: C
FT   METAL        72     72       Iron-sulfur (2Fe-2S) (By similarity).
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 25-116;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P81372;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2006/07/05
//
AC   PRU00466;
DC   Domain;
TR   PROSITE; PS51117; LAMININ_NTER; 1; level=0
XX
Names: Laminin N-terminal domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # laminin N-terminal domain.
FT   From: PS51117
FT   DOMAIN     from     to       Laminin N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 200-225;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q61292;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2005/09/09
//
AC   PRU00467;
DC   Domain;
TR   PROSITE; PS51112; AMMECR1; 1; level=0
XX
Names: AMMECR1 domain
Function: The high level of conservation of the AMMECR1 domain points to a
 basic cellular function, potentially in either the transcription,
 replication, repair or translation machinery.
XX
CC   -!- SIMILARITY: Contains # AMMECR1 domain.
XX
FT   From: PS51112
FT   DOMAIN     from     to       AMMECR1 #.
XX
Chop: Nter=0; Cter=0;
Size: 170-230;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y4X0;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2005/07/15
//
AC   PRU00468;
DC   Domain;
TR   PROSITE; PS51140; CUE; 1; level=0
XX
Names: CUE domain
Function: The Coupling of Ubiquitin conjugation to ER degradation or CUE
 domain can bind monoubiquitin and can be required for ubiquitination of the
 protein in which it is found.
XX
CC   -!- SIMILARITY: Contains # CUE domain.
XX
GO   GO:0006512; P:ubiquitin cycle
KW   Ubl conjugation pathway
XX
FT   From: PS51140
FT   DOMAIN     from     to       CUE #.
XX
Chop: Nter=0; Cter=0;
Size: 35-50;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P54787;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/07/19
//
AC   PRU00469;
DC   Domain;
TR   PROSITE; PS51134; ZF_TFIIB; 1; level=0
XX
Names: Zinc finger TFIIB-type
Function: The zinc finger contacts the rbp1 subunit of Pol II through its dock
 domain
XX
CC   -!- SIMILARITY: Contains # TFIIB-type zinc finger.
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS51134
FT   ZN_FING    from     to       TFIIB-type #.
XX
Chop: Nter=0; Cter=0;
Size: 18-33;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q00403;
Scope:
 Eukaryota
 Archaea
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00470;
DC   Domain;
TR   PROSITE; PS51141; ZF_SBP; 1; level=0
XX
Names: Zinc finger SBP-type
Function: DNA-binding
XX
CC   -!- SIMILARITY: Contains # SBP-type zinc finger.
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS51141
FT   ZN_FING    from     to       SBP-type #.
XX
Chop: Nter=0; Cter=0;
Size: 76-77;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8LFW6;
Scope:
 Eukaryota; Embryophyta
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00471;
DC   Domain;
TR   PROSITE; PS51131; ZN_HOOK; 1; level=0
XX
Names: Zinc-hook domain
Function: dimerization domain
XX
CC   -!- SIMILARITY: Contains # zinc-hook domain.
KW   Zinc
KW   Metal-binding
XX
FT   From: PS51131
FT   DOMAIN     from     to       Zinc-hook #.
XX
Chop: Nter=0; Cter=0;
Size: 95-107;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P12753;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00472;
DC   Domain;
TR   PROSITE; PS51133; ZF_TFIIS_2; 1; level=0
XX
Names: Zinc finger TFIIS-type
Function:  involved in  RNA  cleavages when pol II is blocked by backtracking
XX
CC   -!- SIMILARITY: Contains # TFIIS-type zinc finger.
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS51133
FT   ZN_FING    from     to       TFIIS-type #.
XX
Chop: Nter=0; Cter=0;
Size: 39-42;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P07273;
Scope:
 Eukaryota
 Viruses
 Archaea
Comments: None
XX
# Revision 1.3  2006/07/17
//
AC   PRU00473;
DC   Domain;
TR   PROSITE; PS51123; OMPA_2; 1; level=0
XX
Names: OmpA-like domain
Function: The OmpA-like domain is thought to be responsible for non-covalent
 interactions with peptidoglycan.
XX
CC   -!- SIMILARITY: Contains # OmpA-like domain.
XX
DR   PROSITE; PS01068; OMPA_1; 1; trigger=no
XX
GO   GO:0016020; C:membrane
XX
KW   Membrane
XX
FT   From: PS51123
FT   DOMAIN     from     to       OmpA-like #.
XX
Chop: Nter=0; Cter=0;
Size: 105-140;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0A910;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.1  2005/08/10
//
AC   PRU00474;
DC   Domain;
TR   PROSITE; PS51122; CALPONIN_2; 1; level=0
XX
Names: Calponin-like repeat
Function: The calponin-like repeat is a short actin-binding module.
XX
CC   -!- SIMILARITY: Contains # calponin-like repeat.
XX
DR   PROSITE; PS01052; CALPONIN_1; 1; trigger=no
XX
GO   GO:0003779; F:actin binding
XX
KW   Actin-binding
XX
FT   From: PS51122
FT   REPEAT     from     to       Calponin-like #.
XX
Chop: Nter=0; Cter=0;
Size: 25-29;
Related: None;
Repeats: 3-7;
Topology: Cytoplasmic;
Example: P51911;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/08/10
//
AC   PRU00475;
DC   Domain;
TR   PROSITE; PS51136; WAC; 1; level=0
XX
Names: WAC domain
Function: The DNA-binding region of Acf1 includes the WAC domain, which is
 necessary for the efficient binding of ACF complex to DNA. It seems probable
 that the WAC domain will be involved in DNA binding in other related factors.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # WAC domain.
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
XX
FT   From: PS51136
FT   DOMAIN     from     to       WAC #.
XX
Chop: Nter=0; Cter=0;
Size: 105-110;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P53125;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2007/06/07
//
AC   PRU00476;
DC   Domain;
TR   PROSITE; PS51138; ENT; 1; level=0
XX
Names: EMSY N-terminal (ENT) domain
Function: The ENT domain is a ~90-residue module, which is unique in the human
 proteome, although multiple copies are found in Arabidopsis proteins.
XX
CC   -!- SIMILARITY: Contains # ENT (EMSY N-terminal) domain.
XX
FT   From: PS51138
FT   DOMAIN     from     to       ENT #.
XX
Chop: Nter=0; Cter=0;
Size: 80-100;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q7Z589;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/08/10
//
AC   PRU00477;
DC   Domain;
TR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1; level=0
XX
Names: LPXTG sorting signal motif
Function: The LPXTG motif is part of the C-terminal sorting signal found in
 surface proteins from Gram-positive cocci.
XX
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor
CC       (Potential).
XX
DR   General; Transmembrane; -; 1; trigger=no
XX
GO   GO:0005618; C:cell wall
XX
KW   Cell wall
KW   Peptidoglycan-anchor
XX
FT   From: PS50847
FT   PROPEP        5   Cter       Removed by sortase (Potential).
FT   MOTIF      from      5       LPXTG sorting signal (Potential).
FT   MOD_RES       4      4       Pentaglycyl murein peptidoglycan amidated
FT                                threonine (Potential).
XX
Chop: Nter=0; Cter=0;
Size: 30-40;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P13050;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.6  2007/07/06
//
AC   PRU00478;
DC   Domain;
TR   PROSITE; PS51091; FN1_2; 1; level=0
XX
Names: FN1 domain
Function: In human tissue plasminogen activator chain A, the FN1 domain together with the following EGF-like domain are involved in fibrin-binding
XX
CC   -!- SIMILARITY: Contains # fibronectin type-I domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51091
FT   DOMAIN     from     to       Fibronectin type-I #.
FT   DISULFID      3     32       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     30     42       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 30-60;
Related: None;
Repeats: 12;
Topology: Not cytoplasmic;
Example: P00748;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00479;
DC   Domain;
TR   PROSITE; PS51092; FN2_2; 1; level=0
XX
Names: FN2 domain
Function: The FN2 domain is important for collagen binding.
XX
CC   -!- SIMILARITY: Contains # fibronectin type-II domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51092
FT   DOMAIN     from     to       Fibronectin type-II #.
FT   DISULFID      6     32       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     20     47       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 30-60;
Related: None;
Repeats: 3;
Topology: Not cytoplasmic;
Example: P00748;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00480;
DC   Domain;
TR   PROSITE; PS51130; PDXT_SNO_2; 1; level=0
XX
Names: PdxT/SNO family
Function: PdxS/SNZ and pdxT/SNO proteins form a complex which serves as a
 glutamine amidotransferase to supply ammonia as a source of the ring nitrogen
 of vitamin B6. PdxT/SNO appear to encode the glutaminase subunit, which
 produces ammonia from glutamine.
XX
case <Feature:PS51130:79=C>
DE   RecName: Full=Probable glutamine amidotransferase;
DE            EC=2.6.-.-;
end case
XX
CC   -!- SIMILARITY: Belongs to the glutamine amidotransferase pdxT/SNO
CC       family.
XX
DR   PROSITE; PS01236; PDXT_SNO_1; 1; trigger=no
XX
case <Feature:PS51130:79=C>
GO   GO:0006541; P:glutamine metabolism
GO   GO:0016740; F:transferase activity
end case
case <OC:Eukaryota> and <Feature:PS51130:79=C>
GO   GO:0008615; P:pyridoxine biosynthesis
end case
XX
case <Feature:PS51130:79=C>
KW   Glutamine amidotransferase
KW   Transferase
end case
case <OC:Bacteria> or <OG:Archaea>
KW   Pyridoxal phosphate
end case
case <OC:Eukaryota>
KW   Pyridoxine biosynthesis
end case
XX
FT   From: PS51130
FT   ACT_SITE     79     79       Nucleophile (By similarity).
FT   Condition: C
case <Feature:PS51130:79=C>
FT   ACT_SITE    176    176       By similarity.
FT   Condition: H
FT   ACT_SITE    178    178       By similarity.
FT   Condition: E
end case
FT   BINDING     111    111       Glutamine (Potential).
FT   Condition: R
XX
Chop: Nter=0; Cter=0;
Size: 170-215;
Related: PRU00605; PRU00606;
Repeats: 1;
Topology: Undefined;
Example: Q03144;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.4  2008/06/07
//
AC   PRU00481;
DC   Domain;
TR   PROSITE; PS51129; PDXS_SNZ_2; 1; level=0
XX
Names: PdxS/SNZ family
Function: PdxS/SNZ and pdxT/SNO proteins form a complex which serves as a
 glutamine amidotransferase to supply ammonia as a source of the ring nitrogen
 of vitamin B6. PdxS/SNZ appear to encode the synthase subunit which combines
 ammonia with five- and three-carbon phosphosugars to form vitamin B6.
XX
CC   -!- SIMILARITY: Belongs to the pdxS/SNZ family.
XX
DR   PROSITE; PS01235; PDXS_SNZ_1; 1; trigger=no
XX
Chop: Nter=0; Cter=0;
Size: 275-325;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q03148;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2005/08/26
//
AC   PRU00482;
DC   Domain;
TR   PROSITE; PS51114; FBA; 1; level=0
XX
Names: F-box-associated (FBA) domain
Function: The FBA domain is likely to be a glycoprotein-binding module.
XX
CC   -!- SIMILARITY: Contains # FBA (F-box associated) domain.
XX
FT   From: PS51114
FT   DOMAIN     from     to       FBA #.
XX
Chop: Nter=0; Cter=0;
Size: 150-185;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q80UW2;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/08/26
//
AC   PRU00483;
DC   Domain;
TR   PROSITE; PS51137; VM; 1; level=0
XX
Names: VM domain
Function: The VM domain is a 38-amino acid module found in Drosophila
 melanogaster vitelline membrane (VM) proteins.
XX
CC   -!- SIMILARITY: Contains # VM domain.
XX
FT   From: PS51137
FT   DOMAIN     from     to       VM #.
XX
Chop: Nter=0; Cter=0;
Size: 35-40;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P11449;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2005/08/26
//
AC   PRU00484;
DC   Domain;
TR   PROSITE; PS51139; GTF2I; 1; level=0
XX
Names: GTF2I-like repeat
Function: The GTF2I-like repeats are specific to the TFII-I family of
 transcription factors and are likely to be involved in DNA binding.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the TFII-I family.
CC   -!- SIMILARITY: Contains # GTF2I-like repeat.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51139
FT   REPEAT     from     to       GTF2I-like #.
XX
Chop: Nter=0; Cter=0;
Size: 90-100;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: Q9UHL9;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.4  2007/06/07
//
AC   PRU00485;
DC   Domain;
TR   PROSITE; PS51145; ZU5; 1; level=0
XX
Names: ZU5 domain
 ZU-5 domain
Function: The ZU5 domain is a domain of 90-110 residues present in Zona
 Occludens 1 (ZO-1) protein, in Unc5-like netrin receptors and in ankyrins.
XX
CC   -!- SIMILARITY: Contains # ZU5 domain.
XX
FT   From: PS51145
FT   DOMAIN     from     to       ZU5 #.
XX
Chop: Nter=0; Cter=0;
Size: 85-130;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q26261;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/09/01
//
AC   PRU00487;
DC   Domain;
TR   PROSITE; PS51146; KAIC; 1; level=0
XX
Names: KaiC domain
Function: The kaiC domain is a ~240 residue domain of the cyanobacterial
 circadian (daily) clock protein kaiC and related prokaryotic proteins.
XX
CC   -!- SIMILARITY: Contains # kaiC domain.
XX
case <Feature:PS00017>
GO   GO:0005524; F:ATP binding
GO   GO:0000166; F:nucleotide binding
KW   ATP-binding
KW   Nucleotide-binding
end case
XX
FT   From: PS51146
FT   DOMAIN     from     to       KaiC #.
XX
FT   From: PS00017
FT   NP_BIND    from     to       ATP # (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 220-260;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q79PF4;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2005/09/15
//
AC   PRU00488;
DC   Domain;
TR   PROSITE; PS51147; PFTA; 1; level=0
XX
Names: Protein prenyltransferases alpha subunit repeat
Function: Protein prenyltransferases catalyze the transfer of an isoprenyl
 moiety to a cysteine at or near the C-terminus of several eukaryotic
 proteins.
XX
DE   + RecName: EC=2.5.1.-;
XX
CC   -!- SIMILARITY: Contains # PFTA repeat.
XX
GO   GO:0004659; F:prenyltransferase activity
GO   GO:0016740; F:transferase activity
XX
KW   Prenyltransferase
KW   Transferase
XX
FT   From: PS51147
FT   REPEAT    entry   exit       PFTA #.
XX
Chop: Nter=0; Cter=0;
Size: 25-40;
Related: None;
Repeats: 2-6;
Topology: Undefined;
Example: O24304;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2009/02/27
//
AC   PRU00489;
DC   Domain;
TR   PROSITE; PS51143; MT_A70; 1; level=0
XX
Names: MT-A70-like family
Function: The MT-A70-like family comprises four subfamilies with varying
 degrees of interrelatedness. One subfamily is a small group of bacterial DNA:
 m6A MTases. The other three are paralogous eukaryotic lineages, two of which
 have not been associated with MTase activity but include proteins that
 regulate mRNA levels via unknown mechanisms apparently not involving
 methylation.
XX
CC   -!- SIMILARITY: Belongs to the MT-A70-like family.
XX
Chop: Nter=0; Cter=0;
Size: 215-245;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q86U44; P25583;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2005/10/20
//
AC   PRU00490;
DC   Domain;
TR   PROSITE; PS51154; MACRO; 1; level=0
XX
Names: Macro domain
 A1pp domain
 ADRP domain
 X domain
Function: The Macro domain is a module of ~180 amino acids which can bind
 ADP-ribose, an NAD metabolite or related ligands.
XX
CC   -!- SIMILARITY: Contains # Macro domain.
XX
FT   From: PS51154
FT   DOMAIN    entry   exit       Macro #.
XX
Chop: Nter=13; Cter=0;
Size: 140-210;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q8IXQ6;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses; ssRNA positive-strand viruses, no DNA stage
 Bacteriophage
Comments: None
XX
# Revision 1.3  2007/03/27
//
AC   PRU00491;
DC   Domain;
TR   PROSITE; PS51159; CBM21; 1; level=0
XX
Names: CBM21 (carbohydrate binding type-21) domain
 Carbohydrate-Binding Module (CBM) family 21
 Starch-binding domain (SBD)
Function: The CBM21 domain is a 90-130 amino acid carbohydrate binding domain,
 present in several eukaryotic proteins implicated in glycogen metabolism.
XX
CC   -!- SIMILARITY: Contains # CBM21 (carbohydrate binding type-21)
CC       domain.
XX
FT   From: PS51159
FT   DOMAIN     from     to       CBM21 #.
XX
Chop: Nter=0; Cter=0;
Size: 85-140;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: O95685;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2005/11/14
//
AC   PRU00492;
DC   Domain;
TR   PROSITE; PS51161; ATP_CONE; 1; level=0
XX
Names: ATP-cone domain
Function: The ATP-cone domain is an ATP-binding module.
XX
CC   -!- SIMILARITY: Contains # ATP-cone domain.
XX
GO   GO:0005524; F:ATP binding
GO   GO:0000166; F:nucleotide binding
XX
KW   ATP-binding
KW   Nucleotide-binding
XX
FT   From: PS51161
FT   DOMAIN     from     to       ATP-cone #.
XX
Chop: Nter=0; Cter=0;
Size: 75-105;
Related: None;
Repeats: 1-3;
Topology: Cytoplasmic;
Example: P23921;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.1  2005/11/16
//
AC   PRU00493;
DC   Domain;
TR   PROSITE; PS51149; GLY_RADICAL_2; 1; level=0
XX
Names: Glycine radical domain
Function: The glycine radical domain is a conserved region centered around the
 glycine which, in pfl, is known to bear the free radical.
XX
CC   -!- SIMILARITY: Contains # glycine radical domain.
XX
DR   PROSITE; PS00850; GLY_RADICAL_1; 1; trigger=no
XX
case <Feature:PS51149:97=G>
KW   Organic radical
end case
XX
FT   From: PS51149
FT   DOMAIN     from     to       Glycine radical #.
FT   MOD_RES      97     97       Glycine radical (By similarity).
FT   Condition: G
XX
Chop: Nter=0; Cter=0;
Size: 115-135;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P68066;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Bacteriophage
Comments: None
XX
# Revision 1.1  2005/11/16
//
AC   PRU00494;
DC   Domain;
TR   PROSITE; PS51150; AGOUTI_2; 1; level=0
XX
Names: Agouti domain
Function: The agouti domain is a Cys-rich C-terminal module, which is
 responsible for melanocortin receptor binding activity in vitro.
XX
CC   -!- SIMILARITY: Contains # agouti domain.
XX
DR   PROSITE; PS60024; AGOUTI_1; 1; trigger=no
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51150
FT   DOMAIN     from     to       Agouti #.
FT   DISULFID      1     16       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      8     22       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     15     33       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     19     40       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     24     31       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 35-45;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: O00253;
Scope:
 Eukaryota; Metazoa; Craniata
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00495;
DC   Domain;
TR   PROSITE; PS51153; RPW8; 1; level=0
XX
Names: RPW8 domain
Function: The RPW8 domain is an ~150 amino acid module forming the N-terminus
 of a group of plant disease resistance proteins, which have a nucleotide-
 binding site (NBS) and leucine-rich repeats (LRRs).
XX
CC   -!- SIMILARITY: Contains # RPW8 domain.
XX
GO   GO:0009626; P:hypersensitive response
GO   GO:0006952; P:defense response
XX
KW   Hypersensitive response
KW   Plant defense
XX
FT   From: PS51153
FT   DOMAIN     from     to       RPW8 #.
XX
Chop: Nter=0; Cter=0;
Size: 145-155;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9FW44;
Scope:
 Eukaryota; Viridiplantae; Embryophyta
Comments: None
XX
# Revision 1.2  2005/11/17
//
AC   PRU00496;
DC   Domain;
TR   PROSITE; PS51148; AXH; 1; level=0
XX
Names: AXH domain
Function: The AXH (ataxin-1 and HMG-box protein 1) domain is a module of ~130
 amino acids, which has been suggested to be a molecular scaffold domain
 engaged in multiple protein-protein interactions and in RNA binding.
XX
CC   -!- SIMILARITY: Contains # AXH domain.
XX
FT   From: PS51148
FT   DOMAIN     from     to       AXH #.
XX
Chop: Nter=0; Cter=0;
Size: 130-145;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P54253;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/11/17
//
AC   PRU00497;
DC   Domain;
TR   PROSITE; PS51155; CHIT_BIND_RR_2; 1; level=0
XX
Names: Chitin-binding type R&R domain
Function: The chitin-binding type R&R domain is found in arthropod cuticular
 proteins.
XX
CC   -!- SIMILARITY: Contains # chitin-binding type R&R domain.
XX
DR   PROSITE; PS00233; CHIT_BIND_RR_1; 1; trigger=no
XX
GO   GO:0042302; F:structural constituent of cuticle
XX
KW   Cuticle
XX
FT   From: PS51155
FT   DOMAIN     from     to       Chitin-binding type R&R #.
XX
Chop: Nter=0; Cter=0;
Size: 60-80;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: P02839;
Scope:
 Eukaryota; Metazoa; Arthropoda
Comments: None
XX
# Revision 1.1  2005/11/17
//
AC   PRU00498;
DC   Site;
TR   PROSITE; PS00001; ASN_GLYCOSYLATION; 1; level=0
XX
Names: N-glycosylation site
Function: Unknown
XX
KW   Glycoprotein
FT   From: PS00001
FT   CARBOHYD      1      1       N-linked (GlcNAc...) (Potential).
XX
Chop: Nter=0; Cter=0;
Size: 1;
Related: None;
Repeats: unlimited;
Topology: Not cytoplasmic;
Example: P02724;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.2  2006/07/05
//
AC   PRU00499;
DC   Domain;
TR   PROSITE; PS00017; ATP_GTP_A; 1; level=0
XX
Names: ATP/GTP-binding site motif A (P-loop)
Function: This loop interacts with one of the phosphate groups of the
 nucleotide.
XX
GO   GO:0005524; F:ATP binding
GO   GO:0000166; F:nucleotide binding
XX
KW   ATP-binding
KW   Nucleotide-binding
XX
FT   From: PS00017
FT   NP_BIND    from     to       ATP (Potential).
XX
Chop: Nter=0; Cter=0;
Size: 8;
Related: None;
Repeats: unlimited;
Topology: Undefined;
Example: P19483;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.3  2007/11/29
//
AC   PRU00500;
DC   Domain;
TR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1; level=0
XX
Names: thyroglobulin type-1 domain
 Tg type-I repeat
Function: the Tg type-1 repeat is a module of about 70 amino acids present 11x
 in thyroglobulin (Tg) and as a single or repeated sequence in cysteine
 proteinase inhibitors and other proteins.
XX
CC   -!- SIMILARITY: Contains # thyroglobulin type-1 domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51162
FT   DOMAIN    entry   exit       Thyroglobulin type-1 #.
FT   DISULFID      4     23       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     34     41       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     43     63       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 40-210;
Related: None;
Repeats: 1-11;
Topology: Undefined;
Example: P24592;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00501;
DC   Domain;
TR   PROSITE; PS51158; ALPHA_KINASE; 1; level=0
XX
Names: Alpha-type protein kinase
Function: phosphorylate amino acids located within alpha-helices
XX
CC   -!- SIMILARITY: Contains # alpha-type protein kinase domain.
FT   From: PS51158
FT   DOMAIN     from     to       Alpha-type protein kinase #.
XX
Chop: Nter=0; Cter=0;
Size: 191-277;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O01991;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2006/02/02
//
AC   PRU00502;
DC   Domain;
TR   PROSITE; PS50271; ZF_UBP; 1; level=0
XX
Names: UBP-type zinc finger
Function: ubiquitin binding domain
XX
CC   -!- SIMILARITY: Contains # UBP-type zinc finger.
FT   From: PS50271
FT   ZN_FING    from     to       UBP-type #.
XX
Chop: Nter=0; Cter=0;
Size: 59-76;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q5DU02;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/11/23
//
AC   PRU00503;
DC   Domain;
TR   PROSITE; PS51126; DILUTE; 1; level=0
XX
Names: dilute domain
Function: anchors myosin V to cargoes via attachments to organelle-specific receptors
XX
CC   -!- SIMILARITY: Contains # dilute domain.
FT   From: PS51126
FT   DOMAIN     from     to       Dilute #.
XX
Chop: Nter=0; Cter=0;
Size: 213-300;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q69Z89;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/11/23
//
AC   PRU00504;
DC   Domain;
TR   PROSITE; PS51125; NHL; 1; level=0
XX
Names: NHL repeat
Function: could be involved in protein-protein interaction
XX
CC   -!- SIMILARITY: Contains # NHL repeat.
FT   From: PS51125
FT   REPEAT     from     to       NHL #.
XX
Chop: Nter=0; Cter=0;
Size: 39-52;
Related: None;
Repeats: 4-6;
Topology: Undefined;
Example: Q8CH72;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.3  2006/03/23
//
AC   PRU00505;
DC   Domain;
TR   PROSITE; PS51088; TEA_2; 1; level=0
XX
Names: TEA DNA-binding domain
Function:  DNA binding
XX
CC   -!- SIMILARITY: Contains # TEA DNA-binding domain.
FT   From: PS51088
FT   DNA_BIND   from     to       TEA #.
XX
Chop: Nter=0; Cter=0;
Size: 64-66;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P30052;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/11/23
//
AC   PRU00506;
DC   Domain;
TR   PROSITE; PS51027; INTEGRASE_DBD; 1; level=0
XX
Names: integrase-type DNA-binding domain
Function: DNA-binding
XX
CC   -!- SIMILARITY: Contains # integrase-type DNA-binding domain.
FT   From: PS51027
FT   DNA_BIND   from     to       Integrase-type #.
XX
Chop: Nter=0; Cter=0;
Size: 45-54;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q04095;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.1  2005/11/23
//
AC   PRU00507;
DC   Domain;
TR   PROSITE; PS51151; NAC_AB; 1; level=0
XX
Names: NAC-A/B (NAC-alpha/beta) domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # NAC-A/B (NAC-alpha/beta) domain.
FT   From: PS51151
FT   DOMAIN     from     to       NAC-A/B #.
XX
Chop: Nter=0; Cter=0;
Size: 30-68;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P70670;
Scope:
 Eukaryota
 Archaea
Comments: None
XX
# Revision 1.1  2005/11/23
//
AC   PRU00508;
DC   Domain;
TR   PROSITE; PS51157; ZF_UBR; 1; level=0
XX
Names: UBR-type zinc finger
Function: it binds specifically to proteins bearing N-terminal residues  that  are  destabilizing  according  to  the  N-end rule
XX
CC   -!- SIMILARITY: Contains # UBR-type zinc finger.
FT   From: PS51157
FT   ZN_FING    from     to       UBR-type #.
XX
Chop: Nter=0; Cter=0;
Size: 67-75;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O60014;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/11/23
//
AC   PRU00509;
DC   Domain;
TR   PROSITE; PS51058; ZF_CXXC; 1; level=0
XX
Names: CXXC-type zinc finger
Function: it binds specifically to non-methylated CpG
XX
CC   -!- SIMILARITY: Contains # CXXC-type zinc finger.
FT   From: PS51058
FT   ZN_FING    from     to       CXXC-type #.
XX
Chop: Nter=0; Cter=0;
Size: 6-48;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q6PCT2;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/11/23
//
AC   PRU00510;
DC   Domain;
TR   PROSITE; PS51128; ZF_DKSA_2; 1; level=0
XX
Names: dksA C4-type zinc finger
Function: it binds the RNA polymerase
XX
CC   -!- SIMILARITY: Contains # dksA C4-type zinc finger.
FT   From: PS51128
FT   ZN_FING      44     68       dksA C4-type #.
XX
Chop: Nter=0; Cter=0;
Size: 19-33;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P41059;
Scope:
 Bacteria
 Bacteriophage
Comments: None
XX
# Revision 1.4  2006/04/05
//
AC   PRU00511;
DC   Domain;
TR   PROSITE; PS51111; REJ; 1; level=0
XX
Names: REJ domain
Function: The REJ domain is an extracellular module of ~1000 amino acids,
 which might function in ion transport homeostasis.
XX
CC   -!- SIMILARITY: Contains # REJ domain.
XX
FT   From: PS51111
FT   DOMAIN     from     to       REJ #.
XX
Chop: Nter=0; Cter=0;
Size: 680-900;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q8TDX9;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2005/11/24
//
AC   PRU00512;
DC   Domain;
TR   PROSITE; PS51156; ELM2; 1; level=0
XX
Names: ELM2 domain
Function: The ELM2 (EGL-27 and MTA1 homology) domain has been shown to
 function as a transcriptional repression domain through recruitment of HDAC
 activity.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # ELM2 domain.
XX
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   Nucleus
KW   Repressor
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51156
FT   DOMAIN     from     to       ELM2 #.
XX
Chop: Nter=0; Cter=0;
Size: 85-115;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9P2K3;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.6  2008/04/08
//
AC   PRU00513;
DC   Domain;
TR   PROSITE; PS51172; CBM3; 1-3; level=0
XX
Names: CBM3 (carbohydrate binding type-3) domain
Function: Involved in the binding to crystalline cellulose.
XX
CC   -!- SIMILARITY: Contains # CBM3 (carbohydrate binding type-3) domain.
XX
DR   PROSITE; PS51172; CBM3; 1-3; trigger=no
XX
FT   From: PS51172
FT   DOMAIN     from     to       CBM3 #.
XX
Chop: Nter=0; Cter=0;
Size: 150-160;
Related: none;
Repeats: 1-3;
Topology: Undefined;
Example: Q06851; P04955; P28622;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.4  2005/12/13
//
AC   PRU00514;
DC   Domain;
TR   PROSITE; PS51167; CHORISMATE_MUT_1; 1; level=0
XX
Names: chorismate mutase aroH-type domain
 CM domain
Function: Chorismate mutase is a regulatory enzyme required for biosynthesis
 of the aromatic amino acids phenylalanine and tyrosine.
XX
DE   + RecName: EC=5.4.99.5;
XX
CC   -!- SIMILARITY: Contains # chorismate mutase aroH-type domain.
XX
GO   GO:0009073; P:aromatic amino acid family biosynthesis
GO   GO:0008652; P:amino acid biosynthesis
GO   GO:0016853; F:isomerase activity
XX
KW   Aromatic amino acid biosynthesis
KW   Amino-acid biosynthesis
KW   Isomerase
XX
FT   From: PS51167
FT   DOMAIN     from     to       Chorismate mutase aroH-type #.
XX
Chop: Nter=0; Cter=0;
Size: 105-130;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P19080;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00515;
DC   Domain;
TR   PROSITE; PS51168; CHORISMATE_MUT_2; 1; level=0
XX
Names: chorismate mutase domain
 CM domain
Function: Chorismate mutase is a regulatory enzyme required for biosynthesis
 of the aromatic amino acids phenylalanine and tyrosine.
XX
DE   + RecName: EC=5.4.99.5;
XX
CC   -!- SIMILARITY: Contains # chorismate mutase domain.
XX
GO   GO:0009073; P:aromatic amino acid family biosynthesis
GO   GO:0008652; P:amino acid biosynthesis
GO   GO:0016853; F:isomerase activity
XX
KW   Aromatic amino acid biosynthesis
KW   Amino-acid biosynthesis
KW   Isomerase
XX
FT   From: PS51168
FT   DOMAIN     from     to       Chorismate mutase #.
XX
Chop: Nter=0; Cter=0;
Size: 70-110;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q02287;
Scope:
 Bacteria
 Archaea
 Eukaryota; Chromadorea
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00516;
DC   Domain;
TR   PROSITE; PS51169; CHORISMATE_MUT_3; 1; level=0
XX
Names: chorismate mutase domain
 CM domain
Function: Chorismate mutase is a regulatory enzyme required for biosynthesis
 of the aromatic amino acids phenylalanine and tyrosine.
XX
DE   + RecName: EC=5.4.99.5;
XX
CC   -!- ENZYME REGULATION: Allosterically regulated.
CC   -!- SIMILARITY: Contains # chorismate mutase domain.
XX
GO   GO:0003824; F:catalytic activity
GO   GO:0009073; P:aromatic amino acid family biosynthesis
GO   GO:0008652; P:amino acid biosynthesis
GO   GO:0016853; F:isomerase activity
XX
KW   Allosteric enzyme
KW   Aromatic amino acid biosynthesis
KW   Amino-acid biosynthesis
KW   Isomerase
XX
FT   From: PS51169
FT   DOMAIN     from     to       Chorismate mutase #.
XX
Chop: Nter=0; Cter=0;
Size: 240-270;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O13739;
Scope:
 Eukaryota; Fungi
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00517;
DC   Domain;
TR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1; level=0
XX
Names: prephenate dehydratase domain
 PDT domain
Function: Prephenate dehydratase (EC 4.2.1.51) catalyzes the decarboxylation
 of prephenate into phenylpyruvate.
XX
DE   + RecName: EC=4.2.1.51;
XX
CC   -!- SIMILARITY: Contains # prephenate dehydratase domain.
XX
GO   GO:0009094; P:L-phenylalanine biosynthesis
GO   GO:0009073; P:aromatic amino acid family biosynthesis
GO   GO:0008652; P:amino acid biosynthesis
GO   GO:0016829; F:lyase activity
XX
KW   Phenylalanine biosynthesis
KW   Aromatic amino acid biosynthesis
KW   Amino-acid biosynthesis
KW   Lyase
XX
FT   From: PS51171
FT   DOMAIN     from     to       Prephenate dehydratase #.
XX
Chop: Nter=5; Cter=0;
Size: 170-230;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P32452;
Scope:
 Bacteria
 Archaea
 Eukaryota; Fungi
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00518;
DC   Domain;
TR   PROSITE; PS51163; YRDC; 1; level=0
XX
Names: YrdC-like domain
Function: The yrdC-like domain is an ~185-residue module which can be found in
 stand-alone form, or in association with other domains such as the
 acylphosphatase-like domain, the sua5-like domain, the hypF-like domain or
 the hypF-type zinc finger.
XX
CC   -!- SIMILARITY: Contains # YrdC-like domain.
XX
FT   From: PS51163
FT   DOMAIN     from     to       YrdC-like #.
XX
Chop: Nter=0; Cter=0;
Size: 160-205;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P30131;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2005/12/12
//
AC   PRU00519;
DC   Domain;
TR   PROSITE; PS50040; EF1G_C; 1; level=0
XX
Names: Elongation factor 1 (EF-1) gamma C-terminal domain
Function: The eukaryotic elongation factor 1 (EF-1) gamma chain is a protein
 of about 410 to 440 residues, which consists of two independent domains, a
 glutathione S-transferase (GST) homologous N-terminal region responsible for
 the interaction with EF-1 alpha and a highly conserved exceptionally protease
 resistant ~160 residue C-terminal domain.
XX
CC   -!- SIMILARITY: Contains # EF-1-gamma C-terminal domain.
XX
GO   GO:0006412; P:protein biosynthesis
GO   GO:0003746; F:translation elongation factor activity
XX
KW   Elongation factor
KW   Protein biosynthesis
XX
FT   From: PS50040
FT   DOMAIN     from     to       EF-1-gamma C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 155-165;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P26641;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2005/12/12
//
AC   PRU00520;
DC   Domain;
TR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1; level=0
XX
Names: Acylphosphatase-like domain
Function: Acylphosphatase (EC 3.6.1.7) [1,2] catalyzes the hydrolysis of
 various acyl phosphate carboxyl-phosphate bonds such as carbamyl phosphate,
 succinyl phosphate, 1,3-diphosphoglycerate, etc.
XX
case <FTGroup:1>
DE   + RecName: EC=3.6.1.7;
end case
CC   -!- SIMILARITY: Contains # acylphosphatase-like domain.
XX
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1; trigger=no
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1; trigger=no
case <FTGroup:1>
XX
GO   GO:0016787; F:hydrolase activity
XX
KW   Hydrolase
XX
end case
FT   From: PS51160
FT   DOMAIN     from     to       Acylphosphatase-like #.
FT   ACT_SITE     16     16       By similarity.
FT   Group: 1; Condition: R
FT   ACT_SITE     34     34       By similarity.
FT   Group: 1; Condition: N
XX
Chop: Nter=0; Cter=0;
Size: 65-100;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0AB65;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.6  2009/02/27
//
AC   PRU00521;
DC   Domain;
TR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1; level=0
XX
Names: G-protein coupled receptors family 1
Function: transduces extracellular signals by interaction with guanine nucleotide-binding (G) proteins.
XX
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
XX
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1; trigger=no
XX
GO   GO:0004930; F:G-protein coupled receptor activity
GO   GO:0007186; F:G-protein coupled receptor protein signaling pathway
GO   GO:0004871; F:signal transducer activity
GO   GO:0007165; P:signal transduction
XX
KW   G-protein coupled receptor
KW   Membrane
KW   Receptor
KW   Transducer
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50262
FT   DISULFID     57    136       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 200-400;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9N298;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2009/02/09
//
AC   PRU00522;
DC   Domain;
TR   PROSITE; PS51176; PDH_ADH; 1; level=0
XX
Names: Prephenate/arogenate dehydrogenase domain
 PDH domain
Function: Prephenate dehydrogenase (EC 1.3.1.12) (PDH), arogenate
 dehydrogenase (EC 1.3.1.43) (ADH) and cyclohexadienyl dehydrogenase (which
 can accept both prephenate and arogenate as substrate) are dehydrogenases of
 different intermediates for the biosynthesis of tyrosine.
XX
DE   + RecName: EC=1.3.1.-;
XX
CC   -!- SIMILARITY: Contains # prephenate/arogenate dehydrogenase domain.
XX
GO   GO:0009073; P:aromatic amino acid family biosynthesis
GO   GO:0008652; P:amino acid biosynthesis
GO   GO:0006571; P:tyrosine biosynthesis
GO   GO:0016491; F:oxidoreductase activity
XX
KW   Aromatic amino acid biosynthesis
KW   Amino-acid biosynthesis
KW   Tyrosine biosynthesis
KW   Oxidoreductase
XX
FT   From: PS51176
FT   DOMAIN     from     to       Prephenate/arogenate dehydrogenase #.
XX
Chop: Nter=0; Cter=10;
Size: 250-300;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P20692;
Scope:
 Bacteria
 Archaea
 Eukaryota; Fungi
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00523;
DC   Domain;
TR   PROSITE; PS51175; CBM6; 1-3; level=0
XX
Names: CBM6 (carbohydrate binding type-6) domain
Function: Involved in the binding to amorphous cellulose, xylan, mixed beta-(1,3)(1,4)glucan
 and  beta-1,3-glucan, and is also present in a alpha-1,6-mannanase and several alpha-agarases.
XX
CC   -!- SIMILARITY: Contains # CBM6 (carbohydrate binding type-6) domain.
XX
DR   PROSITE; PS51175; CBM6; 1-3; trigger=no
XX
FT   From: PS51175
FT   DOMAIN     from     to       CBM6 #.
XX
Chop: Nter=0; Cter=0;
Size: 110-140;
Related: none;
Repeats: 1-3;
Topology: Undefined;
Example: P10478; P55296; P55297;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2005/12/19
//
AC   PRU00524;
DC   Domain;
TR   PROSITE; PS51177; LUMAZINE_BIND; 1; level=0
XX
Names: Riboflavin synthase alpha chain lumazine-binding repeat
 Lum-binding domain
Function: Riboflavin synthase, catalyzing the biosynthesis of riboflavin
 (vitamin B2) by dismutation of 6,7-dimethyl-8-(1'-D-ribityl)lumazine (Lum)
 (EC 2.5.1.9), and antenna proteins involved in bioluminescence of marine
 bacteria seem to have evolved from the duplication of a domain of about 100
 residues, the lumazine-binding repeat.
XX
CC   -!- SIMILARITY: Contains # lumazine-binding repeat.
XX
FT   From: PS51177
FT   REPEAT    entry   exit       Lumazine-binding #.
XX
Chop: Nter=0; Cter=0;
Size: 80-110;
Related: None;
Repeats: 2;
Topology: Undefined;
Example: P0AFU8;
Scope:
 Bacteria
 Eukaryota; Fungi
 Eukaryota; Viridiplantae
 Archaea
Comments: None
XX
# Revision 1.1  2005/12/22
//
AC   PRU00525;
DC   Domain;
TR   PROSITE; PS50258; LNR; 1-3; level=0
XX
Names: Lin-12/Notch (LNR) repeat
Function: The LNR is supposed to negatively regulates the Lin-12/Notch
 proteins activity, and participates in maintaining the receptor in its
 resting conformation prior to ligand binding.
XX
CC   -!- SIMILARITY: Contains # LNR (Lin/Notch) repeat.
XX
DR   PROSITE; PS50258; LNR; 1-3; trigger=no
XX
GO   GO:0005509; F:calcium ion binding
GO   GO:0007219; P:Notch signaling pathway
XX
case <FTGroup:1>
KW   Calcium
KW   Metal-binding
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS50258
FT   REPEAT    entry   exit       LNR #.
FT   DISULFID      1     25       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      7     20       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     16     32       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   METAL        13     13       Calcium (By similarity).
FT   Group: 1; Condition: [DN]
FT   METAL        28     28       Calcium (By similarity).
FT   Group: 1; Condition: D
FT   METAL        31     31       Calcium (By similarity).
FT   Group: 1; Condition: [DE]
XX
Chop: Nter=0; Cter=0;
Size: 35-45;
Related: none;
Repeats: 1-3;
Topology: Undefined;
Example: Q3T906;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00526;
DC   Domain;
TR   PROSITE; PS51180; BRO1; 1; level=0
XX
Names: BRO1 domain
Function: The BRO1 domain of fungal and mammalian proteins is involved in
 protein targeting to the lysosome or vacuole by binding multivesicular body
 components (ESCRT-III proteins) like Snf7 and can thus function to target
 BRO1 domain-containing proteins to endosomes.
XX
CC   -!- SIMILARITY: Contains # BRO1 domain.
XX
FT   From: PS51180
FT   DOMAIN    entry   exit       BRO1 #.
XX
Chop: Nter=0; Cter=0;
Size: 280-465;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6PB44;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/01/23
//
AC   PRU00527;
DC   Domain;
TR   PROSITE; PS51174; BARWIN_3; 1; level=0
XX
Names: Barwin domain
Function: A domain found in plant proteins that could be involved in a defense
 mechanism.
XX
CC   -!- SIMILARITY: Contains # barwin domain.
XX
DR   PROSITE; PS00771; BARWIN_1; 1; trigger=no
DR   PROSITE; PS00772; BARWIN_2; 1; trigger=no
FT   From: PS51174
FT   DOMAIN     from     to       Barwin #.
XX
Chop: Nter=0; Cter=0;
Size: 115-130;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P28814;
Scope:
 Eukaryota; Viridiplantae; Embryophyta
 Viruses
Comments: None
XX
# Revision 1.1  2006/01/25
//
AC   PRU00528;
DC   Domain;
TR   PROSITE; PS51178; PASTA; 1; level=0
XX
Names: PASTA domain
Function: The PASTA domain (for penicillin-binding protein and
 serine/threonine kinase associated domain) is an extracellular module of ~70
 residues that is found in the C-termini of eukaryotic-like serine/threonine
 kinases (PSTKs) and high molecular weight penicilin-binding proteins (PBPs).
XX
CC   -!- SIMILARITY: Contains # PASTA domain.
XX
FT   From: PS51178
FT   DOMAIN     from     to       PASTA #.
XX
Chop: Nter=0; Cter=0;
Size: 55-75;
Related: None;
Repeats: 1-5;
Topology: Not cytoplasmic;
Example: Q9S2C0;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2006/01/25
//
AC   PRU00529;
DC   Domain;
TR   PROSITE; PS51165; THUMP; 1; level=0
XX
Names: THUMP domain
Function: The THUMP (after thiouridine synthases, RNA methylases and
 pseudouridine synthases) domain is a module of 100-110 amino acid residues
 which is involved RNA metabolism. THUMP is an ancient domain with predicted
 RNA-binding capacity that probably functions by delivering a variety of RNA
 modification enzymes to their targets.
XX
CC   -!- SIMILARITY: Contains # THUMP domain.
XX
GO   GO:0003723; F:RNA binding
XX
KW   RNA-binding
XX
FT   From: PS51165
FT   DOMAIN     from     to       THUMP #.
XX
Chop: Nter=0; Cter=0;
Size: 90-120;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P53072;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2006/01/25
//
AC   PRU00530;
DC   Domain;
TR   PROSITE; PS51179; POU_3; 1; level=0
XX
Names: POU-specific (POUs) domain
Function: The POUs domain is always found in association with a POU-
 homeodomain, and both are required for high affinity and sequence-specific
 DNA binding.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # POU-specific domain.
XX
DR   PROSITE; PS00035; POU_1; 1; trigger=no
DR   PROSITE; PS00465; POU_2; 1; trigger=no
case <AnyFeature:PS50071>
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
end case
FT   From: PS51179
FT   DOMAIN     from     to       POU-specific #.
XX
Chop: Nter=0; Cter=0;
Size: 70-115;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P24350;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.6  2007/06/21
//
AC   PRU00531;
DC   Domain;
TR   PROSITE; PS51185; WHEP_TRS_2; 1-6; level=0
XX
Names: WHEP-TRS domain
Function: This domain may play  a role in the association of tRNA-synthetases
 into multienzyme complexes.
XX
CC   -!- SIMILARITY: Contains # WHEP-TRS domain.
XX
DR   PROSITE; PS51185; WHEP_TRS_2; 1-6; trigger=no
XX
FT   From: PS51185
FT   DOMAIN     from     to       WHEP-TRS #.
XX
Chop: Nter=0; Cter=0;
Size: 40-60;
Related: none;
Repeats: 1-6;
Topology: Undefined;
Example: P07814;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/03/01
//
AC   PRU00532;
DC   Domain;
TR   PROSITE; PS51186; GNAT; 1; level=0
XX
Names: Gcn5-related N-acetyltransferase (GNAT) domain
Function: The GNAT domain catalyzes the transfer of an acetyl group from the
 CoA donor to a primary amine of the acceptor, a reaction implicated in
 various functions from bacterial antibiotic resistance to mammalian circadian
 rhythm and chromatin remodeling.
XX
DE   + RecName: EC=2.3.1.-;
XX
CC   -!- SIMILARITY: Contains # N-acetyltransferase domain.
XX
GO   GO:0008415; F:acyltransferase activity
GO   GO:0016740; F:transferase activity
XX
KW   Acyltransferase
KW   Transferase
XX
FT   From: PS51186
FT   DOMAIN    entry   exit       N-acetyltransferase #.
XX
Chop: Nter=0; Cter=0;
Size: 80-210;
Related: PRU00533; PRU00536;
Repeats: 1-3;
Topology: Undefined;
Example: Q92831;
Scope:
 Bacteria
 Eukaryota
 Archaea
 Viruses
Comments: None
XX
# Revision 1.5  2009/02/27
//
AC   PRU00533;
DC   Domain;
TR   PROSITE; PS51187; AUTOINDUCER_SYNTH_2; 1; level=0
XX
Names: Autoinducer synthase family
Function: Autoinducers are hormone-like molecules produced by bacterial
 synthases as signals to sense cell density and activate adaptations, by a
 process termed quorum sensing.
XX
CC   -!- SIMILARITY: Belongs to the autoinducer synthase family.
XX
GO   GO:0009372; P:quorum sensing
XX
KW   Autoinducer synthesis
KW   Quorum sensing
XX
Chop: Nter=0; Cter=0;
Size: 170-200;
Related: PRU00532;
Repeats: 1;
Topology: Undefined;
Example: P33883;
Scope:
 Bacteria; Proteobacteria
Comments: None
XX
# Revision 1.2  2010/03/17
//
AC   PRU00534;
DC   Domain;
TR   PROSITE; PS51189; FAT; 1; level=0
XX
Names: FAT domain
Function: The PI-kinase domain of members of the PIK-related family is wedged
 between the ~550-amino acid-long FAT (FRAP, ATM, TRRAP) domain and the ~35
 residue C-terminal FATC domain.
XX
CC   -!- SIMILARITY: Contains # FAT domain.
XX
DR   PROSITE; PS51190; FATC; 1; trigger=no
XX
FT   From: PS51189
FT   DOMAIN     from     to       FAT #.
XX
Chop: Nter=0; Cter=0;
Size: 540-720;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P38110;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/04/28
//
AC   PRU00535;
DC   Domain;
TR   PROSITE; PS51190; FATC; 1; level=0
XX
Names: FATC domain
Function: The PI-kinase domain of members of the PIK-related family is wedged
 between the ~550-amino acid-long FAT (FRAP, ATM, TRRAP) domain and the ~35
 residue C-terminal FATC domain.
XX
CC   -!- SIMILARITY: Contains # FATC domain.
XX
DR   PROSITE; PS51189; FAT; 1; trigger=no
XX
FT   From: PS51190
FT   DOMAIN     from     to       FATC #.
XX
Chop: Nter=0; Cter=0;
Size: 30-35;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P38110;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/04/28
//
AC   PRU00536;
DC   Domain;
TR   PROSITE; PS51191; FEMABX; 1; level=0
XX
Names: FemABX peptidyl transferase family
Function: FemABX peptidyl transferases catalyze the incorporation of amino
 acid(s) into the interchain peptide bridge of peptidoglycan using
 aminoacyl-tRNA as the amino acid donor, a reaction involved in the synthesis
 of the bacterial cell wall.
XX
DE   + RecName: EC=2.3.2.-;
XX
CC   -!- SIMILARITY: Belongs to the femABX family.
XX
GO   GO:0009252; P:peptidoglycan biosynthesis
GO   GO:0000902; P:cellular morphogenesis
GO   GO:0008415; F:acyltransferase activity
GO   GO:0016740; F:transferase activity
XX
KW   Peptidoglycan synthesis
KW   Cell shape
KW   Cell wall
KW   Acyltransferase
KW   Transferase
XX
Chop: Nter=0; Cter=0;
Size: 400-420;
Related: PRU00532;
Repeats: 1;
Topology: Undefined;
Example: P0A0A5;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.4  2009/02/27
//
AC   PRU00537;
DC   Domain;
TR   PROSITE; PS51183; JMJN; 1; level=0
XX
Names: JmjN domain
Function: The JmjN domain is found in the jumonji family of transcription
 factors and always co-occurs with the JmjC domain.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Contains # JmjN domain.
XX
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51183
FT   DOMAIN     from     to       JmjN #.
XX
Chop: Nter=0; Cter=0;
Size: 40-45;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P29375;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2007/06/07
//
AC   PRU00538;
DC   Domain;
TR   PROSITE; PS51184; JMJC; 1; level=0
XX
Names: JmjC domain
Function: the JmjC domain is found in organisms from bacteria to human and has
 been shown to function in a histone demethylation mechanism that is conserved
 from yeast to human.
CC   -!- SIMILARITY: Contains # JmjC domain.
XX
FT   From: PS51184
FT   DOMAIN     from     to       JmjC #.
XX
Chop: Nter=0; Cter=0;
Size: 120-230;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y4C1;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.1  2006/03/16
//
AC   PRU00539;
DC   Domain;
TR   PROSITE; PS50507; RDRP_SSRNA_POS; 0-1; level=0
TR   PROSITE; PS50522; RDRP_PHAGE; 0-1; level=0
TR   PROSITE; PS50523; RDRP_DSRNA_REO; 0-1; level=0
TR   PROSITE; PS50524; RDRP_DSRNA_BIR; 0-1; level=0
TR   PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 0-1; level=0
TR   PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 0-1; level=0
XX
Names: RdRp
Function: RNA-directed RNA polymerase.
XX
DE   + AltName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
XX
CC   -!- FUNCTION: RNA-directed RNA polymerase.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SIMILARITY: Contains # RdRp catalytic domain.
XX
GO   GO:0000166; F:nucleotide binding
GO   GO:0016779; F:nucleotidyltransferase activity
GO   GO:0003968; F:RNA-directed RNA polymerase activity
GO   GO:0003723; F:RNA binding
GO   GO:0006410; P:transcription, RNA-dependent
GO   GO:0016740; F:transferase activity
XX
KW   Nucleotide-binding
KW   Nucleotidyltransferase
KW   RNA replication
KW   RNA-directed RNA polymerase
KW   Transferase
XX
FT   From: any
FT   DOMAIN     from     to       RdRp catalytic #.
XX
Chop: Nter=0; Cter=0;
Size: 90-230;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P24658;
Scope:
 Viruses
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00540;
DC   Domain;
TR   PROSITE; PS51197; HTH_RRF2_2; 1; level=0
XX
Names: Rrf2-type HTH domain
Function: The rrf2-type HTH domain is a putative DNA-binding, winged
 helix-turn-helix (wHTH) domain of about 130 residues present in transcription
 regulators of the rrf2 family, involved in nitrite or iron metabolism. The
 C-terminal part of the domain contains 3 conserved cysteine residues that may
 bind an Fe-S cluster.
XX
CC   -!- SIMILARITY: Contains # HTH rrf2-type DNA-binding domain.
XX
DR   PROSITE; PS01332; HTH_RRF2_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
case <FTGroup:1>
GO   GO:0046872; F:metal ion binding
end case
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0006350; P:transcription
XX
KW   DNA-binding
case <FTGroup:1>
KW   Metal-binding
end case
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51197
FT   DOMAIN     from     to       HTH rrf2-type #.
FT   DNA_BIND     26     49       H-T-H motif (By similarity).
FT   METAL        90     90       Potential.
FT   Group: 1; Condition: C
FT   METAL        96     96       Potential.
FT   Group: 1; Condition: C
FT   METAL       102    102       Potential.
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 120-150;
Related: PRU00393; PRU00307;
Repeats: 1;
Topology: Undefined;
Example: P0AGK8;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.7  2006/11/21
//
AC   PRU00541;
DC   Domain;
TR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 0-1; level=0
TR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 0-1; level=0
XX
Names: Helicase ATP-binding domain
Function: Helicase ATP-binding domain in association with helicase C-terminal domain catalyze  the separation of double-stranded nucleic acids
XX
CC   -!- SIMILARITY: Contains # helicase ATP-binding domain.
XX
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 0-1; trigger=no
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 0-1; trigger=no
XX
GO   GO:0004386; F:helicase activity
GO   GO:0005524; F:ATP binding
GO   GO:0016787; F:hydrolase activity
GO   GO:0000166; F:nucleotide binding
XX
KW   ATP-binding
KW   Helicase
KW   Hydrolase
KW   Nucleotide-binding
XX
FT   From: any
FT   DOMAIN     from     to       Helicase ATP-binding #.
case <Feature:PS51192>=1>
FT   NP_BIND      14     21       ATP (By similarity).
end case
case <Feature:PS51193>=1>
FT   NP_BIND      36     43       ATP (By similarity).
end case
case <Feature:PS51192:121=D>
FT   MOTIF       118    121       DEAD box.
end case
case <Feature:PS51192:121=H>
FT   MOTIF       118    121       DEAH box.
end case
case <Feature:PS51193:121=D>
FT   MOTIF       231    234       DEAD box.
end case
case <Feature:PS51193:121=H>
FT   MOTIF       231    234       DEAH box.
end case
XX
Chop: Nter=0; Cter=0;
Size: 120-350;
Related: None;
Repeats: 2;
Topology: Undefined;
Example: Q14240;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.3  2006/12/18
//
AC   PRU00542;
DC   Domain;
TR   PROSITE; PS51194; HELICASE_CTER; 1; level=0
XX
Names: Helicase C-terminal domain
Function:  Helicase C-terminal domain in association with helicase ATP-binding domain catalyze  the separation of double-stranded nucleic acids
XX
CC   -!- SIMILARITY: Contains # helicase C-terminal domain.
XX
FT   From: PS51194
FT   DOMAIN     from     to       Helicase C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 95-208;
Related: None;
Repeats: 2;
Topology: Undefined;
Example: Q14240;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.1  2006/04/12
//
AC   PRU00543;
DC   Domain;
TR   PROSITE; PS51201; RCK_N; 1-2; level=0
XX
Names: RCK N-terminal domain
Function:  Largely  involved in redox-linked regulation of potassium channels,
 the  N-terminal  part  of  the  regulators  of  K+ conductance (RCK) domain is
 predicted  to  be an active dehydrogenase at least in some cases. Certain bind
 nicotinamide  adenine dinucleotide (NAD) through a glycine motif, but for many
 RCK domains the ligand is unknown.
XX
CC   -!- SIMILARITY: Contains # RCK N-terminal domain.
XX
DR   PROSITE; PS51201; RCK_N; 1-2; trigger=no
XX
GO   GO:0043266; P:regulation of potassium ion transport
GO   GO:0015459; F:potassium channel regulator activity
XX
FT   From: PS51201
FT   DOMAIN     from     to       RCK N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 100-150;
Related: none;
Repeats: 1-2;
Topology: Undefined;
Example: P0AGI8;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.3  2006/04/26
//
AC   PRU00544;
DC   Domain;
TR   PROSITE; PS51202; RCK_C; 1-4; level=0
XX
Names: RCK C-terminal domain
Function: The C-terminal part of the regulators of K+ conductance (RCK) domain
 is  less conserved among RCK domains, being absent in some. It is predicted to
 bind   unidentified   ligands  and  to  regulate  sulfate,  sodium  and  other
 transporters.  It  forms  an  extention  of  the  dimer  interface and further
 stabilizes the RCK homodimer.
XX
CC   -!- SIMILARITY: Contains # RCK C-terminal domain.
XX
DR   PROSITE; PS51202; RCK_C; 1-4; trigger=no
XX
GO   GO:0043266; P:regulation of potassium ion transport
GO   GO:0015459; F:potassium channel regulator activity
XX
FT   From: PS51202
FT   DOMAIN     from     to       RCK C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 75-100;
Related: none;
Repeats: 1-4;
Topology: Undefined;
Example: P0AGI8;
Scope:
 Bacteria
 Archaea
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/04/26
//
AC   PRU00545;
DC   Domain;
TR   PROSITE; PS51200; SHORT_SCORPION_CHLORIDE; 1; level=0
XX
Names: Scorpion short toxin chloride channel inhibitor subfamily
Function: Short scorpion toxin chloride channel inhibitors are short-chain
 neurotoxins (SCNs), which block small-conductance chloride channels. They are
 30-40-residue long and contain four intramolecular disulfide bridges, which
 have been assigned as C1-C4, C2-C6, C3-C7 and C5-C8.
XX
CC   -!- FUNCTION: Probable chloride channel ligand, which blocks small-
CC       conductance chloride channels (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily.
CC       Chloride channel inhibitor family.
XX
GO   GO:0019869; F:chloride channel inhibitor activity
GO   GO:0008200; F:ion channel inhibitor activity
GO   GO:0009405; P:pathogenesis
XX
KW   Secreted
KW   Chloride channel inhibitor
KW   Ionic channel inhibitor
KW   Neurotoxin
KW   Toxin
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51200
FT   DISULFID      1     18       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID      4     25       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     15     30       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     19     32       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 20-35;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P15229;
Scope:
 Eukaryota; Metazoa; Arachnida; Scorpiones
Comments: None
XX
# Revision 1.5  2009/02/09
//
AC   PRU00546;
DC   Domain;
TR   PROSITE; PS51188; ZF_CR; 1; level=0
XX
Names: CR-type zinc finger
Function: important for the autonomous, dnaK-independent chaperone activity,  but also necessary for the interaction site dnaK
XX
CC   -!- SIMILARITY: Contains # CR-type zinc finger.
XX
KW   Metal-binding
KW   Zinc
KW   Zinc-finger
XX
FT   From: PS51188
FT   ZN_FING    from     to       CR-type #.
XX
Chop: Nter=0; Cter=0;
Size: 73-93;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5XAD7;
Scope:
 Eukaryota
 Bacteria
 Viruses
 Archaea
Comments: None
XX
# Revision 1.1  2006/10/17
//
AC   PRU00547;
DC   Domain;
TR   PROSITE; PS51203; CS; 1; level=0
XX
Names: CS domain
Function: The bipartite CS domain, which was named after CHORD-containing
 proteins and SGT1, is a ~100-residue protein-protein interaction module.
XX
CC   -!- SIMILARITY: Contains # CS domain.
XX
FT   From: PS51203
FT   DOMAIN     from     to       CS #.
XX
Chop: Nter=0; Cter=0;
Size: 80-105;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q08446;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/06/08
//
AC   PRU00548;
DC   Domain;
TR   PROSITE; PS50188; B302_SPRY; 1; level=0
XX
Names: B30.2/SPRY domain
Function: The B30.2/SPRY domain in these proteins is likely to function
 through protein-protein interaction.
XX
CC   -!- SIMILARITY: Contains # B30.2/SPRY domain.
XX
FT   From: PS50188
FT   DOMAIN     from     to       B30.2/SPRY #.
XX
Chop: Nter=0; Cter=0;
Size: 105-255;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q13410;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/05/04
//
AC   PRU00549;
DC   Domain;
TR   PROSITE; PS51204; HSA; 1; level=0
XX
Names: HSA domain
Function: The helicase/SANT-associated (HSA) domain is a predicted DNA-binding
 domain of ~75 amino acids, which is found in the eukaryotic SRCAP/p400/DOM
 and SNF2/brahma families.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # HSA domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   DNA-binding
KW   Nucleus
XX
FT   From: PS51204
FT   DOMAIN     from     to       HSA #.
XX
Chop: Nter=0; Cter=0;
Size: 70-85;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8CHI8;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2007/06/07
//
AC   PRU00550;
DC   Domain;
TR   PROSITE; PS51205; VPS9; 1; level=0
XX
Names: VPS9 domain
Function: The VPS9 domain is a GDP-GTP exchange factor (GEF) domain that
 catalyzes nucleotide exchange on Rab5, which activates this Rab GTPase.
XX
CC   -!- SIMILARITY: Contains # VPS9 domain.
XX
GO   GO:0005096; F:GTPase activator activity
KW   GTPase activation
XX
FT   From: PS51205
FT   DOMAIN     from     to       VPS9 #.
XX
Chop: Nter=0; Cter=0;
Size: 130-170;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8TB24;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/05/09
//
AC   PRU00551;
DC   Domain;
TR   PROSITE; PS51206; SF3_HELICASE_1; 0-1; level=0
TR   PROSITE; PS51218; SF3_HELICASE_2; 0-1; level=0
XX
Names: Superfamily 3 helicase domain
 SF3 helicase domain
Function: Helicases encoded mainly by small RNA and DNA viruses and some large
 nucleocytoplasmic DNA viruses.
XX
CC   -!- SIMILARITY: Contains # SF3 helicase domain.
XX
DR   PROSITE; PS00017; ATP_GTP_A; 1; trigger=yes
XX
GO   GO:0006260; P:DNA replication
XX
KW   DNA replication
XX
FT   From: any
FT   DOMAIN     from     to       SF3 helicase #.
XX
Chop: Nter=0; Cter=0;
Size: 128-198;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P50762;
Scope:
 Viruses
Comments: None
XX
# Revision 1.4  2007/11/29
//
AC   PRU00552;
DC   Domain;
TR   PROSITE; PS51195; Q_MOTIF; 1; level=0
XX
Names: Q motif
Function:  The  Q  motif is characteristic of and unique to DEAD box family of helicases. It  is  supposed  to  control  ATP  binding  and  hydrolysis.
XX
XX
FT   From: PS51195
FT   MOTIF      from     to       Q motif.
XX
Chop: Nter=0; Cter=0;
Size: 20-35;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q14240;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.1  2006/05/15
//
AC   PRU00553;
DC   Domain;
TR   PROSITE; PS51207; PXA; 1; level=0
XX
Names: PXA domain
Function: The PX-associated (PXA) domain is a ~200-amino acid module of
 unknown function. Perhaps it is required for protein-protein interaction and/
 or filament formation.
XX
CC   -!- SIMILARITY: Contains # PXA domain.
XX
FT   From: PS51207
FT   DOMAIN     from     to       PXA #.
XX
Chop: Nter=0; Cter=0;
Size: 170-190;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q01846;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/06/08
//
AC   PRU00555;
DC   Domain;
TR   PROSITE; PS51210; PLA2C; 1; level=0
XX
Names: PLA2c domain
Function: The PLA2c domain is the catalytic lipase domain in cytosolic
 phospholipase A2 (cPLA2) (EC 3.1.1.4) and lysophospholipase or phospholipase
 B (PLB) (EC 3.1.1.5) of vertebrates and fungi.
XX
DE   + RecName: EC=3.1.1.-;
XX
CC   -!- SIMILARITY: Contains # PLA2c domain.
XX
GO   GO:0016787; F:hydrolase activity
GO   GO:0016042; P:lipid catabolism
XX
KW   Hydrolase
KW   Lipid degradation
XX
FT   From: PS51210
FT   DOMAIN     from     to       PLA2c #.
XX
Chop: Nter=0; Cter=0;
Size: 520-610;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9P8P2;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00556;
DC   Domain;
TR   PROSITE; PS51208; AUTOTRANSPORTER; 1; level=0
XX
Names: Autotransporter
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # autotransporter (TC 1.B.12) domain.
XX
KW   Membrane
KW   Outer membrane
XX
FT   From: any
FT   DOMAIN     from     to       Autotransporter #.
XX
Chop: Nter=0; Cter=0;
Size: 230-318;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9PL46;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.4  2006/12/05
//
AC   PRU00557;
DC   Domain;
TR   PROSITE; PS51211; VITELLOGENIN; 1; level=0
XX
Names: Vitellogenin domain
Function: The vitellogenin (VTG) protein, a major lipoprotein in many oviparous animals,
 is a precursor of a lipid-binding product found in the yolk of egg-laying animals,
 and involved in lipid and metal storage. At the N-terminal, it contains a sequence
 of about 670 amino acids (LV1n chain), which is also conserved in other large lipoproteins,
 such as microsomal triglyceride transfer protein (MTP) and apolipoprotein B-100 (apoB)
XX
CC   -!- SIMILARITY: Contains # vitellogenin domain.
XX
DR   PROSITE; PS51211; VITELLOGENIN; 1; trigger=no
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51211
FT   DOMAIN     from     to       Vitellogenin #.
FT   DISULFID    139    165       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    181    184       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    409    414       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 600-660;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: Q91062;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/09
//
AC   PRU00558;
DC   Domain;
TR   PROSITE; PS51212; WSC; 1; level=0
XX
Names: WSC domain
Function: The WSC domain is a putative carbohydrate binding domain of about
 90 amino acids.
XX
CC   -!- SIMILARITY: Contains # WSC domain.
XX
FT   From: PS51212
FT   DOMAIN    entry   exit       WSC #.
XX
Chop: Nter=5; Cter=5;
Size: 80-110;
Related: None;
Repeats: 1-5;
Topology: Undefined;
Example: Q7KVA1;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/05/30
//
AC   PRU00559;
DC   Domain;
TR   PROSITE; PS51213; ELK; 1; level=0
XX
Names: ELK domain
Function: The ELK domain could function as a nuclear localization signal. It
 also is considered to act as a protein-protein interaction domain, but the
 precise role of this domain has not been determined.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the TALE/KNOX homeobox family.
CC   -!- SIMILARITY: Contains # ELK domain.
XX
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
XX
FT   From: PS51213
FT   DOMAIN     from     to       ELK #.
XX
Chop: Nter=0; Cter=0;
Size: 20-25;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P24345;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.3  2007/06/07
//
AC   PRU00560;
DC   Domain;
TR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 0-1; level=0
XX
Names: UvrD helicase ATP-binding domain
Function: UvrD helicase unwind DNA with a 3'-5' polarity
XX
CC   -!- SIMILARITY: Contains # uvrD-like helicase ATP-binding domain.
XX
GO   GO:0004386; F:helicase activity
GO   GO:0005524; F:ATP binding
GO   GO:0016787; F:hydrolase activity
GO   GO:0000166; F:nucleotide binding
XX
KW   ATP-binding
KW   Helicase
KW   Hydrolase
KW   Nucleotide-binding
XX
FT   From: PS51198
FT   DOMAIN     from     to       UvrD-like helicase ATP-binding #.
FT   NP_BIND      22     29       ATP (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 200-600;
Related: None;
Repeats: 2;
Topology: Undefined;
Example: P64319;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.3  2009/05/28
//
AC   PRU00561;
DC   Domain;
TR   PROSITE; PS51214; IBB; 1; level=0
XX
Names: IBB domain
Function: The IBB domain is a highly basic amino-terminal region of roughly 40
 amino-acid residues, which is responsible for importin-beta binding.
XX
CC   -!- SIMILARITY: Contains # IBB domain.
XX
GO   GO:0006810; P:transport
XX
KW   Transport
XX
FT   From: PS51214
FT   DOMAIN     from     to       IBB #.
XX
Chop: Nter=0; Cter=0;
Size: 50-70;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P52294;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/07/26
//
AC   PRU00562;
DC   Domain;
TR   PROSITE; PS51215; AWS; 1; level=0
XX
Names: AWS domain
Function: In a subset of SET and post-SET containing proteins, a so-called
 associated with SET (AWS) domain is found instead of the pre-SET domain.
XX
CC   -!- SIMILARITY: Contains # AWS domain.
XX
FT   From: PS51215
FT   DOMAIN     from     to       AWS #.
XX
Chop: Nter=0; Cter=0;
Size: 40-60;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P46995;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/07/26
//
AC   PRU00563;
DC   Domain;
TR   PROSITE; PS51216; NEBULIN; 1; level=0
XX
Names: Nebulin repeat
 Nebulin-like motif
Function: The nebulin repeat is a tandemly repeated actin-binding module of
 about 35 amino acids.
XX
CC   -!- SIMILARITY: Contains # nebulin repeat.
XX
GO   GO:0003779; F:actin binding
KW   Actin-binding
XX
FT   From: PS51216
FT   REPEAT    entry   exit       Nebulin #.
XX
Chop: Nter=3; Cter=3;
Size: 10-45;
Related: None;
Repeats: 2-187;
Topology: Undefined;
Example: O76041;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2006/06/15
//
AC   PRU00564;
DC   Domain;
TR   PROSITE; PS51219; DPCK; 1; level=0
XX
Names: Dephospho-CoA kinase (DPCK) domain
Function: Dephospho-coenzyme A kinase (DPCK) (EC 2.7.1.24) catalyzes the final
 step in coenzyme A (CoA) biosynthesis, the phosphorylation of the 3'-hydroxyl
 group of ribose using ATP as a phosphate donor.
XX
DE   + AltName: Full=Dephospho-CoA kinase;
DE            EC=2.7.1.24;
DE   AltName: Full=Dephosphocoenzyme A kinase;
XX
CC   -!- SIMILARITY: Contains # DPCK (dephospho-CoA kinase) domain.
XX
DR   PROSITE; PS00017; ATP_GTP_A; 1; trigger=yes
XX
GO   GO:0015937; P:coenzyme A biosynthesis
GO   GO:0016301; F:kinase activity
GO   GO:0016740; F:transferase activity
XX
KW   Coenzyme A biosynthesis
KW   Kinase
KW   Transferase
XX
FT   From: PS51219
FT   DOMAIN     from     to       DPCK #.
XX
Chop: Nter=0; Cter=0;
Size: 175-235;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0A6I9;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00565;
DC   Domain;
TR   PROSITE; PS50032; KA1; 1; level=0
XX
Names: KA1 (kinase-associated) domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # KA1 (kinase-associated) domain.
FT   From: PS50032
FT   DOMAIN     from     to       KA1 #.
XX
Chop: Nter=0; Cter=0;
Size: 47-48;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q38997;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/10/17
//
AC   PRU00567;
DC   Domain;
TR   PROSITE; PS51223; MAP; 1; level=0
XX
Names: MAP repeat
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # MAP repeat.
FT   From: PS51223
FT   REPEAT     from     to       MAP #.
XX
Chop: Nter=0; Cter=0;
Size: 29-108;
Related: None;
Repeats: 3-6;
Topology: Undefined;
Example: Q53599;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2006/10/17
//
AC   PRU00568;
DC   Domain;
TR   PROSITE; PS51221; TTL; 1; level=0
XX
Names: TTL domain
Function: The TTL (tubulin tyrosine ligase) domain is a ~350 amino acid module
 present in a family of eukaryotic proteins that could catalyze ligations of
 diverse amino acids to tubulins or other substrates.
XX
DE   + RecName: EC=6.-.-.-;
XX
CC   -!- SIMILARITY: Contains # TTL domain.
XX
GO   GO:0016874; F:ligase activity
XX
KW   Ligase
XX
FT   From: PS51221
FT   DOMAIN     from     to       TTL #.
XX
Chop: Nter=0; Cter=0;
Size: 330-400;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8NG68;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00569;
DC   Domain;
TR   PROSITE; PS51222; DCD; 1; level=0
XX
Names: DCD domain
Function: The DCD domain is found in plant proteins involved in development
 and cell death.
XX
CC   -!- SIMILARITY: Contains # DCD domain.
XX
FT   From: PS51222
FT   DOMAIN     from     to       DCD #.
XX
Chop: Nter=0; Cter=0;
Size: 130-135;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P37707;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.1  2006/07/27
//
AC   PRU00570;
DC   Domain;
TR   PROSITE; PS51220; NIDO; 1; level=0
XX
Names: NIDO domain
Function: The ~180-residue NIDO domain is an extracellular domain of unknown
 function, found in nidogen (entactin) and hypothetical proteins.
XX
CC   -!- SIMILARITY: Contains # NIDO domain.
XX
FT   From: PS51220
FT   DOMAIN     from     to       NIDO #.
XX
Chop: Nter=0; Cter=0;
Size: 135-170;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: P14543;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2006/07/27
//
AC   PRU00571;
DC   Domain;
TR   PROSITE; PS51224; MVP; 1; level=0
XX
Names: MVP repeat
 MVP domain
 vault repeat
Function: The MVP repeat is a ~53 amino acid module of major vault protein
 (MVP) which forms a structural part of the wall of vaults, which are large
 ribonucleoprotein particles that are found in all higher eukaryotes.
XX
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains # MVP (vault) repeat.
XX
GO   GO:0030529; F:ribonucleoprotein complex
GO   GO:0005737; C:cytoplasm
XX
KW   Cytoplasm
KW   Ribonucleoprotein
XX
FT   From: PS51224
FT   REPEAT    entry   exit       MVP #.
XX
Chop: Nter=0; Cter=0;
Size: 35-80;
Related: None;
Repeats: 6-9;
Topology: Undefined;
Example: Q14764;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2008/04/08
//
AC   PRU00572;
DC   Domain;
TR   PROSITE; PS51227; SPR; 1; level=0
XX
Names: Sprouty (SPR) domain profile
Function: The SPR domain is conserved, C-terminal  cystein-rich  region,
 related  to  Sprouty and Spred proteins family. This domain has been
 defined as a novel translocation domain (SpryTD).
XX
CC   -!- SIMILARITY: Contains # SPR (sprouty) domain.
XX
DR   PROSITE; PS51227; SPR; 1; trigger=no
XX
FT   From: PS51227
FT   DOMAIN     from     to       SPR #.
XX
Chop: Nter=0; Cter=0;
Size: 90-120;
Related: none;
Repeats: 1;
Topology: Undefined;
Example: Q7Z699;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/07/05
//
AC   PRU00573;
DC   Domain;
TR   PROSITE; PS51228; ACB_2; 1; level=0
XX
Names: Acyl-CoA-binding (ACB) domain
Function: The ACB domain consists of four alpha-helices arranged in a bowl
 shape with a highly exposed acyl-CoA-binding site.
XX
CC   -!- SIMILARITY: Contains # ACB (acyl-CoA-binding) domain.
XX
DR   PROSITE; PS00880; ACB_1; 1; trigger=no
XX
FT   From: PS51228
FT   DOMAIN     from     to       ACB #.
XX
Chop: Nter=0; Cter=0;
Size: 80-95;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P07108;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2006/07/27
//
AC   PRU00574;
DC   Domain;
TR   PROSITE; PS51229; DCUN1; 1; level=0
XX
Names: DCUN1 domain
Function: The DCUN1 domain is an ~190-residue module of unknown function which
 is found in the eukaryotic defective in cullin neddylation (DCN) protein
 family.
XX
CC   -!- SIMILARITY: Contains # DCUN1 domain.
XX
FT   From: PS51229
FT   DOMAIN     from     to       DCUN1 #.
XX
Chop: Nter=0; Cter=0;
Size: 185-245;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q12395;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU00575;
DC   Domain;
TR   PROSITE; PS51226; TEP1_N; 1; level=0
XX
Names: TEP1 N-terminal repeat
Function: The TEP1 N-terminal repeat is a 30 residue module whereof 4 tandemly
 arranged copies form the N-terminus of telomerase protein component 1 (TP1)
 or TEP1, which is a protein component of two ribonucleoprotein (RNP)
 complexes: vaults and telomerase.
XX
CC   -!- SIMILARITY: Contains # TEP1 N-terminal repeat.
XX
GO   GO:0005694; C:chromosome
GO   GO:0030529; F:ribonucleoprotein complex
GO   GO:0007004; C:telomerase-dependent telomere maintenance
GO   GO:0000781; C:chromosome, telomeric region
XX
KW   Chromosomal protein
KW   Ribonucleoprotein
KW   Telomere
XX
FT   From: PS51226
FT   REPEAT    entry   exit       TEP1 N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 25-35;
Related: None;
Repeats: 4;
Topology: Undefined;
Example: Q99973;
Scope:
 Eukaryota; Craniata
Comments: None
XX
# Revision 1.1  2006/07/10
//
AC   PRU00576;
DC   Domain;
TR   PROSITE; PS51230; EB1_C; 1; level=0
XX
Names: EB1-like C-terminal (EB1-C)
Function: Microtubule-associated proteins of the EB1 (end-binding protein 1)
 family have a bipartite composition: the N-terminal CH domain mediates
 microtubule plus end localization and a C-terminal cargo binding domain
 (EB1-C) that captures cell polarity determinants.
XX
CC   -!- SIMILARITY: Contains # EB1 C-terminal domain.
XX
KW   Microtubule
XX
FT   From: PS51230
FT   DOMAIN     from     to       EB1 C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 70-95;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q15691;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2006/10/17
//
AC   PRU00577;
DC   Domain;
TR   PROSITE; PS51231; DAD; 1; level=0
XX
Names: Diaphanous autoregulatory domain (DAD)
 DRF autoregulatory domain
 Diaphanous autoinhibitory domain
Function: The DAD domain is a ~32 amino acid autoinhibitory domain in
 diaphanous-related formins (DRF), which inhibits the activity of the
 DRF catalytical formin homology 2 (FH2) domain to nucleate and elongate
 nonbranched actin filaments.
XX
CC   -!- SIMILARITY: Contains # DAD (diaphanous autoregulatory) domain.
XX
FT   From: PS51231
FT   DOMAIN     from     to       DAD #.
XX
Chop: Nter=0; Cter=0;
Size: 20-40;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Z207;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/07/14
//
AC   PRU00579;
DC   Domain;
TR   PROSITE; PS51232; GBD_FH3; 1; level=0
XX
Names: Rho GTPase-binding/formin homology 3 (GBD/FH3) domain
Function: The GBD/FH3 domain is approximately 380 residues in length. Its role
 appears to be twofold. On one hand the N-terminal region of formins is
 involved in subcellular localization through interaction with diverse
 targets. On the other hand the GBD/FH3 domain is involved in regulation of
 activation by releasing of an intramolecular interaction between the DAD and
 the N-terminus.
XX
CC   -!- SIMILARITY: Contains # GBD/FH3 (Rho GTPase-binding/formin homology
CC       3) domain.
XX
FT   From: PS51232
FT   DOMAIN     from     to       GBD/FH3 #.
XX
Chop: Nter=0; Cter=0;
Size: 360-525;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9Y4D1;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU00580;
DC   Domain;
TR   PROSITE; PS51233; VWFD; 1-6; level=0
XX
Names: VWFD domain profile
Function:   Von   Willebrand   factor  (VWF)  is  a  large,  multimeric  blood
 glycoprotein  synthesized  in  endothelial  cells  and megakaryocytes, that is
 required  for normal hemostasis. The type D domain (VWFD) is not only required
 for  blood clotting factor VIII binding but also for normal multimerization of
 VWF.
XX
CC   -!- SIMILARITY: Contains # VWFD domain.
XX
DR   PROSITE; PS51233; VWFD; 1-6; trigger=no
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51233
FT   DOMAIN     from     to       VWFD #.
FT   DISULFID     24     32       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 200-230;
Related: none;
Repeats: 1-6;
Topology: Undefined;
Example: P04275;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00581;
DC   Domain;
TR   PROSITE; PS51225; MARVEL; 1; level=0
XX
Names: MARVEL domain
Function: The ~130-residue MAL and related proteins for vesicle trafficking
 and membrane link (MARVEL) domain is a module with a four transmembrane-helix
 architecture that has been identified in proteins of the myelin and
 lymphocyte (MAL), physins, gyrins and occludin families.
XX
CC   -!- SIMILARITY: Contains # MARVEL domain.
XX
DR   General; Transmembrane; -; 4; trigger=no
XX
GO   GO:0016020; C:membrane
GO   GO:0016021; C:integral to membrane
XX
KW   Membrane
KW   Transmembrane
XX
FT   From: PS51225
FT   DOMAIN     from     to       MARVEL #.
XX
Chop: Nter=0; Cter=0;
Size: 115-215;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: Q8IZ96;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2008/11/21
//
AC   PRU00582;
DC   Domain;
TR   PROSITE; PS51252; ANTISTASIN; 1; level=0
XX
Names: Antistasin-like domain
Function: Antistatin is a small, disulphide cross-linked serine protease
 inhibitor isolated from the salivary glands of the Mexican leech. Many
 metazoan proteins share sequence homology with this antistasin-like domain.
XX
CC   -!- SIMILARITY: Contains # antistasin-like domain.
XX
FT   From: PS51252
FT   DOMAIN     from     to       Antistasin-like #.
XX
Chop: Nter=0; Cter=0;
Size: 25-35;
Related: None;
Repeats: 1-6;
Topology: Not cytoplasmic;
Example: P15358;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU00583;
DC   Domain;
TR   PROSITE; PS51253; HTH_CENPB; 1; level=0
XX
Names: CENPB-type HTH domain
Function: The CENPB-type HTH domain is a DNA-binding, helix-turn-helix (HTH)
 domain of about 70-75 amino acids, present in eukaryotic centromere proteins
 and transposases.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # HTH CENPB-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
XX
KW   DNA-binding
KW   Nucleus
XX
FT   From: PS51253
FT   DOMAIN     from     to       HTH CENPB-type #.
FT   DNA_BIND     34     64       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 60-85;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: P07199;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2007/06/07
//
AC   PRU00584;
DC   Domain;
TR   PROSITE; PS51255; ADPK; 1; level=0
XX
Names: ADP-dependent kinase (ADPK) domain
Function: Archeal ADP-dependent glucokinases (ADPGKs) and phosphofructokinases
 (ADPPKKs) form an ADP-dependent kinase (ADPK) family, which was tentatively
 named the PFKC family. A ~460-residue ADPK domain is also found in a
 bifunctional ADP-dependent gluco/phosphofructo-kinase (ADP-GK/PFK) from
 Methanococcus jannaschii as well as in homologous hypothetical proteins
 present in several eukaryotes.
XX
DE   + RecName: EC=2.7.1.-;
XX
case <FTGroup:1>
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
end case
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis.
CC   -!- SIMILARITY: Contains # ADPK (ADP-dependent kinase) domain.
XX
GO   GO:0006096; P:glycolysis
GO   GO:0016301; F:kinase activity
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0016740; F:transferase activity
XX
KW   Glycolysis
KW   Kinase
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
KW   Transferase
XX
FT   From: PS51255
FT   DOMAIN     from     to       ADPK #.
FT   ACT_SITE    446    446       Proton acceptor (By similarity).
FT   Condition: D
FT   METAL       267    267       Magnesium (By similarity).
FT   Group: 1; Condition: E
FT   METAL       297    297       Magnesium (By similarity).
FT   Group: 1; Condition: E
FT   METAL       446    446       Magnesium (By similarity).
FT   Group: 1; Condition: D
XX
Chop: Nter=0; Cter=0;
Size: 440-485;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9BRR6;
Scope:
 Eukaryota
 Archaea
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00585;
DC   Domain;
TR   PROSITE; PS51256; GS; 1; level=0
XX
Names: GS domain
Function: The GS domain is a short (~30 residues), highly conserved regulatory
 sequence which is found N-terminal to the kinase domain on the cytoplasmic
 side of members of the type I TGF-beta receptor (TbetaR-I) family. At least
 three, and perhaps four to five of the serines and threonines in the GS
 domain, must be phosphorylated to fully activate TbetaR-1.
XX
CC   -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. TGFB
CC       receptor subfamily.
CC   -!- SIMILARITY: Contains # GS domain.
XX
KW   Phosphoprotein
XX
FT   From: PS51256
FT   DOMAIN     from     to       GS #.
XX
Chop: Nter=0; Cter=0;
Size: 25-35;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: P36896;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2007/10/13
//
AC   PRU00586;
DC   Domain;
TR   PROSITE; PS51262; COS; 1; level=0
XX
Names: COS domain
Function: The COS domain is an ~60-residue module found in N-terminal RING
 finger/B-box/coiled coil (RBCC) or tripartite motif (TRIM) proteins and in a
 distantly related non-RBCC microtubule-binding protein, GLFND.
XX
CC   -!- SIMILARITY: Contains # COS domain.
XX
FT   From: PS51262
FT   DOMAIN     from     to       COS #.
XX
Chop: Nter=0; Cter=0;
Size: 55-65;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q9UJV3;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2007/01/03
//
AC   PRU00587;
DC   Domain;
TR   PROSITE; PS51258; MHD1; 1; level=0
XX
Names: Munc13-homology domain 1 (MHD1)
Function: The MHD1 domain is present in a wide variety of proteins from
 Arabidopsis thaliana, C. elegans, Drosophila melanogaster, mouse, rat and
 human, some of which may function in a Munc13-like manner to regulate
 membrane trafficking.
XX
CC   -!- SIMILARITY: Contains # MHD1 (MUNC13 homology domain 1) domain.
XX
FT   From: PS51258
FT   DOMAIN     from     to       MHD1 #.
XX
Chop: Nter=0; Cter=0;
Size: 115-190;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P27715;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/01/16
//
AC   PRU00588;
DC   Domain;
TR   PROSITE; PS51259; MHD2; 1; level=0
XX
Names: Munc13-homology domain 2 (MHD2)
Function: The MHD2 domain is present in a wide variety of proteins from
 Arabidopsis thaliana, C. elegans, Drosophila melanogaster, mouse, rat and
 human, some of which may function in a Munc13-like manner to regulate
 membrane trafficking.
XX
CC   -!- SIMILARITY: Contains # MHD2 (MUNC13 homology domain 2) domain.
XX
FT   From: PS51259
FT   DOMAIN     from     to       MHD2 #.
XX
Chop: Nter=0; Cter=0;
Size: 105-170;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P27715;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2007/01/17
//
AC   PRU00589;
DC   Domain;
TR   PROSITE; PS51182; C2_TENSIN; 1; level=0
XX
Names: C2 tensin-type domain
Function: Binds phopholipid  membranes  in  a  Ca2+  independant  manner.
XX
CC   -!- SIMILARITY: Contains # C2 tensin-type domain.
FT   From: any
FT   DOMAIN     from     to       C2 tensin-type #.
XX
Chop: Nter=0; Cter=0;
Size: 110-232;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P60483;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2006/10/17
//
AC   PRU00590;
DC   Domain;
TR   PROSITE; PS51181; PPASE_TENSIN; 1; level=0
XX
Names: phosphatase tensin-type domain
Function: lipid phosphatase domain.
XX
CC   -!- SIMILARITY: Contains # phosphatase tensin-type domain.
XX
GO   GO:0016787; F:hydrolase activity
GO   GO:0004721; F:phosphoprotein phosphatase activity
XX
KW   Hydrolase
KW   Protein phosphatase
XX
FT   From: PS51181
FT   DOMAIN     from     to       Phosphatase tensin-type #.
FT   ACT_SITE    112    112       Phosphocysteine intermediate (Potential).
FT   Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 137-221;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O75061;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2006/12/04
//
AC   PRU00591;
DC   Domain;
TR   PROSITE; PS51170; CW; 1; level=0
XX
Names: cell wall-binding repeat
Function: sugar binding domain.
XX
CC   -!- SIMILARITY: Contains # cell wall-binding repeat.
FT   From: PS51170
FT   REPEAT     from     to       Cell wall-binding #.
XX
Chop: Nter=0; Cter=0;
Size: 13-22;
Related: None;
Repeats: 6-32;
Topology: Undefined;
Example: P18177;
Scope:
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.1  2006/10/17
//
AC   PRU00592;
DC   Domain;
TR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1; level=0
XX
Names: G protein gamma domain
Function: It acts as intermediaries in the transduction of signals generated by transmembrane receptors.
XX
CC   -!- SIMILARITY: Contains # G protein gamma domain.
FT   From: PS50058
FT   DOMAIN     from     to       G protein gamma #.
XX
Chop: Nter=0; Cter=0;
Size: 60-68;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P49809;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2006/10/17
//
AC   PRU00593;
DC   Domain;
TR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1; level=0
XX
Names: araC/xylS-type HTH domain
Function: The araC/xylS-type HTH domain is a DNA-binding, helix-turn-helix
 (HTH) domain of about 100 amino acids, present in bacterial transcription
 regulators of genes involved in resistance to antibiotics, organic solvents
 and heavy metals.
XX
CC   -!- SIMILARITY: Contains # HTH araC/xylS-type DNA-binding domain.
XX
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS01124
FT   DOMAIN     from     to       HTH araC/xylS-type #.
FT   DNA_BIND     18     39       H-T-H motif (By similarity).
FT   DNA_BIND     66     89       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 80-120;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0ACH5;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2006/10/24
//
AC   PRU00594;
DC   Domain;
TR   PROSITE; PS51166; CBM20; 1; level=0
XX
Names: CBM20 (carbohydrate binding type-20) domain
Function: has been shown to bind granular starch.
XX
CC   -!- SIMILARITY: Contains # CBM20 (carbohydrate binding type-20)
CC       domain.
FT   From: any
FT   DOMAIN     from     to       CBM20 #.
XX
Chop: Nter=0; Cter=0;
Size: 98-122;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P26827;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2006/10/17
//
AC   PRU00595;
DC   Domain;
TR   PROSITE; PS51089; HP; 1; level=0
XX
Names: HP (headpiece) domain
Function: F-actin-binding domain
XX
CC   -!- SIMILARITY: Contains # HP (headpiece) domain.
XX
GO   GO:0003779; F:actin binding
XX
KW   Actin-binding
XX
FT   From: PS51089
FT   DOMAIN     from     to       HP #.
XX
Chop: Nter=0; Cter=0;
Size: 62-67;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O75366;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/10/17
//
AC   PRU00596;
DC   Domain;
TR   PROSITE; PS51199; SF4_HELICASE; 1; level=0
XX
Names: SF4 helicase domain
Function: Undefined
XX
CC   -!- SIMILARITY: Contains # SF4 helicase domain.
XX
GO   GO:0005524; F:ATP binding
GO   GO:0006260; P:DNA replication
GO   GO:0003677; F:DNA binding
GO   GO:0004386; F:helicase activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0000166; F:nucleotide binding
GO   GO:0006269; C:DNA replication, synthesis of RNA primer
GO   GO:0005658; C:alpha DNA polymerase:primase complex
XX
KW   ATP-binding
KW   DNA replication
KW   DNA-binding
KW   Helicase
KW   Hydrolase
KW   Nucleotide-binding
KW   Primosome
XX
FT   From: PS51199
FT   DOMAIN     from     to       SF4 helicase #.
FT   NP_BIND      32     39       ATP (Potential).
XX
Chop: Nter=0; Cter=0;
Size: 250-298;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P57611;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.1  2006/10/17
//
AC   PRU00597;
DC   Domain;
TR   PROSITE; PS51164; CBM1_2; 1; level=0
XX
Names: CBM1 (fungal-type carbohydrate-binding) domain
Function: carbohydrate-binding  module.
XX
CC   -!- SIMILARITY: Contains # CBM1 (fungal-type carbohydrate-binding)
CC       domain.
FT   From: PS51164
FT   DOMAIN     from     to       CBM1 #.
XX
Chop: Nter=0; Cter=0;
Size: 26-43;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: O14405;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/10/17
//
AC   PRU00599;
DC   Domain;
TR   PROSITE; PS51263; ADF_H; 1; level=0
XX
Names: ADF-H domain
Function: The actin-depolymerizing factor homology (ADF-H) domain is an ~150-
 amino acid motif present in three phylogenetically distinct classes of
 eukaryotic actin-binding proteins that all appear to use the ADF-H domain for
 their interactions with actin.
XX
CC   -!- SIMILARITY: Contains # ADF-H domain.
XX
GO   GO:0003779; F:actin binding
XX
KW   Actin-binding
XX
FT   From: PS51263
FT   DOMAIN     from     to       ADF-H #.
XX
Chop: Nter=0; Cter=0;
Size: 125-160;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P23528;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/01/19
//
AC   PRU00600;
DC   Domain;
TR   PROSITE; PS51265; ZF_DBF4; 1; level=0
XX
Names: DBF4-type zinc finger
Function: involved in the initiation  of  DNA  replication
XX
CC   -!- SIMILARITY: Contains # DBF4-type zinc finger.
FT   From: PS51265
FT   ZN_FING    from     to       DBF4-type #.
XX
Chop: Nter=0; Cter=0;
Size: 49-69;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UBU7;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2008/04/22
//
AC   PRU00602;
DC   Domain;
TR   PROSITE; PS51269; COMM; 1; level=0
XX
Names: COMM domain
Function: The proteins designated as COMMD or COMM domain containing 1-10 are
 extensively conserved in multicellular eukaryotic organisms. The protein
 family is defined by the presence of a C-terminal motif termed COMM domain,
 which functions as an interface for protein-protein interactions.
XX
CC   -!- SIMILARITY: Contains # COMM domain.
XX
FT   From: PS51269
FT   DOMAIN     from     to       COMM #.
XX
Chop: Nter=0; Cter=0;
Size: 60-80;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8N668;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/01/18
//
AC   PRU00603;
DC   Domain;
TR   PROSITE; PS51271; WAPL; 1; level=0
XX
Names: WAPL domain
Function: The WINGS APART-LIKE (WAPL) protein of Drosophila melanogaster
 regulates heterochromatin structure. Although the high-sequence conservation
 is limited to a third of the protein sequence, a WAPL homologue has been
 identified in mammals.
XX
CC   -!- SIMILARITY: Contains # WAPL domain.
XX
FT   From: PS51271
FT   DOMAIN     from     to       WAPL #.
XX
Chop: Nter=0; Cter=0;
Size: 505-550;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9W517;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2007/01/18
//
AC   PRU00604;
DC   Domain;
TR   PROSITE; PS51277; BURP; 1; level=0
XX
Names: BURP domain
Function: The BURP domain is a ~230-residue module, which is found in the C-
 terminal part of a number of plant cell wall proteins. It is possible that
 the BURP domain represents a general motif for localization of proteins
 within the cell wall matrix.
XX
CC   -!- SIMILARITY: Contains # BURP domain.
XX
FT   From: PS51277
FT   DOMAIN     from     to       BURP #.
XX
Chop: Nter=0; Cter=0;
Size: 190-220;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q08298;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.1  2007/01/18
//
AC   PRU00605;
DC   Domain;
TR   PROSITE; PS51273; GATASE_TYPE_1; 1; level=0
XX
Names: Glutamine amidotransferase (GATase) type 1 domain
 trpG-type gatase
 GATases class-I
 triad type GATase
Function: GATases are enzymes that catalyze the removal of the ammonia group
 from glutamine and transfer this group to a substrate to form a new
 carbon-nitrogen group. In the GATase type 1 domain the catalytic cysteine is
 located in a triad of Cys-His-Glu that forms the active site.
XX
CC   -!- SIMILARITY: Contains # glutamine amidotransferase type-1 domain.
XX
case <Feature:PS51273:77=C>
GO   GO:0006541; P:glutamine metabolism
XX
KW   Glutamine amidotransferase
end case
XX
FT   From: PS51273
FT   DOMAIN     from     to       Glutamine amidotransferase type-1 #.
case <Feature:PS51273:77=C>
FT   ACT_SITE     77     77       Nucleophile (By similarity).
FT   Condition: C
FT   ACT_SITE    163    163       By similarity.
FT   Condition: H
FT   ACT_SITE    165    165       By similarity.
FT   Condition: E
end case
XX
Warn: Proteins with this domain may have different enzymatic activities (EC 2.4.2.-, EC 2.4.2.14, EC 4.1.3.27, EC 4.1.3.-, EC 6.3.4.2, EC 6.3.5.2, EC 6.3.5.5 or EC 6.3.5.3).
Chop: Nter=0; Cter=6;
Size: 165-300;
Related: PRU00480; PRU00606; PRU00607; PRU00608;
Repeats: 1-2;
Topology: Undefined;
Example: P0A6F1;
Scope:
 Bacteria
 Eukaryota
 Archaea
 Viruses
Comments: None
XX
# Revision 1.2  2006/12/08
//
AC   PRU00606;
DC   Domain;
TR   PROSITE; PS51274; GATASE_COBBQ; 1; level=0
XX
Names: CobBQ-type glutamine amidotransferase (GATase) domain
 glutaminase domain
 GATase class-I of cobyrinic/cobyric acid synthetase
Function: GATases are enzymes that catalyze the removal of the ammonia group
 from glutamine and transfer this group to a substrate to form a new
 carbon-nitrogen group. The GATase domain of cobB and cobQ family proteins is
 involved in the biosynthesis of cobalamin (vitamin B12). The catalytic Cys is
 located in a Cys-His active site that resembles that of GATases type 1.
XX
CC   -!- SIMILARITY: Contains # GATase cobBQ-type domain.
XX
GO   GO:0009236; P:cobalamin biosynthesis
GO   GO:0006541; P:glutamine metabolism
XX
KW   Cobalamin biosynthesis
KW   Glutamine amidotransferase
XX
FT   From: PS51274
FT   DOMAIN     from     to       GATase cobBQ-type #.
case <Feature:PS51274:82=C>
FT   ACT_SITE     82     82       Nucleophile (By similarity).
FT   Condition: C
FT   ACT_SITE    186    186       By similarity.
FT   Condition: H
end case
XX
Chop: Nter=0; Cter=0;
Size: 160-230;
Related: PRU00605; PRU00480;
Repeats: 1;
Topology: Undefined;
Example: Q57908;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2006/12/08
//
AC   PRU00607;
DC   Domain;
TR   PROSITE; PS51275; PEPTIDASE_C26_GGH; 1; level=0
XX
Names: Gamma-glutamyl hydrolase domain
 Peptidase C26 family. GGH subfamily.
Function: Gamma-glutamyl hydrolase (GGH) (EC 3.4.19.9) is an enzyme that
 cleaves gamma-linked glutamyl bonds, and with particular substrate the enzyme
 acts as an endopeptidase.
XX
case <Feature:PS51275:110=C>
DE   + RecName: EC=3.4.19.9;
end case
XX
CC   -!- SIMILARITY: Contains # gamma-glutamyl hydrolase domain.
XX
case <Feature:PS51275:110=C>
GO   GO:0008464; F:gamma-glutamyl hydrolase activity
GO   GO:0016787; F:hydrolase activity
XX
KW   Hydrolase
end case
XX
FT   From: PS51275
FT   DOMAIN     from     to       Gamma-glutamyl hydrolase #.
case <Feature:PS51275:110=C>
FT   ACT_SITE    110    110       Nucleophile (By similarity).
FT   Condition: C
FT   ACT_SITE    222    222       By similarity.
FT   Condition: H
end case
XX
Chop: Nter=0; Cter=0;
Size: 280-310;
Related: PRU00605;
Repeats: 1;
Topology: Undefined;
Example: Q92820;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00608;
DC   Domain;
TR   PROSITE; PS51276; PEPTIDASE_C56_PFPI; 1; level=0
XX
Names: PfpI endopeptidase domain
 Peptidase C56 family. PfpI endopeptidase subfamily.
Function: Pfpi-like intracellular proteases are cysteine peptidases, with a
 GATase type 1-like active site.
XX
case <Feature:PS51276:101=C>
DE   + RecName: EC=3.2.-.-;
end case
XX
CC   -!- SIMILARITY: Contains # PfpI endopeptidase domain.
XX
case <Feature:PS51276:101=C>
GO   GO:0016787; F:hydrolase activity
GO   GO:0008233; F:peptidase activity
XX
KW   Hydrolase
KW   Protease
end case
XX
FT   From: PS51276
FT   DOMAIN    entry   exit       PfpI endopeptidase #.
case <Feature:PS51276:101=C>
FT   ACT_SITE    101    101       Nucleophile (By similarity).
FT   Condition: C
FT   ACT_SITE    102    102       Potential.
FT   Condition: H
end case
XX
Chop: Nter=0; Cter=0;
Size: 160-180;
Related: PRU00605;
Repeats: 1-2;
Topology: Undefined;
Example: Q51732;
Scope:
 Bacteria
 Eukaryota
 Archaea
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00609;
DC   Domain;
TR   PROSITE; PS51278; GATASE_TYPE_2; 1; level=0
XX
Names: Glutamine amidotransferase (GATase) type 2 domain
 purF-type gatase
 GATases class-II
 N-terminal nucleophile (Ntn) type GATase
Function: GATases are enzymes that catalyze the removal of the ammonia group
 from glutamine and transfer this group to a substrate to form a new
 carbon-nitrogen group. In the GATase type 2 domain the active site is formed
 by a cysteine present at the N-terminal extremity.
XX
CC   -!- SIMILARITY: Contains # glutamine amidotransferase type-2 domain.
XX
case <Feature:PS51278:1=C>
GO   GO:0006541; P:glutamine metabolism
XX
KW   Glutamine amidotransferase
end case
XX
FT   From: PS51278
FT   DOMAIN     from     to       Glutamine amidotransferase type-2 #.
FT   ACT_SITE      1      1       Nucleophile (By similarity).
FT   Condition: C
XX
Warn: Proteins with this domain may have different enzymatic activities (EC 2.4.2.14, EC 2.6.1.16, EC 6.3.5.4, EC 1.4.1.13, EC 1.4.7.1 or EC 1.4.1.14).
Chop: Nter=0; Cter=3;
Size: 175-410;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0AG16;
Scope:
 Bacteria
 Eukaryota
 Archaea
 Viruses
Comments: None
XX
# Revision 1.2  2006/12/08
//
AC   PRU00610;
DC   Domain;
TR   PROSITE; PS51279; BCNT_C; 1; level=0
XX
Names: Bucentaur C-terminal (BCNT-C) domain
Function: The h-type BCNT proteins contain a highly conserved 82-amino acid
 region at the C-terminus (BCNT-C) that is not present in p97BCNT.
XX
CC   -!- SIMILARITY: Contains # BCNT-C domain.
XX
FT   From: PS51279
FT   DOMAIN     from     to       BCNT-C #.
XX
Chop: Nter=0; Cter=0;
Size: 60-85;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UEE9;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/01/18
//
AC   PRU00611;
DC   Domain;
TR   PROSITE; PS51281; TAP_C; 1; level=0
XX
Names: TAP C-terminal (TAP-C) domain
Function: Members of the NXF family of shuttling transport receptors for
 nuclear export of mRNA have a modular structure. Their most C-terminal TAP-C
 domain is important for binding to FG repeat-containing nuclear pore proteins
 (FG-nucleoporins) and is sufficient to mediate nuclear shuttling.
XX
CC   -!- FUNCTION: Involved in the export of mRNA from the nucleus to the
CC       cytoplasm (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Localizes at both the nuclear and cytoplasmic
CC       site of the pores. Shuttles between the nucleus and the cytoplasm
CC       (By similarity).
CC   -!- SIMILARITY: Contains # TAP-C domain.
XX
GO   GO:0006397; P:mRNA processing
GO   GO:0006406; P:mRNA-nucleus export
GO   GO:0005634; C:nucleus
GO   GO:0006810; P:transport
XX
KW   Cytoplasm
KW   mRNA transport
KW   Nucleus
KW   Transport
XX
FT   From: PS51281
FT   DOMAIN     from     to       TAP-C #.
XX
Chop: Nter=0; Cter=0;
Size: 50-60;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P84149;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2007/06/28
//
AC   PRU00612;
DC   Domain;
TR   PROSITE; PS51282; DWNN; 1; level=0
XX
Names: DWNN domain
Function: The ~75-residue DWNN (Domain With No Name) domain is highly
 conserved through eukaryotic species but is absent in prokaryotes. The DWNN
 domain may act as an ubiquitin-like modifier, possibly playing a role in the
 regulation of the splicing machinery.
XX
CC   -!- SIMILARITY: Contains # DWNN domain.
XX
FT   From: PS51282
FT   DOMAIN     from     to       DWNN #.
XX
Chop: Nter=0; Cter=0;
Size: 70-75;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q7Z6E9;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/01/16
//
AC   PRU00613;
DC   Domain;
TR   PROSITE; PS51283; DUSP; 1; level=0
XX
Names: DUSP domain
 Domain present in ubiquitin-specific proteases
Function: The ~120-residue DUSP domain is located in single or tandem copy
 both N- and C-terminal of the ubiquitin carboxyl-terminal hydrolase catalytic
 core domain of deubiquitinating enzymes (DUB).
XX
CC   -!- SIMILARITY: Contains # DUSP domain.
XX
FT   From: PS51283
FT   DOMAIN     from     to       DUSP #.
XX
Chop: Nter=0; Cter=0;
Size: 90-220;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q9USM5;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2007/07/11
//
AC   PRU00614;
DC   Domain;
TR   PROSITE; PS51284; DOC; 1; level=0
XX
Names: DOC domain
 Domain present in ubiquitin-specific proteases
Function: The DOC domain is found in the APC10 subunit of a multi-subunit E3
 protein ubiquitin ligase as well as in several hypothetical proteins that may
 mediate ubiquitination reactions, because they contain combinations of either
 RING finger, cullin or HECT domains.
XX
CC   -!- SIMILARITY: Contains # DOC domain.
XX
FT   From: PS51284
FT   DOMAIN     from     to       DOC #.
XX
Chop: Nter=0; Cter=0;
Size: 175-190;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UM13;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/07/11
//
AC   PRU00615;
DC   Domain;
TR   PROSITE; PS50531; HTH_IS21; 1; level=0
XX
Names: IS21 transposase-type HTH domain
Function: The IS21 transposase-type HTH domain is a putative DNA-binding,
 helix-turn-helix (HTH) domain of about 60-65 amino acids, present in
 transposases of IS21-like prokaryotic insertion sequences.
XX
CC   -!- SIMILARITY: Contains # HTH IS21-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
XX
KW   DNA-binding
XX
FT   From: PS50531
FT   DOMAIN     from     to       HTH IS21-type #.
FT   DNA_BIND     14     35       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 50-75;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0A134;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2007/01/15
//
AC   PRU00616;
DC   Domain;
TR   PROSITE; PS50532; HTH_IS408; 1; level=0
XX
Names: IS408/IS1162 transposase-type HTH domain
Function: The IS408 transposase-type HTH domain is a putative DNA-binding,
 helix-turn-helix (HTH) domain of about 80-85 amino acids, present in
 transposases of IS408/IS1162-like prokaryotic insertion sequences.
XX
CC   -!- SIMILARITY: Contains # HTH IS408-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
XX
KW   DNA-binding
XX
FT   From: PS50532
FT   DOMAIN     from     to       HTH IS408-type #.
FT   DNA_BIND     13     34       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 70-90;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q51761;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.1  2007/01/15
//
AC   PRU00617;
DC   Domain;
TR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1; level=0
XX
Names: UvrD-like helicase C-terminal domain
Function: UvrD helicase unwind DNA with a 3'-5' polarity
XX
CC   -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain.
XX
FT   From: PS51217
FT   DOMAIN     from     to       UvrD-like helicase C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 150-380;
Related: None;
Repeats: 2;
Topology: Undefined;
Example: P64319;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.3  2009/05/28
//
AC   PRU00619;
DC   Domain;
TR   PROSITE; PS51286; RAP; 1; level=0
XX
Names: RAP domain
 RNA-binding domain abundant in Apicomplexans
Function: The RAP domain might mediate a range of cellular functions through
 its potential interactions with RNA.
XX
CC   -!- SIMILARITY: Contains # RAP domain.
XX
FT   From: PS51286
FT   DOMAIN     from     to       RAP #.
XX
Chop: Nter=0; Cter=0;
Size: 55-65;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q53R41;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/08/23
//
AC   PRU00620;
DC   Domain;
TR   PROSITE; PS51287; T_AG_OBD; 1; level=0
XX
Names: Large T-antigen (T-ag) origin-binding domain (OBD)
Function: T-ag is a multidomain protein that contains an N-terminal J domain,
 a central origin-binding domain (OBD), and a C-terminal superfamily 3
 helicase domain.
XX
CC   -!- SIMILARITY: Contains # T-ag OBD DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
XX
KW   DNA-binding
XX
FT   From: PS51287
FT   DNA_BIND   from     to       T-ag OBD #.
XX
Chop: Nter=0; Cter=0;
Size: 110-125;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P03070;
Scope:
 Viruses; dsDNA viruses, no RNA stage
Comments: None
XX
# Revision 1.1  2007/11/29
//
AC   PRU00621;
DC   Domain;
TR   PROSITE; PS51290; CRIC; 1; level=0
XX
Names: CRIC domain
 Conserved region in CNK domain
Function: The CRIC domain is enriched in leucine residues and functions as a
 protein-protein interaction domain.
XX
CC   -!- SIMILARITY: Contains # CRIC domain.
XX
FT   From: PS51290
FT   DOMAIN     from     to       CRIC #.
XX
Chop: Nter=0; Cter=0;
Size: 85-100;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q969H4;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2007/07/10
//
AC   PRU00622;
DC   Domain;
TR   PROSITE; PS51289; GLG1_C_RICH; 1; level=0
XX
Names: Cysteine-rich GLG1 repeat
Function: The cysteine-rich GLG1 repeat from Golgi apparatus protein 1 (GLG1)
 is a ~60-amino acid module that contains 4 Cys residues, which can form
 intrachain disulfide bridges.
XX
CC   -!- SIMILARITY: Contains # Cys-rich GLG1 repeat.
XX
FT   From: PS51289
FT   REPEAT    entry   exit       Cys-rich GLG1 #.
XX
Chop: Nter=0; Cter=0;
Size: 30-80;
Related: None;
Repeats: 2-16;
Topology: Undefined;
Example: Q02391;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2007/01/15
//
AC   PRU00623;
DC   Domain;
TR   PROSITE; PS51292; ZF_RING_CH; 1; level=0
XX
Names: Zinc finger RING-CH-type
Function: The RING-CH-type  is an E3 ligase mainly found in proteins associated to membranes.
XX
CC   -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
CC       ligase activity (By similarity).
CC   -!- SIMILARITY: Contains # RING-CH-type zinc finger.
XX
KW   Ligase
KW   Ubl conjugation pathway
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS51292
FT   ZN_FING    from     to       RING-CH-type #.
XX
Chop: Nter=0; Cter=0;
Size: 50-85;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8TCQ1;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.1  2008/05/08
//
AC   PRU00624;
DC   Domain;
TR   PROSITE; PS51293; SANT; 1; level=0
XX
Names: SANT domain
Function: The SANT domain is a protein-protein interaction module, which can
 bind to histone-tails. Although SANT domains show remarkable sequence and
 structural similarity to the DNA-binding helix-turn-helix (HTH) domain of the
 myb-like tandem repeat (see <PRU00625>), their function is not DNA binding.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # SANT domain.
XX
GO   GO:0005515; F:protein binding
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
XX
FT   From: PS51293
FT   DOMAIN     from     to       SANT #.
XX
Chop: Nter=0; Cter=0;
Size: 30-80;
Related: PRU00133; PRU00625;
Repeats: 1-2;
Topology: Undefined;
Example: Q99543; Q08773;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2009/10/02
//
AC   PRU00625;
DC   Domain;
TR   PROSITE; PS51294; HTH_MYB; 1; level=0
XX
Names: Myb-type HTH DNA-binding domain
 Myb/SANT repeat
Function: The myb-type HTH domain is a DNA-binding, helix-turn-helix (HTH)
 domain of ~55 amino acids, typically occurring in a tandem repeat in
 eukaryotic transcription factors. Some single myb-like domains can be
 involved in other functions, such as protein-binding, but several single
 myb-like domains bind DNA (see <PRU00133>).
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
XX
case <Feature:PS51294:44-52=R-x-N-V-A-S-H-L-Q>
CC   -!- SIMILARITY: Contains # Myb-like GARP DNA-binding domain.
else
CC   -!- SIMILARITY: Contains # HTH myb-type DNA-binding domain.
end case
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
GO   GO:0005634; C:nucleus
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51294
case <Feature:PS51294:44-52=R-x-N-V-A-S-H-L-Q>
FT   DNA_BIND  entry   exit       Myb-like GARP #.
else
FT   DOMAIN    entry   exit       HTH myb-type #.
FT   DNA_BIND     30     55       H-T-H motif (By similarity).
end case
XX
Chop: Nter=0; Cter=0;
Size: 40-80;
Related: PRU00133; PRU00624;
Repeats: 1-5;
Topology: Undefined;
Example: P54274; O49397;
Scope:
 Eukaryota
 Viruses; Avian type C retroviruses
Comments: None
XX
# Revision 1.4  2007/06/07
//
AC   PRU00626;
DC   Domain;
TR   PROSITE; PS51295; CRM; 1; level=0
XX
Names: CRM domain
 Chloroplast RNA splicing and ribosome maturation domain
Function: The CRM domain is an ~100-amino acid RNA-binding domain.
XX
CC   -!- SIMILARITY: Contains # CRM domain.
XX
GO   GO:0003723; F:RNA binding
XX
KW   RNA-binding
XX
FT   From: PS51295
FT   DOMAIN     from     to       CRM #.
XX
Chop: Nter=0; Cter=0;
Size: 95-105;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q84N49;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2007/07/10
//
AC   PRU00627;
DC   Domain;
TR   PROSITE; PS51025; PWI; 1; level=0
XX
Names: PWI domain
Function: The PWI domain, named after a highly conserved PWI tri-peptide
 located within its N-terminal region, is a ~80 amino acid RNA/DNA-binding
 domain that has an equal preference for single- and double-stranded nucleic
 acids and is likely to have multiple important functions in pre-mRNA
 processing.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # PWI domain.
XX
GO   GO:0005634; C:nucleus
GO   GO:0006397; P:mRNA processing
XX
KW   Nucleus
KW   mRNA processing
XX
FT   From: PS51025
FT   DOMAIN     from     to       PWI #.
XX
Chop: Nter=0; Cter=0;
Size: 85-105;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q5ZMJ9;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/07/10
//
AC   PRU00628;
DC   Domain;
TR   PROSITE; PS51296; RIESKE; 1; level=0
XX
Names: Rieske [2Fe-2S] iron-sulfur domain
Function: binds 2Fe-2S iron-sulfur
XX
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
XX
CC   -!- SIMILARITY: Contains # Rieske domain.
XX
case <FTGroup:1>
KW   2Fe-2S
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51296
FT   DOMAIN     from     to       Rieske #.
FT   METAL        41     41       Iron-sulfur (2Fe-2S) (By similarity).
FT   Group: 1; Condition: C
FT   METAL        43     43       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   Group: 1; Condition: H
FT   METAL        61     61       Iron-sulfur (2Fe-2S) (By similarity).
FT   Group: 1; Condition: C
FT   METAL        64     64       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   Group: 1; Condition: H
FT   DISULFID     46     63       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 25-136;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q93SW6;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.6  2009/02/09
//
AC   PRU00629;
DC   Domain;
TR   PROSITE; PS51297; K_BOX; 1; level=0
XX
Names: K-box domain
Function: The 80-amino acid K-box domain was originally identified as a region
 with low but significant similarity to a region of keratin, which is part of
 the coiled-coil sequence constituting the central rod-shaped domain of
 keratin.
XX
CC   -!- SIMILARITY: Contains # K-box domain.
XX
FT   From: PS51297
FT   DOMAIN     from     to       K-box #.
XX
Chop: Nter=0; Cter=0;
Size: 70-95;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P17839;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.1  2007/07/06
//
AC   PRU00630;
DC   Domain;
TR   PROSITE; PS51299; HTH_APSES; 1; level=0
XX
Names: APSES-type HTH DNA_binding domain
Function: The APSES (ASM-1, Phd1, StuA, EFG1, and Sok2) domain is an ~110-
 residue sequence-specific DNA-binding domain found in a family of fungal
 transcription factors that regulate development or cell cycle progression.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # HTH APSES-type DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51299
FT   DOMAIN     from     to       HTH APSES-type #.
FT   DNA_BIND     35     56       H-T-H motif (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: 105-115;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P36011;
Scope:
 Eukaryota; Fungi
Comments: None
XX
# Revision 1.3  2007/06/21
//
AC   PRU00631;
DC   Domain;
TR   PROSITE; PS51301; KILA_N; 1; level=0
XX
Names: KilA-N domain
Function: The amino-terminal module of the poxvirus D6R/NIR proteins defines a
 novel conserved DNA-binding domain (the KilA-N domain) that is found in a
 wide range of proteins of large bacterial and eukaryotic DNA viruses. The
 KilA-N domain has been suggested to be homologous to the fungal DNA-binding
 APSES domain.
XX
CC   -!- SIMILARITY: Contains # KilA-N domain.
XX
FT   From: PS51301
FT   DOMAIN     from     to       KilA-N #.
XX
Chop: Nter=0; Cter=0;
Size: 70-115;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P19653;
Scope:
 Eukaryota
 Viruses
 Bacteria
Comments: None
XX
# Revision 1.1  2007/07/10
//
AC   PRU00632;
DC   Domain;
TR   PROSITE; PS51302; SIM_C; 1; level=0
XX
Names: Single-minded C-terminal domain
Function: Undefined.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # Single-minded C-terminal domain.
XX
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   Nuclear protein
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51302
FT   DOMAIN     from     to       Single-minded C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 320-435;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P81133;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2007/06/21
//
AC   PRU00636;
DC   Domain;
TR   PROSITE; PS51303; PET; 1; level=0
XX
Names: PET domain
Function: The PET domain is a ~110 amino acid motif in the N-terminal part of
 LIM domain proteins, which has been suggested to play a role in
 protein-protein interactions.
XX
CC   -!- SIMILARITY: Contains # PET domain.
XX
FT   From: PS51303
FT   DOMAIN     from     to       PET #.
XX
Chop: Nter=0; Cter=4;
Size: 100-115;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q71QF9;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2007/03/20
//
AC   PRU00637;
DC   Domain;
TR   PROSITE; PS51306; ASD1; 1; level=0
XX
Names: ASD1 domain
Function: ASD1 is required for targeting proteins of the Shroom family to
 actin.
XX
CC   -!- SIMILARITY: Contains # ASD1 domain.
XX
GO   GO:0003779; F:actin binding
XX
KW   Actin-binding
XX
FT   From: PS51306
FT   DOMAIN     from     to       ASD1 #.
XX
Chop: Nter=0; Cter=0;
Size: 85-105;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8TF72;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2007/04/11
//
AC   PRU00638;
DC   Domain;
TR   PROSITE; PS51307; ASD2; 1; level=0
XX
Names: ASD2 domain
Function: ASD2 is capable of eliciting an actomyosin based constriction event
 in proteins of the Shroom family.
XX
CC   -!- SIMILARITY: Contains # ASD2 domain.
XX
FT   From: PS51307
FT   DOMAIN     from     to       ASD2 #.
XX
Chop: Nter=0; Cter=0;
Size: 265-300;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8TF72;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2007/04/11
//
AC   PRU00639;
DC   Domain;
TR   PROSITE; PS51304; GALECTIN; 1; level=0
XX
Names: Galactoside-binding lectin (galectin) domain
Function: Galectins (also known as galaptins or S-lectin) are a family of
 proteins defined by having at least one characteristic carbohydrate
 recognition domain (CRD) with an affinity for beta-galactosides and sharing
 certain sequence elements.
XX
CC   -!- SIMILARITY: Contains # galectin domain.
XX
GO   GO:0005529; F:sugar binding
XX
KW   Lectin
XX
FT   From: PS51304
FT   DOMAIN     from     to       Galectin #.
XX
Chop: Nter=0; Cter=0;
Size: 120-145;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P09382;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.1  2007/06/21
//
AC   PRU00641;
DC   Domain;
TR   PROSITE; PS51309; PABC; 1; level=0
XX
Names: Poly(A)-binding protein C-terminal (PABC) domain
Function: The ~75-residue poly(A)-binding protein C-terminal domain (PABC) is
 binds a conserved motif of 12-15 amino acids, termed PABP-interacting motif
 (PAM)-2.
XX
CC   -!- SIMILARITY: Contains # PABC domain.
XX
FT   From: PS51309
FT   DOMAIN     from     to       PABC #.
XX
Chop: Nter=0; Cter=0;
Size: 75-85;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P11940;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/07/09
//
AC   PRU00642;
DC   Domain;
TR   PROSITE; PS51310; VPS28_C; 1; level=0
XX
Names: VPS28 C-terminal domain
Function: The C-terminal domain of VPS28 is characterized by a high-sequence
 conservation throughout all kingdoms of life. It serves as an adaptor module
 linked to the ESCRT-I complex that connects its function to other components
 of the VPS machinery, including ESCRT-III VPS20.
XX
CC   -!- SIMILARITY: Belongs to the VPS28 family.
CC   -!- SIMILARITY: Contains # VPS28 C-terminal domain.
XX
GO   GO:0015031; P:protein transport
GO   GO:0006810; P:transport
XX
KW   Protein transport
KW   Transport
XX
FT   From: PS51310
FT   DOMAIN     from     to       VPS28 C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 90-100;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UK41;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/07/09
//
AC   PRU00644;
DC   Domain;
TR   PROSITE; PS51312; SB; 1; level=0
XX
Names: Steadiness box (SB) domain
Function: The assembly of the ESCRT-I complex is directed by the C-terminal
 steadiness box (SB) of VPS23, the N-terminal half of VPS28, and the C-
 terminal half of VPS37.
XX
CC   -!- SIMILARITY: Contains # SB (steadiness box) domain.
XX
GO   GO:0015031; P:protein transport
GO   GO:0006810; P:transport
XX
KW   Protein transport
KW   Transport
XX
FT   From: PS51312
FT   DOMAIN     from     to       SB #.
XX
Chop: Nter=0; Cter=0;
Size: 60-90;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q99816;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2007/07/10
//
AC   PRU00645;
DC   Domain;
TR   PROSITE; PS51313; VPS28_N; 1; level=0
XX
Names: VPS28 N-terminal domain
Function: The assembly of the ESCRT-I complex is directed by the C-terminal
 steadiness box (SB) of VPS23, the N-terminal half of VPS28, and the C-
 terminal half of VPS37.
XX
CC   -!- SIMILARITY: Belongs to the VPS28 family.
CC   -!- SIMILARITY: Contains # VPS28 N-terminal domain.
XX
GO   GO:0015031; P:protein transport
GO   GO:0006810; P:transport
XX
KW   Protein transport
KW   Transport
XX
FT   From: PS51313
FT   DOMAIN     from     to       VPS28 N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 95-120;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UK41;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2007/07/10
//
AC   PRU00646;
DC   Domain;
TR   PROSITE; PS51314; VPS37_C; 1; level=0
XX
Names: VPS37 C-terminal domain
Function: The assembly of the ESCRT-I complex is directed by the C-terminal
 steadiness box (SB) of VPS23, the N-terminal half of VPS28, and the C-
 terminal half of VPS37.
XX
CC   -!- SIMILARITY: Contains # VPS37 C-terminal domain.
XX
GO   GO:0015031; P:protein transport
GO   GO:0006810; P:transport
XX
KW   Protein transport
KW   Transport
XX
FT   From: PS51314
FT   DOMAIN     from     to       VPS37 C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 85-95;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8NEZ2;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/07/10
//
AC   PRU00647;
DC   Domain;
TR   PROSITE; PS51316; NBPF; 1; level=0
XX
Names: Neuroblastoma breakpoint family (NBPF) domain
Function: Proteins of the neuroblastoma breakpoint family (NBPF) contain a
 highly conserved domain of unknown function, which has been named the NBPF
 domain.
XX
CC   -!- SIMILARITY: Contains # NBPF domain.
XX
FT   From: PS51316
FT   DOMAIN    entry   exit       NBPF #.
XX
Chop: Nter=0; Cter=0;
Size: 60-120;
Related: None;
Repeats: 1-10;
Topology: Undefined;
Example: Q3BBV0;
Scope:
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia
Comments: None
XX
# Revision 1.2  2007/07/09
//
AC   PRU00648;
DC   Domain;
TR   PROSITE; PS51318; TAT; 1; level=0
XX
Names: Signal peptide
Function: Signal for Twin arginine translocation (Tat) pathway.
XX
DE   + Flags: Precursor;
XX
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
XX
KW   Signal
XX
FT   From: PS51318
FT   SIGNAL        1     to       Tat-type signal (Potential).
FT   CHAIN      to+1   Cter       <name>.
XX
Chop: Nter=0; Cter=0;
Size: 22-45;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8CVZ3;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Bacteriophage
Comments: None
XX
# Revision 1.4  2008/11/07
//
AC   PRU00649;
DC   Domain;
TR   PROSITE; PS51319; TFIIS_N; 1; level=0
XX
Names: TFIIS N-terminal domain
Function: The TFIIS N-terminal domain is a compact four-helix bundle, which is
 also found in other transcription factors and proteins that are predominantly
 nuclear localized.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # TFIIS N-terminal domain.
XX
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
XX
FT   From: PS51319
FT   DOMAIN     from     to       TFIIS N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 70-85;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q96ST2;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/04/23
//
AC   PRU00650;
DC   Domain;
TR   PROSITE; PS51320; TIFY; 1; level=0
XX
Names: Tify domain
Function: The tify domain is a 36-amino acid domain only found among
 Embryophyta (land plants). It has been named after the most conserved amino
 acid pattern (TIF[F/Y]XG] it contains. Tify domain containing proteins might
 be involved in developmental processes and some of them have features that
 are characteristic for transcription factors: a nuclear localization and the
 presence of a putative DNA-binding domain.
XX
CC   -!- SIMILARITY: Contains # tify domain.
XX
FT   From: PS51320
FT   DOMAIN     from     to       Tify #.
XX
Chop: Nter=0; Cter=0;
Size: 35-40;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8H1G0;
Scope:
 Eukaryota; Viridiplantae; Embryophyta
Comments: None
XX
# Revision 1.2  2007/07/06
//
AC   PRU00651;
DC   Domain;
TR   PROSITE; PS51321; TFIIS_CENTRAL; 1; level=0
XX
Names: TFIIS central domain
Function: The transcription factor IIS (TFIIS) is a modular factor that
 comprises an N-terminal domain, a central domain, and a C-terminal TFIIS-type
 zinc finger. The central domain is conserved in TFIIS homologues and
 interacts with RNA polymerase II.
XX
case <OG:Eukaryota>
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
end case
CC   -!- SIMILARITY: Contains # TFIIS central domain.
XX
case <OG:Eukaryota>
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
end case
XX
FT   From: PS51321
FT   DOMAIN     from     to       TFIIS central #.
XX
Chop: Nter=0; Cter=0;
Size: 75-140;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P07273;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.1  2008/12/22
//
AC   PRU00652;
DC   Domain;
TR   PROSITE; PS51322; UEV; 1; level=0
XX
Names: UEV domain
Function: The N-terminal ubiquitin E2 variant (UEV) domain is ~145 amino acid
 residues in length and shows significant sequence similarity to E2 ubiquitin
 ligases but is unable to catalyze ubiquitin transfer as it lacks the active
 site cysteine that forms the transient thioester bond with the C-terminus of
 ubiquitin (Ub). Nevertheless, at least some UEVs have retained the ability to
 bind Ub, and appear to act either as cofactors in ubiquitylation reactions,
 or as ubiquitin sensors.
XX
CC   -!- SIMILARITY: Contains # UEV (ubiquitin E2 variant) domain.
XX
FT   From: PS51322
FT   DOMAIN     from     to       UEV #.
XX
Chop: Nter=0; Cter=0;
Size: 134-160;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9LHG8;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/12/16
//
AC   PRU00653;
DC   Domain;
TR   PROSITE; PS51323; IGFBP_N_2; 1; level=0
XX
Names: Insulin-like growth factor binding protein N-terminal domain
 IGFBP N-terminal domain
Function: The IGFBP N-terminal domain participates in binding to IGFs.
XX
CC   -!- SIMILARITY: Contains # IGFBP N-terminal domain.
XX
DR   PROSITE; PS00222; IGFBP_N_1; 1; trigger=no
XX
FT   From: PS51323
FT   DOMAIN     from     to       IGFBP N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 60-100;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P48745;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2007/12/05
//
AC   PRU00654;
DC   Domain;
TR   PROSITE; PS51324; ERV_ALR; 1; level=0
XX
Names: ERV/ALR sulfhydryl oxidase domain
Function: The ~100-residue ERV/ALR sulfhydryl oxidase domain is a versatile
 module adapted for catalysis of disulfide bond formation in various
 organelles and biological settings.
XX
case <Feature:PS51324:48-51=C-x*-C>
DE   + RecName: Full=FAD-linked sulfhydryl oxidase;
DE            EC=1.8.3.2;
XX
CC   -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes
CC       disulfide bond formation (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4 R'C(R)SH + O(2) = 2 R'C(R)S-S(R)CR' + 2
CC       H(2)O.
CC   -!- COFACTOR: FAD (By similarity).
end case
CC   -!- SIMILARITY: Contains # ERV/ALR sulfhydryl oxidase domain.
XX
case <Feature:PS51324:48-51=C-x*-C>
GO   GO:0055114; P:oxidation-reduction process
GO   GO:0016491; F:oxidoreductase activity
GO   GO:0016972; F:thiol oxidase activity
XX
KW   FAD
KW   Flavoprotein
KW   Oxidoreductase
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51324
FT   DOMAIN     from     to       ERV/ALR sulfhydryl oxidase #.
FT   DISULFID     48     51       Redox-active (By similarity).
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     78     95       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 84-120;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P55789;
Scope:
 Eukaryota
 Viruses; dsDNA viruses, no RNA stage
Comments: None;
XX
# Revision 1.3  2010/12/02
//
AC   PRU00655;
DC   Domain;
TR   PROSITE; PS51325; ALPHA_BOX; 1; level=0
XX
Names: Alpha box DNA-binding domain
Function: All ascomycete MAT idiomorphs encode proteins with confirmed or
 putative DNA-binding motifs, such as an alpha box for MAT1-1 strains and a
 high mobility group (HMG) DNA-binding domain for MAT1-2 strains.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the MATALPHA1 family.
CC   -!- SIMILARITY: Contains # alpha box DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51325
FT   DNA_BIND   from     to       Alpha box #.
XX
Chop: Nter=0; Cter=0;
Size: 55-60;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P01365;
Scope:
 Eukaryota; Fungi; Ascomycota
Comments: None
XX
# Revision 1.1  2008/04/14
//
AC   PRU00656;
DC   Domain;
TR   PROSITE; PS51326; AVIDIN_2; 1; level=0
XX
Names: Avidin-like domain
Function: Avidin and streptavidin both form homotetrameric complexes of
 noncovalently associated chains. Each chain forms a very strong and specific
 non-covalent complex with one molecule of biotin. The fibropellin avidin-like
 domain forms a homotetramer incapable of binding biotin.
XX
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Contains # avidin-like domain.
XX
DR   PROSITE; PS00577; AVIDIN_1; 1; trigger=no
XX
KW   Secreted
XX
FT   From: PS51326
FT   DOMAIN     from     to       Avidin-like #.
XX
Chop: Nter=0; Cter=0;
Size: 115-125;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P02701;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2007/12/05
//
AC   PRU00657;
DC   Domain;
TR   PROSITE; PS51327; DICER_DSRBF; 1; level=0
XX
Names: Dicer double-stranded RNA-binding fold domain
Function: A typical eukaryotic Dicer consists of a helicase domain, a domain
 of unknown function, and a PAZ domain at the amino (N)-terminus as well as
 two ribonuclease III domains and a dsRNA-binding domain (dsRBD) at the
 carboxy (C)-terminus.
XX
case <AnyFeature:PS51192> and <AnyFeature:PS51194>
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
end case
CC   -!- SIMILARITY: Contains # Dicer dsRNA-binding fold domain.
XX
GO   GO:0003723; F:RNA binding
XX
KW   RNA-binding
XX
FT   From: PS51327
FT   DOMAIN     from     to       Dicer dsRNA-binding fold #.
XX
Chop: Nter=0; Cter=0;
Size: 90-100;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UPY3;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/04/17
//
AC   PRU00658;
DC   Domain;
TR   PROSITE; PS51328; L_LECTIN_LIKE; 1; level=0
XX
Names: L-type lectin-like (leguminous) domain
Function: The L-type lectin-like domain is a carbohydrate recognition domain
 (CRD) with an overall globular shape composed of a beta-sandwich of two major
 twisted antiparallel beta-sheet.
XX
CC   -!- SIMILARITY: Contains # L-type lectin-like domain.
XX
GO   GO:0005529; F:sugar binding
XX
KW   Lectin
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51328
FT   DOMAIN     from     to       L-type lectin-like #.
FT   DISULFID    146    185       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 215-230;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q12396;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.4  2009/02/09
//
AC   PRU00659;
DC   Domain;
TR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1; level=0
XX
Names: C-CAP/cofactor C-like domain
Function: The C-CAP/cofactor C-like domain is a protein interaction domain
 present in several cytoskeleton-related proteins.
XX
CC   -!- SIMILARITY: Contains # C-CAP/cofactor C-like domain.
XX
DR   PROSITE; PS01088; CAP_1; 0-1; trigger=no
DR   PROSITE; PS01089; CAP_2; 0-1; trigger=no
XX
FT   From: PS51329
FT   DOMAIN     from     to       C-CAP/cofactor C-like #.
XX
Chop: Nter=0; Cter=0;
Size: 130-160;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q01518;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2008/04/23
//
AC   PRU00660;
DC   Domain;
TR   PROSITE; PS51330; DHFR_2; 1; level=0
XX
Names: Dihydrofolate reductase (DHFR) domain
Function: Dihydrofolate reductases (DHFRs) (EC 1.5.1.3) are ubiquitous enzymes
 which catalyze the NADPH-linked reduction of 7,8-dihydrofolate to 5,6,7,8-
 tetrahydrofolate.
XX
DE   + RecName: EC=1.5.1.3;
XX
CC   -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
CC       dihydrofolate + NADPH.
CC   -!- SIMILARITY: Contains # DHFR (dihydrofolate reductase) domain.
XX
DR   PROSITE; PS00075; DHFR_1; 1; trigger=no
XX
GO   GO:0004146; F:dihydrofolate reductase activity
GO   GO:0055114; P:oxidation-reduction process
GO   GO:0050661; F:NADP or NADPH binding
XX
KW   NADP
KW   Oxidoreductase
XX
FT   From: PS51330
FT   DOMAIN     from     to       DHFR #.
XX
Chop: Nter=0; Cter=0;
Size: 145-257;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5V3R2;
Scope:
 Bacteria
 Eukaryota
 Viruses
 Archaea
Comments: None;
XX
# Revision 1.2  2010/12/02
//
AC   PRU00661;
DC   Domain;
TR   PROSITE; PS51331; THYX; 1; level=0
XX
Names: Flavin-dependent thymidylate synthase (thyX) domain
Function: The thyx domain contains FAD and methylates dUMP at position 5 of
 the pyrimidine ring.
XX
case not <Triggered>
DE   + RecName: Full=Probable thymidylate synthase;
DE            Short=TS;
DE            Short=TSase;
DE            EC=2.1.1.148;
end case
XX
CC   -!- FUNCTION: Catalyzes the formation of dTMP and tetrahydrofolate
CC       from dUMP and methylenetetrahydrofolate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP +
CC       FADH(2) = dTMP + tetrahydrofolate + FAD.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SIMILARITY: Contains # thyX (flavin-dependent thymidylate
CC       synthase) domain.
XX
GO   GO:0008168; F:methyltransferase activity
GO   GO:0016740; F:transferase activity
GO   GO:0050797; F:thymidylate synthase (FAD) activity
GO   GO:0006231; P:dTMP biosynthetic process
GO   GO:0050660; F:FAD binding
XX
KW   FAD
KW   Flavoprotein
KW   Methyltransferase
KW   Nucleotide biosynthesis
KW   Transferase
XX
FT   From: PS51331
FT   DOMAIN     from     to       ThyX #.
FT   MOTIF        80     90       ThyX motif #.
FT   Condition: R-H-R-X(7,8)-S
XX
Chop: Nter=0; Cter=0;
Size: 183-266;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: O86840;
Scope:
 Bacteria
 Archaea
 Viruses; dsDNA viruses, no RNA stage
 Eukaryota; Dictyostelium
Comments: None;
XX
# Revision 1.4  2009/07/07
//
AC   PRU00663;
DC   Domain;
TR   PROSITE; PS51334; PRONE; 1; level=0
XX
Names: PRONE domain
Function: The PRONE domain has been shown to be necessary and sufficient to
 promote nucleotide release from Rop.
XX
CC   -!- SIMILARITY: Contains # PRONE domain.
XX
GO   GO:0005085; F:guanyl-nucleotide exchange factor activity
XX
KW   Guanine-nucleotide releasing factor
XX
FT   From: PS51334
FT   DOMAIN     from     to       PRONE #.
XX
Chop: Nter=0; Cter=0;
Size: 380-410;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q93ZY2;
Scope:
 Eukaryota; Viridiplantae
Comments: None
XX
# Revision 1.1  2008/04/23
//
AC   PRU00664;
DC   Domain;
TR   PROSITE; PS51335; ELMO; 1; level=0
XX
Names: ELMO domain
Function: The ELMO (for EnguLfment and cell MOtility) domain has been proposed
 to be a GAP domain for ARL2 and other members of the Arf family.
XX
CC   -!- SIMILARITY: Contains # ELMO domain.
XX
FT   From: PS51335
FT   DOMAIN     from     to       ELMO #.
XX
Chop: Nter=0; Cter=0;
Size: 150-185;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q92556;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/04/23
//
AC   PRU00665;
DC   Domain;
TR   PROSITE; PS51336; DM10; 1; level=0
XX
Names: DM10 domain
Function: DM10 domains might act as flagellar NDK regulatory modules or as
 units specifically involved in axonemal targeting or assembly.
XX
CC   -!- SIMILARITY: Contains # DM10 domain.
XX
FT   From: PS51336
FT   DOMAIN     from     to       DM10 #.
XX
Chop: Nter=0; Cter=0;
Size: 85-145;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q5JVL4;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/04/17
//
AC   PRU00666;
DC   Domain;
TR   PROSITE; PS51332; B12_BINDING; 1; level=0
XX
Names: B12-binding domainn
Function: The  B12-binding  domain is mainly found in two families of enzymes present in animals  and  prokaryotes,  which use vitamin B12 (cobalamin) as cofactor.
XX
CC   -!- SIMILARITY: Contains # B12-binding domain.
XX
FT   From: PS51332
FT   DOMAIN     from     to       B12-binding #.
XX
Chop: Nter=0; Cter=0;
Size: 115-145;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q99707;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2010/03/05
//
AC   PRU00668;
DC   Domain;
TR   PROSITE; PS51338; IMD; 1; level=0
XX
Names: N-terminal IRSp53 and MIM homology domain
 IMD
Function: The IMD domain can bind to and bundle actin filaments, bind to
 membranes and interact with the small GTPase Rac .
XX
CC   -!- SIMILARITY: Contains # IMD (IRSp53/MIM homology) domain.
XX
FT   From: PS51338
FT   DOMAIN     from     to       IMD #.
XX
Chop: Nter=0; Cter=0;
Size: 225-255;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: O43312;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/12/04
//
AC   PRU00669;
DC   Domain;
TR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1; level=0
XX
Names: Myotubularin phosphatase domain
Function: Myotubularins phosphatase domain is a 3-phosphatases  specific  for
 membrane-embedded PtdIns3P and PtdIns(3,5)P2, two PIs that function within
 the endosomal-lysosomal pathway
XX
CC   -!- SIMILARITY: Contains # myotubularin phosphatase domain.
XX
FT   From: PS51339
FT   DOMAIN     from     to       Myotubularin phosphatase #.
XX
Chop: Nter=0; Cter=0;
Size: 305-452;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q13496;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2007/11/21
//
AC   PRU00670;
DC   Domain;
TR   PROSITE; PS51340; MOSC; 1; level=0
XX
Names: MOSC domain
Function: The MOSC domain is predicted to be a sulfur-carrier domain that
 receives sulfur abstracted by the pyridoxal phosphate-dependent NifS-like
 enzymes, on its conserved cysteine, and delivers it for the formation of
 diverse sulfur-metal clusters.
XX
CC   -!- SIMILARITY: Contains # MOSC domain.
XX
FT   From: PS51340
FT   DOMAIN     from     to       MOSC #.
XX
Chop: Nter=0; Cter=0;
Size: 65-185;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q9C5X8;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2008/04/11
//
AC   PRU00671;
DC   Domain;
TR   PROSITE; PS51341; ZF_LTAG_D1; 1; level=0
XX
Names: Zinc finger large T-antigen (T-ag) D1-type
Function: Undefined.
XX
CC   -!- SIMILARITY: Contains # T-ag D1-type zinc finger.
XX
GO   GO:0008270; F:zinc ion binding
GO   GO:0046872; F:metal ion binding
XX
KW   Metal-binding
KW   Zinc
KW   Zinc-finger
XX
FT   From: PS51341
FT   ZN_FING    from     to       T-ag D1-type #.
XX
Chop: Nter=0; Cter=0;
Size: 90-100;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P03070;
Scope:
 Viruses; dsDNA viruses, no RNA stage
Comments: None
XX
# Revision 1.1  2007/11/30
//
AC   PRU00672;
DC   Site;
TR   PROSITE; PS00005; PKC_PHOSPHO_SITE; 1; level=1
XX
Names: Protein kinase C phosphorylation site
Function: In vivo, protein kinase C exhibits a preference for the
 phosphorylation of serine or threonine residues found close to a C-terminal
 basic residue.
XX
KW   Phosphoprotein
XX
FT   From: PS00005
FT   MOD_RES       1      1       Phosphoserine (By similarity).
FT   Condition: S
FT   MOD_RES       1      1       Phosphothreonine (By similarity).
FT   Condition: T
XX
Chop: Nter=0; Cter=0;
Size: 3;
Related: None;
Repeats: unlimited; no keyword;
Topology: Undefined;
Example: P03070;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.1  2007/12/03
//
AC   PRU00673;
DC   Site;
TR   PROSITE; PS00006; CK2_PHOSPHO_SITE; 1; level=1
XX
Names: Casein kinase II phosphorylation site
Function: Casein kinase II (CK-2) is a protein serine/threonine kinase whose
 activity is independent of cyclic nucleotides and calcium.
XX
KW   Phosphoprotein
XX
FT   From: PS00006
FT   MOD_RES       1      1       Phosphoserine (By similarity).
FT   Condition: S
FT   MOD_RES       1      1       Phosphothreonine (By similarity).
FT   Condition: T
XX
Chop: Nter=0; Cter=0;
Size: 3;
Related: None;
Repeats: unlimited; no keyword;
Topology: Undefined;
Example: P03070;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.1  2007/12/03
//
AC   PRU00674;
DC   Domain;
TR   PROSITE; PS51342; COLIPASE_2; 1; level=0
XX
Names: Colipase family
Function: Colipase is a small protein of ~100 amino acids that functions as a
 cofactor for pancreatic lipase. It also binds to the bile-salt covered
 triacylglycerol interface thus allowing the enzyme to anchor itself to the
 water-lipid interface. Colipases contain ten cysteines involved in five
 disulfide bonds.
XX
case <FTGroup:1>
CC   -!- FUNCTION: Colipase is a cofactor of pancreatic lipase. It allows
CC       the lipase to anchor itself to the lipid-water interface. Without
CC       colipase the enzyme is washed off by bile salts, which have an
CC       inhibitory effect on the lipase (By similarity).
CC   -!- SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic lipase
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed by the pancreas.
end case
CC   -!- SIMILARITY: Belongs to the colipase family.
XX
case <FTGroup:1>
DR   PROSITE; PS00121; COLIPASE_1; 1; trigger=no
XX
GO   GO:0007586; P:digestion
GO   GO:0016042; P:lipid catabolic process
XX
KW   Digestion
KW   Lipid degradation
KW   Secreted
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51342
FT   DISULFID     12     23       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID     18     34       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID     22     56       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID     44     64       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
FT   DISULFID     58     82       By similarity.
FT   Tag: disulf; Group: 1; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 80-90;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q91XL7;
Scope:
 Eukaryota; Metazoa; Vertebrata
Comments: None
XX
# Revision 1.3  2009/02/09
//
AC   PRU00675;
DC   Domain;
TR   PROSITE; PS51343; PII_GLNB_DOM; 1; level=0
XX
Names: P-II protein family
 PII protein
 P(II) protein
Function: P-II family proteins are regulators of nitrogen metabolism.
XX
case <OC:Rhodophyta> or <OC:Viridiplantae>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
end case
CC   -!- SIMILARITY: Belongs to the P(II) protein family.
XX
case <Feature:PS51343:51=Y>
DR   PROSITE; PS00496; PII_GLNB_UMP; 1; trigger=no
end case
DR   PROSITE; PS00638; PII_GLNB_CTER; 1; trigger=no
XX
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
case <Feature:PS51343:51=Y>
GO   GO:0000166; F:nucleotide binding
end case
case <OC:Rhodophyta> or <OC:Viridiplantae>
GO   GO:0009507; C:chloroplast
end case
XX
KW   Transcription
KW   Transcription regulation
case <Feature:PS51343:51=Y>
KW   Nucleotide-binding
end case
case <OC:Rhodophyta> or <OC:Viridiplantae>
KW   Chloroplast
KW   Plastid
end case
XX
FT   From: PS51343
FT   MOD_RES      51     51       O-UMP-tyrosine (By similarity).
FT   Condition: Y
XX
Chop: Nter=0; Cter=0;
Size: 100-135;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9CJK1; Q9TM37;
Scope:
 Eukaryota; Rhodophyta
 Eukaryota; Viridiplantae
 Archaea
 Bacteria
 Plastid
Comments: None
XX
# Revision 1.2  2009/04/08
//
AC   PRU00676;
DC   Domain;
TR   PROSITE; PS51344; HTH_TFE_IIE; 1; level=0
XX
Names: TFE/IIEalpha-type HTH domain
Function: It has been proposed that the TFE/IIEalpha-type HTH domain acts as a
 bridging factor or adapter between the TATA box-binding protein, the
 polymerase, and possibly promoter DNA.
XX
CC   -!- SIMILARITY: Contains # HTH TFE/IIEalpha-type domain.
XX
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51344
FT   DOMAIN     from     to       HTH TFE/IIEalpha-type #.
XX
Chop: Nter=0; Cter=0;
Size: 85-110;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P29083;
Scope:
 Eukaryota
 Archaea
Comments: None
XX
# Revision 1.1  2008/01/14
//
AC   PRU00677;
DC   Domain;
TR   PROSITE; PS51345; MYOTOXINS_2; 1; level=0
XX
Names: Myotoxins family
Function: Myotoxins are small basic peptides (42 to 45 residues) from the 
 venom of rattlesnakes that cause severe muscle necrosis by a non-enzymatic 
 mechanism. Myotoxins contain six cysteines involved in three disulfide bonds.
XX
case <Feature:PS00459>
CC   -!- FUNCTION: This toxin specifically modifies voltage-sensitive
CC       sodium channels, it exhibits analgesic activity and causes severe
CC       muscle necrosis by a non-enzymatic mechanism. Moreover, it
CC       actively interacts with lipid membranes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
end case
CC   -!- SIMILARITY: Belongs to the snake toxin myotoxin family.
XX
DR   PROSITE; PS00459; MYOTOXINS_1; 0-1; trigger=no
XX
case <Feature:PS00459>
GO   GO:0019871; F:sodium channel inhibitor activity
GO   GO:0008200; F:ion channel inhibitor activity
GO   GO:0009405; P:pathogenesis
XX
KW   Secreted
KW   Sodium channel inhibitor
KW   Ionic channel inhibitor
KW   Myotoxin
KW   Toxin
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51345
FT   DISULFID      4     36       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     11     30       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     18     37       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 35-50;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O73799;
Scope:
 Eukaryota; Metazoa; Squamata; Serpentes
Comments: None
XX
# Revision 1.2  2009/02/09
//
AC   PRU00678;
DC   Domain;
TR   PROSITE; PS51346; PROKAR_ZN_DEPEND_PLPC_2; 1; level=0
XX
Names: Prokaryotic zinc-dependent phospholipase C domain
Function: Phospholipase C (EC 3.1.4.3) has a ~245 amino-acids domain 
 with the active site (PLC) in a cleft which is also occupied by 3 zinc 
 ions. There are nine conserved residues known to be involved in binding the
 zinc ions: 5 His, 2 Asp, 1 Glu and 1 Trp.
XX
case <FTGroup:1> and <FTGroup:2> and <FTGroup:3>
DE   + AltName: Full=phospholipase C;
DE            EC=3.1.4.3;
DE            Short=PLC;
XX
CC   -!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = 1,2-
CC       diacylglycerol + choline phosphate.
CC   -!- COFACTOR: Binds 3 zinc ions per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
end case
CC   -!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C
CC       family.
CC   -!- SIMILARITY: Contains # Zn-dependent PLC domain.
XX
case <FTGroup:1> and <FTGroup:2> and <FTGroup:3>
DR   PROSITE; PS00384; PROKAR_ZN_DEPEND_PLPC_1; 1; trigger=no
end case
XX
case <FTGroup:1> or <FTGroup:2> or <FTGroup:3>
GO   GO:0016787; F:hydrolase activity
GO   GO:0046872; F:metal ion binding
GO   GO:0008270; F:zinc ion binding
XX
KW   Hydrolase
KW   Metal-binding
KW   Zinc
end case
XX
FT   From: PS51346
FT   DOMAIN        3     to       Zn-dependent PLC #.
FT   METAL         4      4       Zinc #1 (By similarity).
FT   Group: 1; Condition: W
FT   METAL        14     14       Zinc #1 (By similarity).
FT   Group: 1; Condition: H
FT   METAL        59     59       Zinc #3 (By similarity).
FT   Group: 3; Condition: D
FT   METAL        71     71       Zinc #3 (By similarity).
FT   Group: 3; Condition: H
FT   METAL       129    129       Zinc #3 (By similarity).
FT   Group: 3; Condition: H
FT   METAL       133    133       Zinc #1 (By similarity).
FT   Group: 1; Condition: D
FT   METAL       133    133       Zinc #3 (By similarity).
FT   Group: 3; Condition: D
FT   METAL       139    139       Zinc #2 (By similarity).
FT   Group: 2; Condition: H
FT   METAL       151    151       Zinc #2 (By similarity).
FT   Group: 2; Condition: H
FT   METAL       155    155       Zinc #2 (By similarity).
FT   Group: 2; Condition: E
XX
Chop: Nter=3; Cter=0;
Size: 230-260;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q46150;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU00679;
DC   Domain;
TR   PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1; level=0
XX
Names: Phosphotriesterase family
Function: The enzyme phosphotriesterase (EC 3.1.8.1) (PTE) (also known as
 parathion hydrolase) belongs to a family of enzymes that possess a binuclear
 zinc metal center at their active site. The two zinc ions are coordinated by
 six different residues, four of which being histidines.
XX
case <FTGroup:1> and <FTGroup:2>
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
end case
CC   -!- SIMILARITY: Belongs to the phosphotriesterase family.
XX
case <FTGroup:1>
DR   PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1; trigger=no
end case
XX
case <FTGroup:1> or <FTGroup:2>
GO   GO:0016787; F:hydrolase activity
GO   GO:0046872; F:metal ion binding
GO   GO:0008270; F:zinc ion binding
XX
KW   Hydrolase
KW   Metal-binding
KW   Zinc
end case
XX
FT   From: PS51347
FT   METAL        21     21       Zinc #1 (By similarity).
FT   Group: 1; Condition: H
FT   METAL        23     23       Zinc #1 (By similarity).
FT   Group: 1; Condition: H
FT   METAL       142    142       Zinc #1; via carbamate group (By
FT                                similarity).
FT   Group: 1; Condition: [KE]
FT   METAL       142    142       Zinc #2; via carbamate group (By
FT                                similarity).
FT   Group: 2; Condition: [KE]
FT   METAL       175    175       Zinc #2 (By similarity).
FT   Group: 2; Condition: H
FT   METAL       204    204       Zinc #2 (By similarity).
FT   Group: 2; Condition: H
FT   METAL       263    263       Zinc #1 (By similarity).
FT   Group: 1; Condition: D
FT   MOD_RES     142    142       N6-carboxylysine (By similarity).
FT   Condition: K
XX
Chop: Nter=0; Cter=0;
Size: 280-360;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0A433;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.3  2008/07/29
//
AC   PRU00680;
DC   Domain;
TR   PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1; level=0
XX
Names: Alpha-lactalbumin / lysozyme C family
Function: Alpha-lactalbumin, a regulatory protein in milk, and lysozyme 
 (EC 3.2.1.17) C (chicken type), which acts as a bacteriolytic enzyme, belong
 to a family of proteins with eight conserved cysteines that form four 
 disulfide bonds. Alpha-lactalbumin lacks the enzymatic activity and the 
 corresponding Glu and Asp residues. Alpha-lactalbumin binds a calcium ion, 
 while most lysozyme C do not bind calcium.
XX
case <FTGroup:1>
DE   + AltName: Full=lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
XX
CC   -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those
CC       in tissues and body fluids are associated with the monocyte-
CC       macrophage system and enhance the activity of immunoagents (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of 1,4-beta-linkages between N-
CC       acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC       peptidoglycan and between N-acetyl-D-glucosamine residues in
CC       chitodextrins.
end case
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
XX
DR   PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; 1; trigger=no
XX
case <FTGroup:1>
GO   GO:0003824; F:catalytic activity
GO   GO:0019835; P:cytolysis
GO   GO:0042742; P:defense response to bacterium
GO   GO:0016798; F:hydrolase activity, acting on glycosyl bonds
GO   GO:0008152; P:metabolic process
GO   GO:0016787; F:hydrolase activity
end case
case <Feature:PS51348:85=D> and <Feature:PS51348:90-91=D-D>
GO   GO:0005509; F:calcium ion binding
end case
XX
case <FTGroup:1>
KW   Antimicrobial
KW   Bacteriolytic enzyme
KW   Glycosidase
KW   Hydrolase
end case
case <Feature:PS51348:85=D> and <Feature:PS51348:90-91=D-D>
KW   Calcium
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51348
FT   ACT_SITE     35     35       By similarity.
FT   Group: 1; Condition: E
FT   ACT_SITE     52     52       By similarity.
FT   Group: 1; Condition: D
case <Feature:PS51348:85=D> and <Feature:PS51348:90-91=D-D>
FT   CA_BIND      81     92       By similarity.
end case
FT   DISULFID      6    125       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     30    114       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     64     80       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     76     94       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 110-140;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q659U0;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00681;
DC   Domain;
TR   PROSITE; PS51350; PTS_HPR_DOM; 1; level=0
XX
Names: PTS HPR domain
Function: The histidine-containing phosphocarrier protein (HPr) is a central
 component of the phosphoenolpyruvate-dependent sugar phosphotransferase
 system (PTS), which transfers metabolic carbohydrates across the cell
 membrane in many bacterial species.
XX
CC   -!- SIMILARITY: Contains # HPr domain.
XX
case <Feature:PS51350:15=H>
DR   PROSITE; PS00369; PTS_HPR_HIS; 1; trigger=no
end case
case <Feature:PS51350:46=S>
DR   PROSITE; PS00589; PTS_HPR_SER; 1; trigger=no
end case
XX
GO   GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system
GO   GO:0016740; F:transferase activity
GO   GO:0016301; F:kinase activity
XX
KW   Kinase
case <Feature:PS51350:46=S> and <OC:Firmicutes>
KW   Phosphoprotein
end case
KW   Phosphotransferase system
KW   Transferase
XX
FT   From: PS51350
FT   DOMAIN     from     to       HPr #.
case <AnyFeature:PS51094:61=H> or <AnyFeature:PS51096:9=H>
FT   ACT_SITE     15     15       Pros-phosphohistidine intermediate; for
FT                                HPr activity (By similarity).
FT   Condition: H
else
FT   ACT_SITE     15     15       Pros-phosphohistidine intermediate (By
FT                                similarity).
FT   Condition: H
end case
case <Feature:PS51350:46=S> and <OC:Firmicutes>
FT   MOD_RES      46     46       Phosphoserine; by HPrK/P (By similarity).
end case
XX
Chop: Nter=0; Cter=0;
Size: 80-95;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P08877;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2008/05/14
//
AC   PRU00682;
DC   Domain;
TR   PROSITE; PS51351; TFIIE_BETA_C; 1; level=0
XX
Names: TFIIE beta central core DNA-binding domain
Function: The ~120-residue central core domain of TFIIE beta plays a role in
 double-stranded DNA binding of TFIIE.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the TFIIE beta subunit family.
CC   -!- SIMILARITY: Contains # TFIIE beta DNA-binding domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51351
FT   DNA_BIND   from     to       TFIIE beta #.
XX
Chop: Nter=0; Cter=0;
Size: 70-85;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q2KJF9;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/04/15
//
AC   PRU00683;
DC   Domain;
TR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1; level=0
XX
Names: FMN-dependent alpha-hydroxy acid dehydrogenase domain
Function: These enzymes are oxidoreductases that act on alpha-hydroxy 
 acids and which are FMN-containing flavoproteins with a TIM barrel 
 structure.
XX
case <Feature:PS51349:278=H>
DE   + RecName: EC=1.-.-.-;
end case
XX
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family.
CC   -!- SIMILARITY: Contains # FMN hydroxy acid dehydrogenase domain.
XX
case <Feature:PS51349:278=H>
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1; trigger=no
XX
GO   GO:0016491; F:oxidoreductase activity
end case
XX
KW   Flavoprotein
KW   FMN
case <Feature:PS51349:278=H>
KW   Oxidoreductase
end case
XX
FT   From: PS51349
FT   DOMAIN     from     to       FMN hydroxy acid dehydrogenase #.
FT   NP_BIND     309    333       FMN (By similarity).
FT   ACT_SITE    278    278       Proton acceptor (By similarity).
FT   Condition: H
FT   BINDING      27     27       Substrate (Potential).
FT   Condition: Y
FT   BINDING     109    109       FMN (By similarity).
FT   Condition: S
FT   BINDING     131    131       FMN (By similarity).
FT   Condition: Q
FT   BINDING     133    133       Substrate (By similarity).
FT   Condition: Y
FT   BINDING     159    159       FMN (By similarity).
FT   Condition: T
FT   BINDING     168    168       Substrate (By similarity).
FT   Condition: R
FT   BINDING     254    254       FMN (By similarity).
FT   Condition: K
FT   BINDING     281    281       Substrate (Potential).
FT   Condition: R
XX
Chop: Nter=0; Cter=0;
Size: 340-390;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6FFS1;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00686;
DC   Domain;
TR   PROSITE; PS51354; GLUTAREDOXIN_2; 1; level=0
XX
Names: Glutaredoxin  domain
Function: It functions as an electron carrier.
XX
CC   -!- SIMILARITY: Contains # glutaredoxin domain.
XX
FT   From: PS51354
FT   DOMAIN     from     to       Glutaredoxin #.
XX
Chop: Nter=0; Cter=0;
Size: 80-130;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P0AC69;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.2  2010/01/26
//
AC   PRU00691;
DC   Domain;
TR   PROSITE; PS51352; THIOREDOXIN_2; 1; level=0
XX
Names: thioredoxin domain
Function: The thioredoxin domain participate in various redox reactions via the reversible oxidation of an active center disulfide bond.
XX
CC   -!- SIMILARITY: Contains # thioredoxin domain.
XX
GO   GO:0045454; P:cell redox homeostasis
XX
FT   From: PS51352
FT   DOMAIN     from     to       Thioredoxin #.
XX
Chop: Nter=0; Cter=0;
Size: 100-200;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: P0A862;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.1  2010/03/05
//
AC   PRU00692;
DC   Domain;
TR   PROSITE; PS51359; COX5B_2; 1; level=0
XX
Names: Cytochrome c oxidase subunit Vb, zinc binding domain
Function: This domain occurs in a subunit which forms a part of the cytochrome
 c oxidase (EC 1.9.3.1) enzymatic complex. It contains 3 to 4 conserved
 cysteine residues which bind a zinc atom.
XX
case <Feature:PS51359:61=C> and <Feature:PS51359:84=C> and <Feature:PS51359:87=C>
DE   + AltName: Full=cytochrome c oxidase subunit;
XX
CC   -!- FUNCTION: This protein is one of the nuclear-coded polypeptide
CC       chains of cytochrome c oxidase, the terminal oxidase in
CC       mitochondrial electron transport (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane (By
CC       similarity).
end case
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase Vb family.
XX
case <Feature:PS51359:61=C> and <Feature:PS51359:84=C> and <Feature:PS51359:87=C>
DR   PROSITE; PS00848; COX5B_1; 1; trigger=no
XX
GO   GO:0016020; C:membrane
GO   GO:0046872; F:metal ion binding
GO   GO:0005739; C:mitochondrion
GO   GO:0008270; F:zinc ion binding
XX
KW   Mitochondrion inner membrane
KW   Membrane
KW   Metal-binding
KW   Mitochondrion
KW   Zinc
end case
XX
FT   From: PS51359
FT   METAL        61     61       Zinc (By similarity).
FT   Condition: C
FT   METAL        63     63       Zinc (By similarity).
FT   Condition: C
FT   METAL        84     84       Zinc (By similarity).
FT   Condition: C
FT   METAL        87     87       Zinc (By similarity).
FT   Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 90-110;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5S3G4;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2008/11/07
//
AC   PRU00693;
DC   Domain;
TR   PROSITE; PS51360; PLUS3; 1; level=0
XX
Names: Plus3 domain
Function: The capacity to bind single-stranded DNA is at least one function of
 the Plus3 domain.
XX
CC   -!- SIMILARITY: Contains # Plus3 domain.
XX
FT   From: PS51360
FT   DOMAIN     from     to       Plus3 #.
XX
Chop: Nter=0; Cter=0;
Size: 125-135;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P53064;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/04/23
//
AC   PRU00694;
DC   Domain;
TR   PROSITE; PS51361; TENEURIN_N; 1; level=0
XX
Names: Teneurin N-terminal domain
Function: The N-terminal intracellular domain of vertebrate teneurins contains
 two EF-hand-like calcium-binding motifs and two polyproline regions involved
 in protein-protein interactions, followed by a single-span transmembrane
 domain.
XX
CC   -!- SIMILARITY: Contains # teneurin N-terminal domain.
XX
FT   From: PS51361
FT   DOMAIN     from     to       Teneurin N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 200-415;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UKZ4;
Scope:
 Eukaryota; Metazoa; Craniata
Comments: None
XX
# Revision 1.1  2008/04/15
//
AC   PRU00695;
DC   Domain;
TR   PROSITE; PS51363; W2; 1; level=0
XX
Names: W2 domain
Function: The W2 domain (two invariant tryptophans) is a region of ~165 amino
 acids which is found in the C-terminus of some eukayrotic initiation factors
 (eIFs).
XX
CC   -!- SIMILARITY: Contains # W2 domain.
XX
FT   From: PS51363
FT   DOMAIN     from     to       W2 #.
XX
Chop: Nter=0; Cter=0;
Size: 60-195;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q04637;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/04/14
//
AC   PRU00698;
DC   Domain;
TR   PROSITE; PS51366; MI; 1; level=0
XX
Names: MI domain
Function: The MI (after MA-3 and eIF4G) domain is a protein-protein
 interaction module of ~130 amino acids that appears in several translation
 factors.
XX
CC   -!- SIMILARITY: Contains # MI domain.
XX
FT   From: PS51366
FT   DOMAIN     from     to       MI #.
XX
Chop: Nter=0; Cter=0;
Size: 110-140;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: Q04637;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/04/24
//
AC   PRU00699;
DC   Domain;
TR   PROSITE; PS51367; THAUMATIN_2; 1; level=0
XX
Names: Thaumatin family
 pathogenesis-related group 5
 PR5-like
 PR-5 family
 osmotin-like
Function: Thaumatin, an intensely sweet-tasting protein from Thaumatococcus 
 daniellii plants and several stress-induced proteins with 8 disulfide bonds
 from plants form this family.
XX
CC   -!- SIMILARITY: Belongs to the thaumatin family.
XX
DR   PROSITE; PS00316; THAUMATIN_1; 1; trigger=no
XX
case <OC:Viridiplantae>
GO   GO:0009607; P:response to biotic stimulus
GO   GO:0006952; P:defense response
end case
XX
case <OC:Viridiplantae>
KW   Pathogenesis-related protein
KW   Plant defense
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51367
FT   DISULFID     10    210       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     56     66       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     71     77       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    124    199       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    129    182       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    137    147       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    151    160       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    161    169       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 140-230;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P81295;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/09
//
AC   PRU00700;
DC   Domain;
TR   PROSITE; PS51368; UREASE_3; 1; level=0
XX
Names: Urease domain
Function: Urease (EC 3.5.1.5) is a nickel-binding enzyme that catalyzes the
 hydrolysis of urea to carbon dioxide and ammonia. The urease domain forms an
 (alpha beta)(8) barrel structure that binds two nickel ions and with a
 histidine that is catalytically involved.
XX
case <Feature:PS51368:192=H> and <FTGroup:1> and <FTGroup:2> and not <OC:Bacteria> and not <OC:Archaea>
DE   + AltName: Full=Urease;
DE            EC=3.5.1.5;
DE   AltName: Full=Urea amidohydrolase;
end case
XX
case <Feature:PS51368:192=H> and <FTGroup:1> and <FTGroup:2>
CC   -!- CATALYTIC ACTIVITY: Urea + H(2)O = CO(2) + 2 NH(3).
end case
case <FTGroup:1> or <FTGroup:2>
CC   -!- COFACTOR: Binds #(nickel,ion) per subunit (By similarity).
end case
case <OC:Bacteria>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
end case
CC   -!- SIMILARITY: Belongs to the urease family.
CC   -!- SIMILARITY: Contains # urease domain.
XX
case <Feature:PS51368:6=H> and <Feature:PS51368:8=H>
DR   PROSITE; PS01120; UREASE_1; 1; trigger=no
end case
case <Feature:PS51368:192=H>
DR   PROSITE; PS00145; UREASE_2; 1; trigger=no
end case
XX
case <Feature:PS51368:192=H>
GO   GO:0016787; F:hydrolase activity
end case
case <FTGroup:1> or <FTGroup:2>
GO   GO:0046872; F:metal ion binding
GO   GO:0016151; F:nickel ion binding
end case
case <OC:Bacteria>
GO   GO:0005737; C:cytoplasm
end case
XX
case <OC:Bacteria>
KW   Cytoplasm
end case
case <Feature:PS51368:192=H>
KW   Hydrolase
end case
case <FTGroup:1> or <FTGroup:2>
KW   Metal-binding
KW   Nickel
end case
XX
FT   From: PS51368
FT   DOMAIN     from     to       Urease #.
FT   ACT_SITE    192    192       Proton donor (By similarity).
FT   Condition: H
FT   METAL         6      6       Nickel #2 (By similarity).
FT   Group: 2; Condition: H
FT   METAL         8      8       Nickel #2 (By similarity).
FT   Group: 2; Condition: H
FT   METAL        89     89       Nickel #1; via carbamate group (By
FT                                similarity).
FT   Group: 1; Condition: K
FT   METAL        89     89       Nickel #2; via carbamate group (By
FT                                similarity).
FT   Group: 2; Condition: K
FT   METAL       118    118       Nickel #1 (By similarity).
FT   Group: 1; Condition: H
FT   METAL       144    144       Nickel #1 (By similarity).
FT   Group: 1; Condition: H
FT   METAL       232    232       Nickel #2 (By similarity).
FT   Group: 2; Condition: D
FT   BINDING      91     91       Substrate (By similarity).
FT   Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 420-470;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5KCQ6;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.7  2009/07/02
//
AC   PRU00701;
DC   Domain;
TR   PROSITE; PS51369; TCP; 1; level=0
XX
Names: TCP domain
Function: So far, members of the TCP family have only been found in plants and
 function in processes related to cell proliferation. The TCP domain is
 probably involved in DNA-binding and protein-protein interactions.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Contains # TCP domain.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51369
FT   DOMAIN     from     to       TCP #.
XX
Chop: Nter=0; Cter=0;
Size: 50-65;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9SPT4;
Scope:
 Eukaryota; Viridiplantae; Embryophyta
Comments: None
XX
# Revision 1.1  2008/02/20
//
AC   PRU00702;
DC   Domain;
TR   PROSITE; PS51370; R; 1; level=0
XX
Names: R domain
Function: Most members of the CYC/TB1 subfamily have an R domain, predicted to
 form a coiled coil that may mediate protein-protein interactions.
XX
CC   -!- SIMILARITY: Contains # R domain.
XX
FT   From: PS51370
FT   DOMAIN     from     to       R #.
XX
Chop: Nter=0; Cter=0;
Size: 15-25;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9SPT4;
Scope:
 Eukaryota; Viridiplantae; Embryophyta
Comments: None
XX
# Revision 1.2  2008/02/25
//
AC   PRU00704;
DC   Domain;
TR   PROSITE; PS51372; PRD_2; 1; level=0
XX
Names: PRD domain
Function: PRDs in transcrptional antiterminators and activators are
 phosphoenolpyruvate:sugar phosphotransferase system (PTS) PTS regulatory
 targets that are (de)phosphorylated in response to the availability of carbon
 sources.
XX
CC   -!- SIMILARITY: Contains # PRD domain.
XX
DR   PROSITE; PS00654; PRD_1; 1; trigger=no
case <FTTag:phospho>
KW   Phosphoprotein
end case
XX
FT   From: PS51372
FT   DOMAIN     from     to       PRD #.
FT   MOD_RES      38     38       Phosphohistidine (By similarity).
FT   Tag: phospho; Condition: H
FT   MOD_RES      97     97       Phosphohistidine (By similarity).
FT   Tag: phospho; Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 95-123;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: P46321;
Scope:
 Bacteria
Comments: None;
XX
# Revision 1.1  2009/04/09
//
AC   PRU00705;
DC   Domain;
TR   PROSITE; PS51373; HIPIP; 1; level=0
XX
Names: High potential iron-sulfur proteins family
Function: High potential iron-sulfur proteins (HiPIP) are a specific class of 
 high-redox potential 4Fe-4S ferredoxins that functions in anaerobic electron
 transport and which occurs commonly in purple photosynthetic bacteria and in
 other bacteria, such as Paracoccus denitrificans and Thiobacillus 
 ferrooxidans.
XX
DE   RecName: Full=High-potential iron-sulfur protein;
DE            Short=HiPIP;
XX
CC   -!- FUNCTION: Specific class of high-redox-potential 4Fe-4S
CC       ferredoxins. Functions in anaerobic electron transport in most
CC       purple and in some other photosynthetic bacteria and in at least
CC       one genus (Paracoccus) of halophilic, denitrifying bacteria.
CC   -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein
CC       (HiPIP) family.
XX
GO   GO:0051539; F:4 iron, 4 sulfur cluster binding
GO   GO:0006118; P:electron transport
GO   GO:0005506; F:iron ion binding
GO   GO:0051536; F:iron-sulfur cluster binding
GO   GO:0046872; F:metal ion binding
GO   GO:0006810; P:transport
GO   GO:0042597; C:periplasmic space
XX
KW   4Fe-4S
KW   Electron transport
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
KW   Periplasm
KW   Transport
XX
FT   From: PS51373
FT   METAL        36     36       Iron-sulfur (4Fe-4S) (By similarity).
FT   Condition: C
FT   METAL        39     39       Iron-sulfur (4Fe-4S) (By similarity).
FT   Condition: C
FT   METAL        53     53       Iron-sulfur (4Fe-4S) (By similarity).
FT   Condition: C
FT   METAL        67     67       Iron-sulfur (4Fe-4S) (By similarity).
FT   Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 55-90;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P59860;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2008/06/07
//
AC   PRU00707;
DC   Domain;
TR   PROSITE; PS51376; DBB; 1; level=0
XX
Names: DBB domain
Function: The DBB domain in both Dof and BCAP is required to mediate self-
 association in yeast cells, indicating that this domain may have a more
 general role in mediating protein-protein interactions.
XX
CC   -!- SIMILARITY: Contains # DBB domain.
XX
FT   From: PS51376
FT   DOMAIN     from     to       DBB #.
XX
Chop: Nter=0; Cter=0;
Size: 125-130;
Related: None;
Repeats: 1;
Topology: Cytoplasmic;
Example: Q8NDB2;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.1  2008/12/19
//
AC   PRU00708;
DC   Domain;
TR   PROSITE; PS51375; PPR; 1; level=0
XX
Names: AdoMet activation domain
Function: Some  of the proteins containing PPR repeats have been shown to play
 a role in post-transcriptional  processes  within  organelles and they are
 thought to be sequence-specific RNA-binding proteins.
XX
CC   -!- SIMILARITY: Contains # PPR (pentatricopeptide) repeat.
FT   From: PS51375
FT   REPEAT    entry   exit       PPR #.
XX
Chop: Nter=0; Cter=0;
Size: 25-45;
Related: None;
Repeats: 1-30;
Topology: Undefined;
Example: Q76C99;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2008/04/29
//
AC   PRU00709;
DC   Domain;
TR   PROSITE; PS51377; KIND; 1; level=0
XX
Names: KIND domain
Function: The KIND (kinase non-catalytic C-lobe domain) is a putative protein
 interaction domain, which has been identified as being similar to the C-
 terminal protein kinase catalytic fold (C lobe).
XX
CC   -!- SIMILARITY: Contains # KIND domain.
XX
FT   From: PS51377
FT   DOMAIN     from     to       KIND #.
XX
Chop: Nter=0; Cter=0;
Size: 70-240;
Related: None;
Repeats: 1-2;
Topology: Cytoplasmic;
Example: Q76NI1;
Scope:
 Eukaryota; Metazoa
Comments: None;
XX
# Revision 1.1  2008/12/19
//
AC   PRU00710;
DC   Domain;
TR   PROSITE; PS51378; INVERT_DEFENSINS; 1; level=0
XX
Names: Invertebrate defensins family
 arthropod defensins family
 insect defensins family
Function: Invertebrate defensins are a family of cysteine-rich antimicrobial
 peptides, primarily active against Gram-positive bacteria.
XX
CC   -!- FUNCTION: Antibacterial peptide mostly active against Gram-
CC       positive bacteria (By similarity).
case <AnyFeature:Signal>
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
end case
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family.
XX
GO   GO:0006952; P:defense response
XX
KW   Antibiotic
KW   Antimicrobial
KW   Defensin
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51378
FT   DISULFID      4     25       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     11     31       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     15     33       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 25-50;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P91793;
Scope:
 Eukaryota; Fungi
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.3  2010/03/16
//
AC   PRU00711;
DC   Domain;
TR   PROSITE; PS51379; 4FE4S_FER_2; 1; level=0
XX
Names: 4Fe-4S ferredoxin-type domain
Function: binds 4Fe-4S
XX
CC   -!- SIMILARITY: Contains # 4Fe-4S ferredoxin-type domain.
XX
KW   4Fe-4S
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
XX
FT   From: PS51379
FT   DOMAIN     from     to       4Fe-4S ferredoxin-type #.
XX
Chop: Nter=0; Cter=0;
Size: 15-45;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P58324;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2008/05/15
//
AC   PRU00712;
DC   Domain;
TR   PROSITE; PS51380; EXS; 1; level=0
XX
Names: EXS domain
Function: The function of the EXS domain is unknown, although it could be
 involved in either phosphate transport or sensing or in sorting proteins to
 endomembrane.
XX
CC   -!- SIMILARITY: Contains # EXS domain.
XX
FT   From: PS51380
FT   DOMAIN     from     to       EXS #.
XX
Chop: Nter=0; Cter=0;
Size: 175-215;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8S403;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/09/10
//
AC   PRU00713;
DC   Domain;
TR   PROSITE; PS51381; B9; 1; level=0
XX
Names: B9 domain
Function: Although its function is unknown, a cilia-specific role has been
 suggested for the poorly characterized B9 domain.
XX
CC   -!- SIMILARITY: Contains # B9 domain.
XX
FT   From: PS51381
FT   DOMAIN     from     to       B9 #.
XX
Chop: Nter=0; Cter=0;
Size: 115-130;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9NXB0;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/09/10
//
AC   PRU00714;
DC   Domain;
TR   PROSITE; PS51382; SPX; 1; level=0
XX
Names: SPX domain
Function: The tripartite SPX domain could function as a sensor for inorganic
 phosphate (Pi) level and is most likely a domain for protein interaction.
 Possibly all SPX domains bind G-protein beta-subunits for the purpose of
 signal transduction.
XX
CC   -!- SIMILARITY: Contains # SPX domain.
XX
FT   From: PS51382
FT   DOMAIN     from     to       SPX #.
XX
Chop: Nter=0; Cter=0;
Size: 95-485;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8S403;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/09/10
//
AC   PRU00715;
DC   Domain;
TR   PROSITE; PS51383; YJEF_C_3; 1; level=0
XX
Names: YjeF C-terminal domain
Function: The YjeF C-terminal domain has an alpha/beta fold and shows high
 structural homology to the members of a ribokinase-like superfamily.
XX
CC   -!- SIMILARITY: Contains # YjeF C-terminal domain.
XX
DR   PROSITE; PS01049; YJEF_C_1; 1; trigger=no
DR   PROSITE; PS01050; YJEF_C_2; 1; trigger=no
XX
FT   From: PS51383
FT   DOMAIN     from     to       YjeF C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 250-330;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P94368;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2008/08/28
//
AC   PRU00716;
DC   Domain;
TR   PROSITE; PS51384; FAD_FR; 1; level=0
XX
Names: Ferredoxin reductase-type FAD-binding domain
Function: Binds flavin adenine dinucleotide (FAD)
XX
CC   -!- SIMILARITY: Contains # FAD-binding FR-type domain.
XX
FT   From: PS51384
FT   DOMAIN     from     to       FAD-binding FR-type #.
XX
Chop: Nter=0; Cter=0;
Size: 71-135;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P00387;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2008/08/14
//
AC   PRU00717;
DC   Domain;
TR   PROSITE; PS51386; RINT1_TIP20; 1; level=0
XX
Names: RINT1/TIP20 domain
Function: The RINT1/TIP20 domain might be a protein-protein interaction module
 necessary for the formation of functional complexes.
XX
CC   -!- SIMILARITY: Contains # RINT1/TIP20 domain.
XX
FT   From: PS51386
FT   DOMAIN     from     to       RINT1/TIP20 #.
XX
Chop: Nter=0; Cter=0;
Size: 550-585;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P33891;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/09/08
//
AC   PRU00718;
DC   Domain;
TR   PROSITE; PS51387; FAD_PCMH; 1; level=0
XX
Names: PCMH-type FAD-binding domain
Function: this domain binds the flavin adenine dinucleotide (FAD).
XX
CC   -!- SIMILARITY: Contains # FAD-binding PCMH-type domain.
XX
DR   PROSITE; PS51387; FAD_PCMH; 1; trigger=no
XX
FT   From: PS51387
FT   DOMAIN     from     to       FAD-binding PCMH-type #.
XX
Chop: Nter=0; Cter=0;
Size: 108-321;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O00116;
Scope:
 Eukaryota
 Bacteria
Comments: None;
XX
# Revision 1.1  2009/06/03
//
AC   PRU00719;
DC   Domain;
TR   PROSITE; PS51385; YJEF_N; 1; level=0
XX
Names: YjeF N-terminal domain
Function: The YjeF N-terminal domains represent a novel version of the
 Rossmann fold, one of the most common protein folds in nature observed in
 numerous enzyme families, that has acquired a set of catalytic residues and
 structural features that distinguish them from the conventional
 dehydrogenases.
XX
CC   -!- SIMILARITY: Contains # YjeF N-terminal domain.
XX
FT   From: PS51385
FT   DOMAIN     from     to       YjeF N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 195-245;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P31806;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2008/08/28
//
AC   PRU00720;
DC   Domain;
TR   PROSITE; PS51388; GED; 1; level=0
XX
Names: GED domain
Function: Dynamin superfamily members are large GTPases, conserved through
 evolution mainly described as mechanochemical enzymes involved in membrane
 scission events. All members display a common architecture: a large GTPase
 domain followed by a 'middle domain' of ill-defined function and a downstream
 coiled-coil GTPase effector domain (GED) that functions in higher order
 assembly and as a GTPase activating protein (GAP) for dynamin's GTPase
 activity.
XX
CC   -!- SIMILARITY: Contains # GED domain.
XX
FT   From: PS51388
FT   DOMAIN     from     to       GED #.
XX
Chop: Nter=0; Cter=0;
Size: 70-100;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q05193;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/07/31
//
AC   PRU00721;
DC   Domain;
TR   PROSITE; PS51389; XIN; 1; level=0
XX
Names: Xin repeat
Function: The Xin repeat is an actin-binding motif, capable of binding to
 actin filaments and organizing microfilaments into loose networks.
XX
CC   -!- DOMAIN: Xin repeats bind F-actin (By similarity).
CC   -!- SIMILARITY: Belongs to the Xin family.
CC   -!- SIMILARITY: Contains # Xin repeat.
XX
GO   GO:0003779; F:actin binding
XX
KW   Actin-binding
XX
FT   From: PS51389
FT   REPEAT     from     to       Xin #.
XX
Chop: Nter=0; Cter=0;
Size: 15-20;
Related: None;
Repeats: 17-28;
Topology: Undefined;
Example: Q5PZ43;
Scope:
 Eukaryota; Metazoa; Craniata
Comments: None
XX
# Revision 1.1  2008/07/31
//
AC   PRU00722;
DC   Domain;
TR   PROSITE; PS51390; WAP; 1; level=0
XX
Names: WAP
 four-disulfide core (4-DSC) domain
Function: The 'four-disulfide core' or WAP domain comprises 8 cysteine 
 residues involved in disulfide bonds. Single or multiple copies occur in 
 eukaryotic proteins, such as whey acidic protein (WAP), antileukoproteinase
 and elastase-inhibitor proteins.
XX
CC   -!- SIMILARITY: Contains # WAP domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51390
case <Feature:PS51390:8=C> and <Feature:PS51390:36=C> and <Feature:PS51390:18=C> and <Feature:PS51390:40=C> and <Feature:PS51390:23=C> and <Feature:PS51390:35=C> and <Feature:PS51390:29=C> and <Feature:PS51390:44=C>
FT   DOMAIN    entry   exit       WAP #.
else
FT   DOMAIN    entry   exit       WAP #; atypical.
end case
FT   DISULFID      8     36       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     18     40       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     23     35       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     29     44       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=5; Cter=3;
Size: 30-65;
Related: None;
Repeats: 1-7;
Topology: Undefined;
Example: Q6V9X0;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/09
//
AC   PRU00723;
DC   Domain;
TR   PROSITE; PS50103; ZF_C3H1; 1; level=0
XX
Names: Zinc finger C3H1-type
Function: In  various  proteins  the  C3H1-type  zinc finger has been shown to interact  with  the  3'-untranslated  region of  mRNAs
XX
CC   -!- SIMILARITY: Contains # C3H1-type zinc finger.
XX
KW   Zinc-finger
KW   Zinc
KW   Metal-binding
XX
FT   From: PS50103
FT   ZN_FING   entry   exit       C3H1-type #.
XX
Chop: Nter=0; Cter=0;
Size: 23-50;
Related: None;
Repeats: 1-10;
Topology: Undefined;
Example: Q96K80;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.1  2008/07/22
//
AC   PRU00724;
DC   Domain;
TR   PROSITE; PS51391; CID; 1; level=0
XX
Names: CID domain
Function: Several RNA-processing factors recognize the C-terminal domain (CTD)
 of the large subunit of RNA polymerase II by means of a conserved CTD-
 interacting domain (CID).
XX
CC   -!- SIMILARITY: Contains # CID domain.
XX
FT   From: PS51391
FT   DOMAIN     from     to       CID #.
XX
Chop: Nter=0; Cter=0;
Size: 125-165;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O94913;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/07/31
//
AC   PRU00725;
DC   Domain;
TR   PROSITE; PS51392; KEN; 1; level=0
XX
Names: KEN domain
Function: The dimerization of the kinase domain activates the ribonuclease
 function of the ~135-residue globular kinase-extension nuclease (KEN) domain
 made of eight helices.
XX
CC   -!- SIMILARITY: Contains # KEN domain.
XX
FT   From: PS51392
FT   DOMAIN     from     to       KEN #.
XX
Chop: Nter=0; Cter=0;
Size: 119-189;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P32361;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.2  2009/04/08
//
AC   PRU00726;
DC   Domain;
TR   PROSITE; PS51393; LIPOXYGENASE_3; 1; level=0
XX
Names: Lipoxygenase iron-binding catalytic domain
Function: Lipoxygenases (EC 1.13.11.-) form a class of iron-containing fatty 
 acid dioxygenases, which catalyze the hydroperoxidation of lipids, containing
 a cis,cis-1,4-pentadiene structure.
XX
case <OC:Viridiplantae>
DE   RecName: Full=lipoxygenase;
DE            EC=1.13.11.12;
XX
CC   -!- FUNCTION: Plant lipoxygenase may be involved in a number of
CC       diverse aspects of plant physiology including growth and
CC       development, pest resistance, and senescence or responses to
CC       wounding. It catalyzes the hydroperoxidation of lipids, containing
CC       a cis,cis-1,4-pentadiene structure (By similarity).
CC   -!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,11E)-(13S)-13-
CC       hydroperoxyoctadeca-9,11-dienoate.
end case
XX
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
XX
case <OC:Viridiplantae>
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
end case
XX
case <OC:Metazoa>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
end case
case <OC:Bacteria>
CC   -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
end case
XX
CC   -!- SIMILARITY: Contains # lipoxygenase domain.
XX
case <Feature:PS51393:340=H> and <Feature:PS51393:345=H>
DR   PROSITE; PS00711; LIPOXYGENASE_1; 1; trigger=no
end case
case <Feature:PS51393:530=H>
DR   PROSITE; PS00081; LIPOXYGENASE_2; 1; trigger=no
end case
XX
GO   GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO   GO:0005506; F:iron ion binding
GO   GO:0046872; F:metal ion binding
GO   GO:0016491; F:oxidoreductase activity
case <OC:Mammalia>
GO   GO:0019370; P:leukotriene biosynthetic process
end case
case <OC:Viridiplantae>
GO   GO:0006633; P:fatty acid biosynthetic process
GO   GO:0008610; P:lipid biosynthetic process
GO   GO:0031408; P:oxylipin biosynthetic process
end case
case <OC:Bacteria>
GO   GO:0042597; C:periplasmic space
end case
XX
KW   Dioxygenase
KW   Iron
KW   Metal-binding
KW   Oxidoreductase
case <OC:Mammalia>
KW   Leukotriene biosynthesis
end case
case <OC:Viridiplantae>
KW   Fatty acid biosynthesis
KW   Lipid synthesis
KW   Oxylipin biosynthesis
end case
case <OC:Bacteria>
KW   Periplasm
end case
XX
FT   From: PS51393
FT   DOMAIN     from     to       Lipoxygenase #.
FT   METAL       340    340       Iron; catalytic (By similarity).
FT   Condition: H
FT   METAL       345    345       Iron; catalytic (By similarity).
FT   Condition: H
FT   METAL       530    530       Iron; catalytic (By similarity).
FT   Condition: H
FT   METAL       534    534       Iron; catalytic (By similarity).
FT   Condition: [NH]
FT   METAL       678    678       Iron; via carboxylate; catalytic (By
FT                                similarity).
FT   Condition: I
XX
Chop: Nter=1; Cter=0;
Size: 540-730;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q84YK8; Q9BYJ1; Q8RNT4;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2008/07/11
//
AC   PRU00727;
DC   Domain;
TR   PROSITE; PS51394; PFU; 1; level=0
XX
Names: PFU domain
Function: In addition to ubiquitin, the PFU domain of DOA1 has been shown to
 bind to the SH3 domain.
XX
CC   -!- SIMILARITY: Contains # PFU domain.
XX
FT   From: PS51394
FT   DOMAIN     from     to       PFU #.
XX
Chop: Nter=0; Cter=0;
Size: 95-105;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y263;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/01/23
//
AC   PRU00729;
DC   Domain;
TR   PROSITE; PS51396; PUL; 1; level=0
XX
Names: PUL domain
Function: The PUL domain is a protein-protein interaction domain.
XX
CC   -!- SIMILARITY: Contains # PUL domain.
XX
FT   From: PS51396
FT   DOMAIN     from     to       PUL #.
XX
Chop: Nter=0; Cter=0;
Size: 250-265;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y263;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/01/23
//
AC   PRU00730;
DC   Domain;
TR   PROSITE; PS51397; WLM; 1; level=0
XX
Names: WLM domain
Function: The WLM (WSS1-like metalloprotease) domain is a globular domain
 related to the zincin-like superfamily of Zn-dependent peptidase. Since the
 WLM domain contains all known active site residues of zincins, it is
 predicted to be a catalytically active peptidase domain.
XX
CC   -!- SIMILARITY: Contains # WLM domain.
XX
DR   PROSITE; PS00142; ZINC_PROTEASE; 0-1; trigger=no
XX
FT   From: PS51397
FT   DOMAIN     from     to       WLM #.
XX
Chop: Nter=0; Cter=0;
Size: 165-215;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P38838;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.2  2009/01/23
//
AC   PRU00731;
DC   Domain;
TR   PROSITE; PS51398; PAW; 1; level=0
XX
Names: PAW domain
Function: The C-terminal PAW domain of PNGase binds to the mannose moieties
 of N-linked oligosaccharide chains.
XX
CC   -!- SIMILARITY: Belongs to the transglutaminase-like superfamily.
CC       PNGase family.
CC   -!- SIMILARITY: Contains # PAW domain.
XX
FT   From: PS51398
FT   DOMAIN     from     to       PAW #.
XX
Chop: Nter=0; Cter=0;
Size: 185-210;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q96IV0;
Scope:
 Eukaryota; Metazoa
Comments: None;
XX
# Revision 1.1  2009/01/23
//
AC   PRU00732;
DC   Domain;
TR   PROSITE; PS51399; SEP; 1; level=0
XX
Names: SEP domain
Function: The function of the SEP domain is as yet unknown but it has been
 proposed to act as a reversible competitive inhibitor of the lysosomal
 cysteine protease cathepsin L.
XX
CC   -!- SIMILARITY: Contains # SEP domain.
XX
FT   From: PS51399
FT   DOMAIN     from     to       SEP #.
XX
Chop: Nter=0; Cter=0;
Size: 60-70;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q9UNZ2;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2008/12/22
//
AC   PRU00734;
DC   Domain;
TR   PROSITE; PS51401; CHORD; 1; level=0
XX
Names: CHORD domain
Function: Cysteine- and histidine-rich domains (CHORDs) are 60-amino acid
 modules that bind two zinc ions.
XX
CC   -!- SIMILARITY: Contains # CHORD domain.
XX
case <FTGroup:1> or <FTGroup:2>
KW   Zinc
KW   Metal-binding
end case
XX
FT   From: PS51401
FT   DOMAIN     from     to       CHORD #.
FT   METAL         1      1       Zinc #1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL         6      6       Zinc #1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        20     20       Zinc #1 (By similarity).
FT   Group: 1; Condition: C
FT   METAL        23     23       Zinc #2 (By similarity).
FT   Group: 2; Condition: H
FT   METAL        38     38       Zinc #2 (By similarity).
FT   Group: 2; Condition: C
FT   METAL        39     39       Zinc #2 (By similarity).
FT   Group: 2; Condition: C
FT   METAL        55     55       Zinc #2 (By similarity).
FT   Group: 2; Condition: C
FT   METAL        60     60       Zinc #1 (By similarity).
FT   Group: 1; Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 55-65;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: Q9UHD1;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2008/12/19
//
AC   PRU00736;
DC   Domain;
TR   PROSITE; PS51403; NC1_IV; 1; level=0
XX
Names: Collagen IV carboxyl-terminal non-collagenous (NC1) domain
Function: Each type IV chain contains a long triple-helical collagenous domain
 flanked by a short 7S domain of 25 residues and a globular non-collagenous
 NC1 domain of ~230 residues at the N- and C-terminus, respectively.
XX
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane (By similarity).
CC   -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous
CC       domain (NC1) at their C-terminus, frequent interruptions of the G-
CC       X-Y repeats in the long central triple-helical domain (which may
CC       cause flexibility in the triple helix), and a short N-terminal
CC       triple-helical 7S domain (By similarity).
CC   -!- PTM: Prolines at the third position of the tripeptide repeating
CC       unit (G-X-Y) are hydroxylated in some or all of the chains (By
CC       similarity).
CC   -!- PTM: Prolines at the third position of the tripeptide repeating
CC       unit (G-X-Y) are hydroxylated in some or all of the chains (By
CC       similarity).
CC   -!- PTM: Type IV collagens contain numerous cysteine residues which
CC       are involved in inter- and intramolecular disulfide bonding. 12 of
CC       these, located in the NC1 domain, are conserved in all known type
CC       IV collagens (By similarity).
CC   -!- SIMILARITY: Belongs to the type IV collagen family.
CC   -!- SIMILARITY: Contains # collagen IV NC1 (C-terminal non-
CC       collagenous) domain.
XX
GO   GO:0005604; C:basement membrane
GO   GO:0005578; C:proteinaceous extracellular matrix
XX
KW   Basement membrane
KW   Collagen
KW   Extracellular matrix
KW   Secreted
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51403
FT   DOMAIN     from     to       Collagen IV NC1 #.
FT   DISULFID     16    106       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     49    103       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     61     67       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 220-230;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P02462;
Scope:
 Eukaryota; Metazoa
Comments: None;
XX
# Revision 1.2  2009/02/09
//
AC   PRU00739;
DC   Domain;
TR   PROSITE; PS51406; FIBRINOGEN_C_2; 1; level=0
XX
Names: Fibrinogen C-terminal domain
Function: The C-terminal domain of the alpha, beta and gamma chains of 
 fibrinogen can function as a molecular recognition unit that interacts 
 with either proteins or carbohydrates.
XX
CC   -!- SIMILARITY: Contains # fibrinogen C-terminal domain.
XX
case <Feature:PS51406:175=C>
DR   PROSITE; PS00514; FIBRINOGEN_C_1; 1; trigger=no
end case
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51406
FT   DOMAIN     from     to       Fibrinogen C-terminal #.
FT   DISULFID     10     39       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    162    175       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=2; Cter=24;
Size: 50-265;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O43827;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.2  2009/02/09
//
AC   PRU00740;
DC   Domain;
TR   PROSITE; PS51407; LAMP_3; 1; level=0
XX
Names: Lysosome-associated membrane glycoprotein (lamp) family
 LAMP family
Function: Lysosome-associated membrane glycoproteins (lamp) are integral
 membrane proteins, specific to lysosomes.
XX
case <OC:Chordata>
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I
CC       membrane protein (By similarity).
else
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
end case
CC   -!- SIMILARITY: Belongs to the LAMP family.
XX
DR   General; Transmembrane; -; 1; trigger=no
XX
case <Feature:PS51407:11=C>
DR   PROSITE; PS00310; LAMP_1; 1; trigger=no
end case
case <Feature:PS51407:345=C>
DR   PROSITE; PS00311; LAMP_2; 1; trigger=no
end case
XX
case <OC:Chordata>
GO   GO:0005764; C:lysosome
GO   GO:0005765; C:lysosomal membrane
end case
GO   GO:0016020; C:membrane
GO   GO:0016021; C:integral to membrane
XX
case <OC:Chordata>
KW   Lysosome
end case
KW   Membrane
KW   Transmembrane
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51407
case <Feature:PS51407:374=K>
FT   TRANSMEM    352    373       Helical; (Potential).
FT   TOPO_DOM    374    387       Cytoplasmic (Potential).
else
FT   TRANSMEM    352    376       Helical; (Potential).
FT   TOPO_DOM    377    387       Cytoplasmic (Potential).
end case
FT   DISULFID     11     50       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    124    160       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    202    240       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    308    345       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 230-410;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P13473; Q7TST5; Q11117;
Scope:
 Eukaryota; Metazoa
Comments: None
XX
# Revision 1.4  2010/05/10
//
AC   PRU00741;
DC   Domain;
TR   PROSITE; PS51408; TRANSFERRIN_LIKE_4; 1; level=0
XX
Names: Transferrin-like domain
Function: The transferrin family is a group of glycosylated proteins found in
 both vertebrates and invertebrates. Most family members contain two
 transferrin-like domains of around 340 amino acids, the result of an ancient
 duplication event.
XX
case <FTGroup:1>
DE   + AltName: EC 3.4.21.-;
end case
CC   -!- SIMILARITY: Belongs to the transferrin family.
CC   -!- SIMILARITY: Contains # transferrin-like domain.
case <FTGroup:1>
DR   PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1; trigger=no
DR   PROSITE; PS00206; TRANSFERRIN_LIKE_2; 1; trigger=no
DR   PROSITE; PS00207; TRANSFERRIN_LIKE_3; 1; trigger=no
end case
XX
case <FTGroup:1>
GO   GO:0016787; F:hydrolase activity
GO   GO:0008233; F:peptidase activity
GO   GO:0004252; F:serine-type endopeptidase activity
end case
case <FTGroup:2>
GO   GO:0005506; F:iron ion binding
GO   GO:0046872; F:metal ion binding
end case
XX
case <FTGroup:1>
KW   Hydrolase
KW   Protease
KW   Serine protease
end case
case <FTGroup:2>
KW   Iron
KW   Metal-binding
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51408
FT   DOMAIN     from     to       Transferrin-like #.
FT   ACT_SITE     68     68       Probable.
FT   Group: 1; Condition: K
FT   ACT_SITE    256    256       Nucleophile (Probable).
FT   Group: 1; Condition: S
FT   METAL        56     56       Iron #1 (By similarity).
FT   Group: 2; Condition: D
FT   METAL        85     85       Iron #1 (By similarity).
FT   Group: 2; Condition: Y
FT   METAL       184    184       Iron #1 (By similarity).
FT   Group: 2; Condition: Y
FT   METAL       249    249       Iron #1 (By similarity).
FT   Group: 2; Condition: H
FT   BINDING     111    111       Carbonate #1 (By similarity).
FT   Group: 2; Condition: T
FT   BINDING     115    115       Carbonate #1 (By similarity).
FT   Group: 2; Condition: R
FT   BINDING     117    117       Carbonate #1; via amide nitrogen (By
FT                                similarity).
FT   Group: 2; Condition: A
FT   BINDING     118    118       Carbonate #1; via amide nitrogen (By
FT                                similarity).
FT   Group: 2; Condition: G
FT   DISULFID      4     41       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     14     32       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    109    190       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    151    169       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    154    175       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    166    173       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    227    241       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 245-610;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: P02788;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.4  2009/02/26
//
AC   PRU00742;
DC   Domain;
TR   PROSITE; PS51409; ARGINASE_2; 1; level=0
XX
Names: Arginase family
 ureohydrolase superfamily
Function: Arginase family proteins are ureohydrolases with important roles in
 arginine/agmatine metabolism, the urea cycle, histidine degradation, and 
 other pathways. The family includes arginase and related enzymes of ~300 
 amino acids that typically contain two manganese ions in the active site.
XX
case <Feature:PS51409:96=[HN]> and <Feature:PS51409:120=D> and <Feature:PS51409:122=H> and <Feature:PS51409:124=D> and <Feature:PS51409:213=[DC]> and <Feature:PS51409:215=D>
DE   + RecName: EC=3.5.3.-;
end case
XX
case <Feature:PS51409:96=[HN]> and <Feature:PS51409:120=D> and <Feature:PS51409:122=H> and <Feature:PS51409:124=D> and <Feature:PS51409:213=[DC]> and <Feature:PS51409:215=D>
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
else case <Feature:PS51409:96=[HN]> or <Feature:PS51409:120=D> or <Feature:PS51409:122=H> or <Feature:PS51409:124=D> or <Feature:PS51409:213=[DC]> or <Feature:PS51409:215=D>
CC   -!- COFACTOR: Manganese (By similarity).
end case
CC   -!- SIMILARITY: Belongs to the arginase family.
XX
case <Feature:PS51409:213=[DC]> and <Feature:PS51409:215=D>
DR   PROSITE; PS01053; ARGINASE_1; 1; trigger=no
end case
XX
case <Feature:PS51409:96=[HN]> or <Feature:PS51409:120=D> or <Feature:PS51409:122=H> or <Feature:PS51409:124=D> or <Feature:PS51409:213=[DC]> or <Feature:PS51409:215=D>
GO   GO:0016787; F:hydrolase activity
GO   GO:0030145; F:manganese ion binding
GO   GO:0046872; F:metal ion binding
XX
KW   Hydrolase
KW   Manganese
KW   Metal-binding
end case
XX
FT   From: PS51409
FT   METAL        96     96       Manganese #1 (By similarity).
FT   Condition: [HN]
FT   METAL       120    120       Manganese #1 (By similarity).
FT   Condition: D
FT   METAL       120    120       Manganese #2 (By similarity).
FT   Condition: D
FT   METAL       122    122       Manganese #2 (By similarity).
FT   Condition: H
FT   METAL       124    124       Manganese #1 (By similarity).
FT   Condition: D
FT   METAL       213    213       Manganese #1 (By similarity).
FT   Condition: [DC]
FT   METAL       213    213       Manganese #2 (By similarity).
FT   Condition: [DC]
FT   METAL       215    215       Manganese #2 (By similarity).
FT   Condition: D
XX
Chop: Nter=0; Cter=0;
Size: 260-350;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9HQD7; P46637;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU00744;
DC   Domain;
TR   PROSITE; PS51411; PSP1_C; 1; level=0
XX
Names: PSP1 C-terminal domain
Function: The actual biological significance of the PSP1 C-terminal domain has
 not yet been clearly established.
XX
CC   -!- SIMILARITY: Contains # PSP1 C-terminal domain.
XX
FT   From: PS51411
FT   DOMAIN     from     to       PSP1 C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 85-115;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P50896;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2008/11/24
//
AC   PRU00745;
DC   Domain;
TR   PROSITE; PS51412; MACPF_2; 1; level=0
XX
Names: Membrane attack complex/perforin (MACPF) domain
Function: The MACPF domain oligomerizes, undergoes conformational change, and
 is required for lytic activity.
XX
CC   -!- SIMILARITY: Contains # MACPF domain.
XX
DR   PROSITE; PS00279; MACPF_1; 1; trigger=no
XX
FT   From: PS51412
FT   DOMAIN     from     to       MACPF #.
XX
Chop: Nter=0; Cter=0;
Size: 315-385;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q29RU4;
Scope:
 Eukaryota
 Bacteria
Comments: None;
XX
# Revision 1.1  2008/11/28
//
AC   PRU00746;
DC   Domain;
TR   PROSITE; PS51413; DBINO; 1; level=0
XX
Names: DBINO domain
Function: The DBINO (DNA binding domain of INO80) domain is characteristic of
 the INO80 subfamily and is predicted to have DNA-binding function.
XX
CC   -!- FUNCTION: DNA helicase component of the INO80 complex which
CC       remodels chromatin by shifting nucleosomes and is involved in DNA
CC       repair (By similarity).
CC   -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # DBINO domain.
XX
GO   GO:0016568; P:chromatin modification
GO   GO:0006974; P:response to DNA damage stimulus
GO   GO:0006281; P:DNA repair
GO   GO:0003677; F:DNA binding
GO   GO:0005634; C:nucleus
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   Activator
KW   Chromatin regulator
KW   DNA damage
KW   DNA repair
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51413
FT   DOMAIN     from     to       DBINO #.
XX
Chop: Nter=0; Cter=0;
Size: 125-135;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: O14148;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2008/12/12
//
AC   PRU00747;
DC   Domain;
TR   PROSITE; PS51414; HSR; 1; level=0
XX
Names: HSR domain
Function: The HSR domain is a nuclear dot (DT) targeting and dimerization
 domain of ~100 amino acids.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # HSR domain.
XX
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
XX
FT   From: PS51414
FT   DOMAIN     from     to       HSR #.
XX
Chop: Nter=0; Cter=0;
Size: 100-120;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: P23497;
Scope:
 Eukaryota; Vertebrata
Comments: None;
XX
# Revision 1.1  2009/03/03
//
AC   PRU00748;
DC   Domain;
TR   PROSITE; PS51415; XYLOSE_ISOMERASE; 1; level=0
XX
Names: Xylose isomerase family
Function: Xylose isomerase (EC 5.3.1.5) is an enzyme found in microorganisms
 and plants which catalyzes the interconversion of the aldo sugars D-xylose
 or D-glucose to the keto sugars D-xylulose and D-fructose. The catalytic
 activity requires magnesium, cobalt or manganese.
XX
case <Feature:PS51415:66=H>
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
end case
XX
case <Feature:PS51415:66=H>
CC   -!- CATALYTIC ACTIVITY: D-xylose = D-xylulose.
end case
case not <OC:Viridiplantae>
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
else case <OC:Viridiplantae>
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
end case
CC   -!- SUBUNIT: Homotetramer (By similarity).
case <OC:Bacteria>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
end case
CC   -!- SIMILARITY: Belongs to the xylose isomerase family.
XX
GO   GO:0009045; F:xylose isomerase activity
GO   GO:0042732; P:D-xylose metabolic process
GO   GO:0005975; P:carbohydrate metabolic process
GO   GO:0016853; F:isomerase activity
GO   GO:0000287; F:magnesium ion binding
GO   GO:0046872; F:metal ion binding
GO   GO:0006098; P:pentose-phosphate shunt
case <OC:Viridiplantae>
GO   GO:0030145; F:manganese ion binding
end case
case <OC:Bacteria>
GO   GO:0005737; C:cytoplasm
end case
XX
KW   Carbohydrate metabolism
KW   Isomerase
KW   Magnesium
KW   Metal-binding
KW   Pentose shunt
KW   Xylose metabolism
case <OC:Viridiplantae>
KW   Manganese
end case
case <OC:Bacteria>
KW   Cytoplasm
end case
XX
FT   From: PS51415
FT   ACT_SITE     66     66       By similarity.
FT   Condition: H
case not <OC:Viridiplantae>
FT   METAL       197    197       Magnesium 1 (By similarity).
FT   Condition: E
FT   METAL       233    233       Magnesium 1 (By similarity).
FT   Condition: E
FT   METAL       233    233       Magnesium 2 (By similarity).
FT   Condition: E
FT   METAL       236    236       Magnesium 2 (By similarity).
FT   Condition: H
FT   METAL       261    261       Magnesium 1 (By similarity).
FT   Condition: D
FT   METAL       272    272       Magnesium 2 (By similarity).
FT   Condition: D
FT   METAL       274    274       Magnesium 2 (By similarity).
FT   Condition: D
FT   METAL       304    304       Magnesium 1 (By similarity).
FT   Condition: D
else case <OC:Viridiplantae>
FT   METAL       197    197       Manganese 1 (By similarity).
FT   Condition: E
FT   METAL       233    233       Manganese 1 (By similarity).
FT   Condition: E
FT   METAL       233    233       Manganese 2 (By similarity).
FT   Condition: E
FT   METAL       236    236       Manganese 2 (By similarity).
FT   Condition: H
FT   METAL       261    261       Manganese 1 (By similarity).
FT   Condition: D
FT   METAL       272    272       Manganese 2 (By similarity).
FT   Condition: D
FT   METAL       274    274       Manganese 2 (By similarity).
FT   Condition: D
FT   METAL       304    304       Manganese 1 (By similarity).
FT   Condition: D
end case
XX
Chop: Nter=0; Cter=0;
Size: 370-420;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q93RJ9; Q9FKK7;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2009/03/03
//
AC   PRU00749;
DC   Domain;
TR   PROSITE; PS51416; MIB_HERC2; 1; level=0
XX
Names: MIB/HERC2 domain
Function: The MIB/HERC2 domain is a conserved region of ~80 amino acids, which
 has been identified in animal Mind bomb 1 and 2 (MIB1 and MIB2) and HERC2 E3
 ubiquitin ligases.
XX
CC   -!- SIMILARITY: Contains # MIB/HERC2 domain.
XX
GO   GO:0006511; P:ubiquitin-dependent protein catabolic process
XX
KW   Ubl conjugation pathway
XX
FT   From: PS51416
FT   DOMAIN     from     to       MIB/HERC2 #.
XX
Chop: Nter=0; Cter=0;
Size: 65-85;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: O95714;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/03/03
//
AC   PRU00750;
DC   Domain;
TR   PROSITE; PS51425; SCD; 1; level=0
XX
Names: Stromalin conservative (SCD) domain
Function: Stromalins are represented in several organisms from yeast to humans
 and are characterized by the stromalin conservative domain (SCD), an 86 amino
 acid motif found in all proteins of the family described to date.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # SCD (stromalin conservative) domain.
XX
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
XX
FT   From: PS51425
FT   DOMAIN     from     to       SCD #.
XX
Chop: Nter=0; Cter=0;
Size: 85-95;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q8WVM7;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/03/03
//
AC   PRU00751;
DC   Domain;
TR   PROSITE; PS51426; ABL; 1; level=0
XX
Names: ABL domain
Function: The ABL (Alpha/Beta/Loop) domain is found between the histidine
 kinase domain and the response regulatory domain of all RcsC sequences of all
 enterobacteria sequenced so far.
XX
CC   -!- SIMILARITY: Contains # ABL domain.
XX
FT   From: PS51426
FT   DOMAIN     from     to       ABL #.
XX
Chop: Nter=0; Cter=0;
Size: 100-105;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P14376;
Scope:
 Bacteria; Enterobacteriaceae
Comments: None;
XX
# Revision 1.1  2009/03/03
//
AC   PRU00758;
DC   Domain;
TR   PROSITE; PS51424; ROC; 1; level=0
XX
Names: small GTPase superfamily. Miro family
Function: Small  GTPase  domain  found  in mitochondrial proteins involved in mitochondrial trafficking.
XX
DE   + Includes:
DE     RecName: EC=3.6.5.2;
XX
CC   -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
CC   -!- SIMILARITY: Contains # Roc domain.
XX
GO   GO:0005525; F:GTP binding
GO   GO:0003924; F:GTPase activity
GO   GO:0007264; P:small GTPase mediated signal transduction
GO   GO:0007165; P:signal transduction
XX
KW   GTP-binding
KW   Hydrolase
KW   Nucleotide-binding
XX
FT   From: PS51424
FT   DOMAIN     from     to       Roc #.
FT   NP_BIND      14     21       GTP.
FT   NP_BIND      65     69       GTP.
FT   NP_BIND     124    127       GTP.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8MVR1;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/04/23
//
AC   PRU00760;
DC   Domain;
TR   PROSITE; PS51430; KAIA_N; 1; level=0
XX
Names: KaiA N-terminal domain
Function: Although the fold of the kaiA N-terminal domain is that of a
 canonical receiver domain, the primary sequence is dissimilar, and it lacks
 the conserved aspartate residue necessary for phosphorylation. KaiA
 activation most likely involves direct protein-protein interactions of the N-
 terminal domain that result in functional modulation of the C-terminal
 effector domain.
XX
CC   -!- SIMILARITY: Contains # kaiA N-terminal domain.
XX
FT   From: PS51430
FT   DOMAIN     from     to       KaiA N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 150-175;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6L8L7;
Scope:
 Bacteria; Cyanobacteria
Comments: None;
XX
# Revision 1.1  2009/03/11
//
AC   PRU00761;
DC   Domain;
TR   PROSITE; PS51431; KAIA_C; 1; level=0
XX
Names: KaiA C-terminal domain
Function: KaiA activation most likely involves direct protein-protein
 interactions of the N- terminal domain that result in functional modulation
 of the C-terminal effector domain.
XX
CC   -!- FUNCTION: Component of the kaiABC clock protein complex, which
CC       constitutes the main circadian regulator in cyanobacteria. The
CC       kaiABC complex may act as a promoter-nonspecific transcription
CC       regulator that represses transcription, possibly by acting on the
CC       state of chromosome compaction. In the complex, it enhances the
CC       phosphorylation status of kaiC. In contrast, the presence of kaiB
CC       in the complex decreases the phosphorylation status of kaiC,
CC       suggesting that kaiB acts by antagonizing the interaction between
CC       kaiA and kaiC. A kaiA dimer is sufficient to enhance kaiC hexamer
CC       phosphorylation (By similarity).
CC   -!- SUBUNIT: Homodimer. Component of the kaiABC complex, at least
CC       composed of a kaiC homohexamer, a kaiB dimer and two kaiA dimers.
CC       The kaiABC complex also interacts with sasA (By similarity).
CC   -!- DOMAIN: The kaiA domain mediates the interaction with kaiC, the
CC       homodimerization, and is responsible for the clock oscillation
CC       function (By similarity).
CC   -!- SIMILARITY: Contains # kaiA C-terminal domain.
XX
GO   GO:0007623; P:circadian rhythm
XX
KW   Biological rhythms
XX
FT   From: PS51431
FT   DOMAIN     from     to       KaiA C-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 100-110;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6L8L7;
Scope:
 Bacteria; Cyanobacteria
Comments: None;
XX
# Revision 1.1  2009/03/13
//
AC   PRU00762;
DC   Domain;
TR   PROSITE; PS51433; PNT; 1; level=0
XX
Names: Pointed (PNT) domain
Function: A role in protein-protein association has been established for the
 PNT domain.
XX
CC   -!- SIMILARITY: Contains # PNT (pointed) domain.
XX
FT   From: PS51433
FT   DOMAIN     from     to       PNT #.
XX
Chop: Nter=0; Cter=0;
Size: 80-90;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P51023;
Scope:
 Eukaryota; Metazoa
 Viruses
Comments: None;
XX
# Revision 1.1  2009/03/02
//
AC   PRU00763;
DC   Domain;
TR   PROSITE; PS51432; AP_NUCLEASE_F2_4; 1; level=0
XX
Names: AP endonucleases family 2
Function: Endonuclease 4 related enzymes play a role in DNA repair. These 
 nucleases cleave phosphodiester bonds at apurinic or apyrimidinic sites (AP
 sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate
 residues.
XX
case <OC:Bacteria> or <OC:Archaea> or <OC:Amoebozoa>
DE   + RecName: Full=Probable endonuclease 4;
DE            EC=3.1.21.2;
DE   AltName: Full=Endonuclease IV;
DE   AltName: Full=Endodeoxyribonuclease IV;
else case <OC:Fungi> or <OC:Nematoda>
DE   + RecName: Full=DNA-(apurinic or apyrimidinic site) lyase 1;
DE            EC=4.2.99.18;
DE   AltName: Full=Apurinic-apyrimidinic endonuclease 1;
DE            Short=AP endonuclease 1;
else case <OC:Viruses>
DE   + RecName: Full=Putative endonuclease 4;
DE            EC=3.1.21.2;
DE   AltName: Full=Endonuclease IV;
end case
XX
case <OC:Bacteria> or <OC:Archaea>
CC   -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
CC       phosphodiester bonds at apurinic or apyrimidinic sites (AP sites)
CC       to produce new 5'-ends that are base-free deoxyribose 5-phosphate
CC       residues. It preferentially attacks modified AP sites created by
CC       bleomycin and neocarzinostatin (By similarity).
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphooligonucleotide end-products.
else case <OC:Fungi> or <OC:Nematoda>
CC   -!- FUNCTION: DNA repair enzyme that cleaves apurinic/apyrimidinic
CC       (AP) sites and removes 3'-blocking groups present at single strand
CC       breaks of damaged DNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate.
else case <OC:Amoebozoa> or <OC:Viruses>
CC   -!- FUNCTION: Plays a role in DNA repair. It cleaves phosphodiester
CC       bonds at apurinic or apyrimidinic sites (AP sites) to produce new
CC       5'-ends that are base-free deoxyribose 5-phosphate residues (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphooligonucleotide end-products.
end case
case <OC:Eukaryota>
CC   -!- SUBCELLULAR LOCATION: Nucleus.
end case
CC   -!- COFACTOR: Binds 3 zinc ions (By similarity).
CC   -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
XX
case <Feature:PS51432:67=H>
DR   PROSITE; PS00729; AP_NUCLEASE_F2_1; 1; trigger=no
end case
case <Feature:PS51432:177=D> and <Feature:PS51432:180=H>
DR   PROSITE; PS00730; AP_NUCLEASE_F2_2; 1; trigger=no
end case
case <Feature:PS51432:214=H> and <Feature:PS51432:227=D> and <Feature:PS51432:229=H>
DR   PROSITE; PS00731; AP_NUCLEASE_F2_3; 1; trigger=no
end case
XX
GO   GO:0006974; P:response to DNA damage stimulus
GO   GO:0006281; P:DNA repair
GO   GO:0046872; F:metal ion binding
GO   GO:0008270; F:zinc ion binding
GO   GO:0003677; F:DNA binding
case <OC:Bacteria> or <OC:Archaea> or <OC:Amoebozoa> or <OC:Viruses>
GO   GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity
GO   GO:0004519; F:endonuclease activity
GO   GO:0004518; F:nuclease activity
GO   GO:0016787; F:hydrolase activity
else case <OC:Fungi> or <OC:Nematoda>
GO   GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity
GO   GO:0016829; F:lyase activity
end case
case <OC:Eukaryota>
GO   GO:0005634; C:nucleus
else case <OC:Bacteria>  or <OC:Archaea>
GO   GO:0005737; C:cytoplasm
end case
XX
KW   DNA damage
KW   DNA repair
KW   Metal-binding
KW   Zinc
case <OC:Bacteria> or <OC:Archaea> or <OC:Amoebozoa> or <OC:Viruses>
KW   Endonuclease
KW   Hydrolase
KW   Nuclease
else case <OC:Fungi> or <OC:Nematoda>
KW   Lyase
end case
case <OC:Eukaryota>
KW   Nucleus
end case
XX
FT   From: PS51432
FT   METAL        67     67       Zinc 1 (By similarity).
FT   Condition: H
FT   METAL       107    107       Zinc 1 (By similarity).
FT   Condition: H
FT   METAL       143    143       Zinc 1 (By similarity).
FT   Condition: E
FT   METAL       143    143       Zinc 2 (By similarity).
FT   Condition: E
FT   METAL       177    177       Zinc 2 (By similarity).
FT   Condition: D
FT   METAL       180    180       Zinc 3 (By similarity).
FT   Condition: H
FT   METAL       214    214       Zinc 2 (By similarity).
FT   Condition: H
FT   METAL       227    227       Zinc 3 (By similarity).
FT   Condition: D
FT   METAL       229    229       Zinc 3 (By similarity).
FT   Condition: H
FT   METAL       259    259       Zinc 2 (By similarity).
FT   Condition: E
XX
Chop: Nter=0; Cter=0;
Size: 240-305;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: A4IR02; Q966U0; Q5UPY4; Q10002;
Scope:
 Bacteria
 Archaea
 Eukaryota
 Viruses
Comments: None;
XX
# Revision 1.1  2009/03/02
//
AC   PRU00764;
DC   Domain;
TR   PROSITE; PS51435; AP_NUCLEASE_F1_4; 1; level=0
XX
Names: AP endonucleases family 1
Function: Exonuclease III and AP endonuclease 1 related enzymes play a role
 in DNA repair. These nucleases cleave phosphodiester bonds at apurinic or
 apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free
 deoxyribose 5-phosphate residues.
XX
case <OC:Eukaryota>
DE   + RecName: Full=DNA-(apurinic or apyrimidinic site) lyase;
DE            EC=4.2.99.18;
else case <OC:Bacteria>
DE   + RecName: Full=Exodeoxyribonuclease III;
DE            Short=Exonuclease III;
DE            Short=EXO III;
DE            EC=3.1.11.2;
end case
XX
case <OC:Eukaryota>
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
else case <OC:Bacteria>
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'-to 5'-
CC       direction to yield nucleoside 5'-phosphates.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- SIMILARITY: Belongs to the DNA repair enzymes AP/exoA family.
XX
case <Feature:PS51435:40=E>
DR   PROSITE; PS00726; AP_NUCLEASE_F1_1; 1; trigger=no
end case
DR   PROSITE; PS00727; AP_NUCLEASE_F1_2; 1; trigger=no
DR   PROSITE; PS00728; AP_NUCLEASE_F1_3; 1; trigger=no
XX
GO   GO:0003677; F:DNA binding
GO   GO:0004519; F:endonuclease activity
GO   GO:0006281; P:DNA repair
case <OC:Eukaryota>
GO   GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity
GO   GO:0005634; C:nucleus
else case <OC:Bacteria>
GO   GO:0000287; F:magnesium ion binding
GO   GO:0008853; F:exodeoxyribonuclease III activity
GO   GO:0005737; C:cytoplasm
end case
XX
KW   DNA damage
KW   DNA repair
KW   Metal-binding
case <OC:Eukaryota>
KW   Lyase
KW   Nucleus
else case <OC:Bacteria>
KW   Cytoplasm
KW   Exonuclease
KW   Hydrolase
KW   Magnesium
KW   Nuclease
end case
XX
FT   From: PS51435
FT   ACT_SITE    258    258       Proton acceptor (By similarity).
FT   Condition: H
FT   METAL         7      7       Magnesium or manganese (By similarity).
FT   Condition: N
FT   METAL        40     40       Magnesium or manganese (By similarity).
FT   Condition: E
FT   METAL       158    158       Magnesium or manganese (By similarity).
FT   Condition: D
FT   METAL       160    160       Magnesium or manganese (By similarity).
FT   Condition: N
FT   METAL       257    257       Magnesium or manganese (By similarity).
FT   Condition: D
FT   METAL       258    258       Magnesium or manganese (By similarity).
FT   Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 230-370;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P28352; P44318;
Scope:
 Eukaryota
 Bacteria
Comments: None;
XX
# Revision 1.1  2009/03/02
//
AC   PRU00765;
DC   Domain;
TR   PROSITE; PS51434; NUP_C; 1; level=0
XX
Names: Peptidase S59 domain
Function: The NUP C-terminal domains of Nup98 and Nup145 possess peptidase S59
 autoproteolytic activity.
XX
CC   -!- SIMILARITY: Contains # peptidase S59 domain.
XX
FT   From: PS51434
FT   DOMAIN     from     to       Peptidase S59 #.
XX
Chop: Nter=0; Cter=0;
Size: 135-150;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P52948;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/03/05
//
AC   PRU00767;
DC   Domain;
TR   PROSITE; PS51437; CG_1; 1; level=0
XX
Names: CG-1 DNA-binding domain
Function: The CG-1 domain of CAMTA recognizes specific CGCG box-containing DNA
 sequences, and a nearby region activates the transcription.
XX
CC   -!- SIMILARITY: Contains # CG-1 DNA-binding domain.
XX
DR   PROSITE; PS50079; NLS_BP; 0-1; trigger=yes
XX
GO   GO:0006350; P:transcription
GO   GO:0006355; P:regulation of transcription, DNA-dependent
XX
KW   Activator
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51437
FT   DNA_BIND   from     to       CG-1 #.
XX
Chop: Nter=0; Cter=0;
Size: 105-135;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y6Y1;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/03/02
//
AC   PRU00768;
DC   Domain;
TR   PROSITE; PS50079; NLS_BP; 1; level=-1
XX
Names: Bipartite nuclear localization signal
Function: The uptake of protein by the nucleus is extremely selective and
 nuclear proteins must therefore contain within their final structure a signal
 that specifies selective accumulation in the nucleus.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
XX
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
XX
FT   From: PS50079
FT   MOTIF        -1      7       Nuclear localization signal (By
FT                                similarity) #.
XX
Chop: Nter=0; Cter=0;
Size: 15-20;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9Y6Y1;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/03/02
//
AC   PRU00769;
DC   Domain;
TR   PROSITE; PS51438; ALBUMIN_2; 1; level=0
XX
Names: Albumin domain
Function: A domain consisting of 10 alpha-helices found in serum transport
 proteins.
XX
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the ALB/AFP/VDB family.
CC   -!- SIMILARITY: Contains # albumin domain.
XX
GO   GO:0005576; C:extracellular region
XX
KW   Secreted
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51438
FT   DOMAIN     from     to       Albumin #.
FT   DISULFID     14     60       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     59     67       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     83    100       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     99    110       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    137    182       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    181    190       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 30-230;
Related: None;
Repeats: 1-7;
Topology: Not cytoplasmic;
Example: P49822;
Scope:
 Eukaryota; Vertebrata
Comments: None;
XX
# Revision 1.2  2009/04/08
//
AC   PRU00770;
DC   Domain;
TR   PROSITE; PS51439; MENTAL; 1; level=0
XX
Names: MENTAL domain
Function: The ~170-amino acid MENTAL (MLN64 N-terminal) domain mediates MLN64
 and MENTHO homo- and hetero-interactions, targets both proteins to late
 endosomes and binds cholesterol.
XX
CC   -!- SIMILARITY: Contains # MENTAL domain.
XX
DR   General; Transmembrane; -; 4; trigger=strict
XX
GO   GO:0015485; F:cholesterol binding
GO   GO:0017127; F:cholesterol transporter activity
GO   GO:0005768; C:endosome
GO   GO:0008289; F:lipid binding
GO   GO:0006869; P:lipid transport
GO   GO:0016020; C:membrane
GO   GO:0006810; P:transport
XX
KW   Endosome
KW   Lipid-binding
KW   Lipid transport
KW   Membrane
KW   Transport
FT   From: PS51439
FT   DOMAIN     from     to       MENTAL #.
XX
Chop: Nter=0; Cter=0;
Size: 170-175;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q14849;
Scope:
 Eukaryota; Metazoa
Comments: None;
XX
# Revision 1.3  2009/04/02
//
AC   PRU00771;
DC   Domain;
TR   PROSITE; PS51441; CPCD_LIKE; 1; level=0
XX
Names: CpcD-like domain
Function: The cpcD-like domain is found in ferredoxin-NADP(+) oxydoreductase
 (FNR) (EC=1.18.1.2) and phycobilisome (PBS)-associated linker proteins from
 numerous cyanobacteria.
XX
CC   -!- SIMILARITY: Contains # cpcD-like domain.
XX
GO   GO:0030089; C:phycobilisome
XX
KW   Phycobilisome
XX
FT   From: PS51441
FT   DOMAIN     from     to       CpcD-like #.
XX
Chop: Nter=0; Cter=0;
Size: 41-69;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P80558;
Scope:
 Bacteria; Cyanobacteria
Comments: None;
XX
# Revision 1.1  2009/04/08
//
AC   PRU00772;
DC   Domain;
TR   PROSITE; PS51442; M_PRO; 1; level=0
XX
Names: Coronavirus main protease (M-pro) domain
 3C-like proteinase (3CL-pro)
 peptidase family C30
Function: It is a viral cysteine proteinase wich mediates most maturation
 cleavage events within the precursor polyprotein.
XX
case <FTGroup:1>
CC   -!- FUNCTION: The main proteinase 3CL-PRO is responsible for the
CC       majority of cleavages as it cleaves the C-terminus of replicase
CC       polyprotein at 11 sites. Recognizes substrates containing the core
CC       sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog
CC       Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK (By similarity).
CC   -!- SIMILARITY: Contains # peptidase C30 domain.
XX
GO   GO:0019082; P:viral protein processing
GO   GO:0006508; P:proteolysis
GO   GO:0008233; F:peptidase activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0008234; F:cysteine-type peptidase activity
XX
KW   Hydrolase
KW   Protease
KW   Thiol protease
end case
XX
FT   From: PS51442
FT   DOMAIN     from     to       Peptidase C30 #.
FT   ACT_SITE     41     41       For 3CL-PRO activity.
FT   Group: 1; Condition: H
FT   ACT_SITE    144    144       For 3CL-PRO activity.
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 292-317;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0C6Y1;
Scope:
 Viruses; Coronavirinae
Comments: None;
XX
# Revision 1.2  2010/07/20
//
AC   PRU00773;
DC   Domain;
TR   PROSITE; PS51443; PCS; 1; level=0
XX
Names: Phytochelatin synthase (PCS) domain
Function: Phytochelatins (PCs) are synthesized posttranslationally by the PC
 synthase (PCS) (EC 2.3.2.15), a gamma-glutamylcysteine (gamma-EC)
 transpeptidase. PC synthesis is proposed to have two distinct steps: (Step1)
 formation of gamma-EC concomitant with the cleavage of Gly from GSH; and
 (Step 2) transfer of the gamma-EC unit to an acceptor GSH molecule or an
 oligomeric PC peptide (PCn).
XX
case <FTGroup:1>
DE   + RecName: Full=Glutathione gamma-glutamylcysteinyltransferase;
DE            EC=2.3.2.15;
end case
XX
case <FTGroup:1>
CC   -!- CATALYTIC ACTIVITY: Glutathione + (Glu(-Cys))(n)-Gly = Gly +
CC       (Glu(-Cys))(n+1)-Gly.
end case
CC   -!- SIMILARITY: Belongs to the phytochelatin synthase family.
CC   -!- SIMILARITY: Contains # peptidase C83 domain.
XX
case <FTGroup:1>
GO   GO:0016756; F:glutathione gamma-glutamylcysteinyltransferase activity
GO   GO:0046938; P:phytochelatin biosynthetic process
GO   GO:0008415; F:acyltransferase activity
XX
KW   Transferase
KW   Acyltransferase
end case
XX
FT   From: PS51443
FT   DOMAIN     from     to       Peptidase C83 #.
FT   ACT_SITE     56     56       By similarity.
FT   Group: 1; Condition: C
FT   ACT_SITE    168    168       By similarity.
FT   Group: 1; Condition: H
FT   ACT_SITE    186    186       By similarity.
FT   Group: 1; Condition: D
XX
Chop: Nter=0; Cter=0;
Size: 210-231;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q2TE74;
Scope:
 Eukaryota
 Bacteria; Cyanobacteria
Comments: None;
XX
# Revision 1.2  2009/04/08
//
AC   PRU00774;
DC   Domain;
TR   PROSITE; PS51444; FH2; 1; level=0
XX
Names: Formin homology-2 (FH2) domain
Function: The defining feature of formins is a highly conserved ~400 residue
 region, the Formin Homology-2 (FH2) domain, which forms a head-to-tail ring-
 shaped dimer, and directly binds to the actin filament at its barbed end. The
 FH2 domain catalyzes the nucleation and elongation of actin filament,
 preventing capping proteins from binding to the barbed end.
XX
CC   -!- SIMILARITY: Contains # FH2 (formin homology 2) domain.
XX
GO   GO:0003779; F:actin binding
GO   GO:0030036; P:actin cytoskeleton organization
GO   GO:0005856; C:cytoskeleton
XX
KW   Actin-binding
KW   Cytoskeleton
FT   From: PS51444
FT   DOMAIN     from     to       FH2 #.
XX
Chop: Nter=0; Cter=0;
Size: 285-486;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O60610;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/04/08
//
AC   PRU00775;
DC   Domain;
TR   PROSITE; PS51445; PBS_LINKER; 1; level=0
XX
Names: Phycobilisome (PBS) linker domain
Function: Phycobilisome (PBS) linker polypeptides share a conserved domain of
 ~180 residues, which can be present in one or multiple copies.
XX
CC   -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC   -!- SIMILARITY: Contains # PBS-linker domain.
XX
GO   GO:0030089; C:phycobilisome
XX
KW   Phycobilisome
XX
FT   From: PS51445
FT   DOMAIN     from     to       PBS-linker #.
XX
Chop: Nter=0; Cter=0;
Size: 62-194;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: P51263;
Scope:
 Bacteria; Cyanobacteria
 Eukaryota
Comments: None;
XX
# Revision 1.2  2009/04/09
//
AC   PRU00776;
DC   Domain;
TR   PROSITE; PS51446; PACIFASTIN; 1; level=0
XX
Names: Pacifastin domain
Function: Fill in
XX
CC   -!- SIMILARITY: Belongs to the protease inhibitor I19 family.
CC   -!- SIMILARITY: Contains # pacifastin domain.
XX
GO   GO:0004866; F:endopeptidase inhibitor activity
GO   GO:0004867; F:serine-type endopeptidase inhibitor activity
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
KW   Protease inhibitor
KW   Serine protease inhibitor
XX
FT   From: PS51446
FT   DOMAIN     from     to       Pacifastin #.
FT   SITE         29     30       Reactive bond (By similarity).
FT   Condition: x-K
FT   DISULFID      4     19       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     14     32       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     17     27       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 25-48;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: O46163;
Scope:
 Eukaryota; Arthropoda
Comments: None;
XX
# Revision 1.2  2009/04/15
//
AC   PRU00777;
DC   Domain;
TR   PROSITE; PS51272; SLH; 1; level=0
XX
Names: S-layer homology (SLH) domain
Function: S-layers are paracrystalline mono-layered assemblies of
 (glyco)proteins which coat the surface of bacteria. Several S-layer proteins
 and some other cell wall proteins contain one or more copies of a domain of
 about 50-60 residues, which has been called SLH (for S-layer homology).
XX
CC   -!- SIMILARITY: Contains # SLH (S-layer homology) domain.
XX
FT   From: PS51272
FT   DOMAIN     from     to       SLH #.
XX
Chop: Nter=0; Cter=0;
Size: 33-84;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P49051;
Scope:
 Bacteria
Comments: None;
XX
# Revision 1.2  2009/04/14
//
AC   PRU00778;
DC   Domain;
TR   PROSITE; PS51447; FDX_ACB; 1; level=0
XX
Names: Ferredoxin-fold anticodon binding (FDX-ACB) domain
Function: Bacterial and mitochondrial phenylalanine-tRNA synthetases (PheRSs)
 share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents
 a canonical double split alpha+beta motif having no insertions.
XX
CC   -!- SIMILARITY: Contains # FDX-ACB domain.
XX
FT   From: PS51447
FT   DOMAIN     from     to       FDX-ACB #.
XX
Chop: Nter=0; Cter=0;
Size: 72-113;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q98CQ1;
Scope:
 Bacteria
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/03/08
//
AC   PRU00779;
DC   Domain;
TR   PROSITE; PS51448; P_TREFOIL_2; 1; level=0
XX
Names: P-type ('Trefoil') domain
Function: The P-type domain is a cysteine-rich domain of approximately forty
 five amino-acid residues, which is found in some extracellular eukaryotic
 proteins.
XX
CC   -!- SIMILARITY: Contains # P-type (trefoil) domain.
XX
DR   PROSITE; PS00025; P_TREFOIL_1; 1; trigger=no
XX
FT   From: PS51448
FT   DOMAIN     from     to       P-type #.
XX
Chop: Nter=0; Cter=0;
Size: 31-62;
Related: None;
Repeats: 1-6;
Topology: Undefined;
Example: Q8CH34;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/05/12
//
AC   PRU00780;
DC   Domain;
TR   PROSITE; PS51449; MTTASE_N; 1; level=0
TR   PROSITE; PS01278; MTTASE_RADICAL; 1; level=0
XX
Names: Methylthiotransferase domains
Function: Methylthiotransferases (MTTases) catalyze a C-H to C-S bond 
 conversion in the methylthiolation of tRNA or ribosomal protein substrate.
XX
case <OC:Bacteria> or <OC:Archaea>
DE   + RecName: EC=2.-.-.-;
DE   + AltName: Full=methylthiotransferase;
end case
XX
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters. One cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC       similarity).
case <OC:Bacteria>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
end case
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family.
case <Feature:PS51449>
CC   -!- SIMILARITY: Contains # MTTase N-terminal domain.
end case
XX
GO   GO:0005506; F:iron ion binding
GO   GO:0051539; F:4 iron, 4 sulfur cluster binding
case <OC:Bacteria> or <OC:Archaea>
GO   GO:0016740; F:transferase activity
end case
case <OC:Bacteria>
GO   GO:0005737; C:cytoplasm
end case
XX
KW   4Fe-4S
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
KW   S-adenosyl-L-methionine
case <OC:Bacteria> or <OC:Archaea>
KW   Transferase
end case
case <OC:Bacteria>
KW   Cytoplasm
end case
XX
FT   From: PS51449
FT   DOMAIN     from     to       MTTase N-terminal #.
FT   METAL        10     10       Iron-sulfur (4Fe-4S) (By similarity).
FT   Condition: C
FT   METAL        46     46       Iron-sulfur (4Fe-4S) (By similarity).
FT   Condition: C
FT   METAL        77     77       Iron-sulfur (4Fe-4S) (By similarity).
FT   Condition: C
FT   From: PS01278
FT   METAL         7      7       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        11     11       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        14     14       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: 90-150;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q54KV4; B4RNW8;
Scope:
 Bacteria
 Eukaryota
 Archaea
Comments: None;
XX
# Revision 1.1  2009/05/28
//
AC   PRU00781;
DC   Domain;
TR   PROSITE; PS51455; PIPK; 1; level=0
XX
Names: Phosphatidylinositol phosphate kinase (PIPK) domain
Function: Phosphatidylinositol phosphate kinases (PIPKs) phosphorylate
 phosphatidylinositol phosphate (PtdInsP) to phosphatidylinositol bisphosphate
 (PtdInsP2).
XX
CC   -!- SIMILARITY: Contains # PIPK domain.
XX
GO   GO:0005524; F:ATP binding
GO   GO:0016301; F:kinase activity
GO   GO:0000166; F:nucleotide binding
GO   GO:0046488; P:phosphatidylinositol metabolic process
GO   GO:0016307; F:phosphatidylinositol phosphate kinase activity
GO   GO:0016740; F:transferase activity
XX
KW   ATP-binding
KW   Kinase
KW   Nucleotide-binding
KW   Transferase
XX
FT   From: PS51455
FT   DOMAIN     from     to       PIPK #.
XX
Chop: Nter=0; Cter=0;
Size: 314-442;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q56YP2;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.2  2010/02/05
//
AC   PRU00783;
DC   Domain;
TR   PROSITE; PS50146; DAGK; 1; level=0
XX
Names: DAG-kinase catalytic (DAGKc) domain
 diacylglycerol kinase catalytic domain
 DGK C4-a domain
 DgkB domain 1
Function: The DAG-kinase catalytic domain (DAGKc) is present in mammalian 
 lipid kinases, such as diacylglycerol (DAG), ceramide and sphingosine 
 kinases, as well as in related bacterial lipid kinases.
XX
DE   + RecName: EC 2.7.-.-;
XX
CC   -!- SIMILARITY: Contains # DAGKc domain.
XX
GO   GO:0016740; F:transferase activity
GO   GO:0016301; F:kinase activity
XX
KW   Kinase
KW   Transferase
XX
FT   From: PS50146
FT   DOMAIN     from     to       DAGKc #.
XX
Chop: Nter=0; Cter=0;
Size: 110-195;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q87ZA2; Q03603;
Scope:
 Bacteria
 Eukaryota
 Archaea
Comments: None;
XX
# Revision 1.1  2009/06/19
//
AC   PRU00784;
DC   Domain;
TR   PROSITE; PS51457; BEN; 1; level=0
XX
Names: BEN domain
Function: The BEN domain is predicted to functions as an adaptor for the
 higher-order structuring of chromatin, and recruitment of chromatin modifying
 factors in transcriptional regulation.
XX
CC   -!- SIMILARITY: Contains # BEN domain.
XX
FT   From: PS51457
FT   DOMAIN     from     to       BEN #.
XX
Chop: Nter=0; Cter=0;
Size: 86-121;
Related: None;
Repeats: 1-4;
Topology: Undefined;
Example: Q5T5X7;
Scope:
 Eukaryota; Euteleostomi
 Viruses; Orthopoxvirus
Comments: None;
XX
# Revision 1.1  2009/06/24
//
AC   PRU00791;
DC   Domain;
TR   PROSITE; PS51459; FIDO; 1; level=0
XX
Names: Fido domain
Function: The fido domain of Vibrio VopS covalently modifies Rho GTPase
 threonine with AMP to inhibit downstream signaling events in host cells.
XX
CC   -!- SIMILARITY: Contains # fido domain.
XX
FT   From: PS51459
FT   DOMAIN     from     to       Fido #.
XX
Chop: Nter=0; Cter=0;
Size: 95-165;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q29JP8;
Scope:
 Eukaryota; Metazoa
 Bacteria
 Viruses; dsDNA viruses, no RNA stage
Comments: None;
XX
# Revision 1.1  2009/10/16
//
AC   PRU00792;
DC   Domain;
TR   PROSITE; PS51460; GAR; 1; level=0
XX
Names: GAR domain
Function: The GAR domain comprises ~57 amino acids and has been shown to bind
 to microtubules.
XX
CC   -!- SIMILARITY: Contains # GAR domain.
XX
GO   GO:0005856; C:cytoskeleton
XX
KW   Cytoskeleton
XX
FT   From: PS51460
FT   DOMAIN     from     to       GAR #.
XX
Chop: Nter=0; Cter=0;
Size: 63-89;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8JZP9;
Scope:
 Eukaryota; Euarchontoglires
Comments: None;
XX
# Revision 1.2  2010/07/20
//
AC   PRU00793;
DC   Domain;
TR   PROSITE; PS51461; NC1_FIB; 1; level=0
XX
Names: Fibrillar collagen C-terminal non-collagenous (NC1) domain
Function: The NC1 domain is the most conserved part of fibrillar collagens
 from invertebrates to vertebrates (types I-III, V, XI, XXIV and XXVII).
XX
case <OC:Metazoa>
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (By similarity).
end case
CC   -!- SIMILARITY: Contains # fibrillar collagen NC1 domain.
case <OC:Metazoa>
CC   -!- SIMILARITY: Belongs to the fibrillar collagen family.
XX
GO   GO:0005615; C:extracellular space
GO   GO:0005201; F:extracellular matrix structural constituent
XX
KW   Collagen
KW   Extracellular matrix
KW   Secreted
XX
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51461
FT   DOMAIN     from     to       Fibrillar collagen NC1 #.
FT   DISULFID     31     31       Interchain (By similarity).
FT   Tag: disulf; Condition: C
FT   DISULFID     37     37       Interchain (By similarity).
FT   Tag: disulf; Condition: C
FT   DISULFID     54     54       Interchain (By similarity).
FT   Tag: disulf; Condition: C
FT   DISULFID     63     63       Interchain (By similarity).
FT   Tag: disulf; Condition: C
FT   DISULFID     72    225       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID    133    178       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 185-251;
Related: None;
Repeats: 1-4;
Topology: Not cytoplasmic;
Example: P02452;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.5  2009/07/28
//
AC   PRU00794;
DC   Domain;
TR   PROSITE; PS51462; NUDIX; 1; level=0
XX
Names: Nudix hydrolase domain
Function: The Nudix superfamily is widespread among eucaryotes, bacteria,
 archaea and viruses and consists mainly of pyrophosphohydrolases that act
 upon substrates of general structure NUcleoside DIphosphate linked to another
 moiety, X (NDP-X) to yield NMP plus P-X.
XX
CC   -!- SIMILARITY: Contains # nudix hydrolase domain.
XX
DR   PROSITE; PS00893; NUDIX_BOX; 1; trigger=no
DR   PROSITE; PS01293; NUDIX_COA; 0-1; trigger=no
XX
GO   GO:0016787; F:hydrolase activity
GO   GO:0046872; F:metal ion binding
XX
KW   Hydrolase
KW   Metal-binding
XX
FT   From: PS51462
FT   DOMAIN     from     to       Nudix hydrolase #.
FT   MOTIF        36     57       Nudix box #.
XX
Chop: Nter=0; Cter=0;
Size: 105-260;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5RD76;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None;
XX
# Revision 1.2  2009/10/02
//
AC   PRU00795;
DC   Domain;
TR   PROSITE; PS50219; CNH; 1; level=0
XX
Names: Citron homology (CNH) domain
Function: Little is known about the function of the CNH domain, although it
 has been proposed to regulate kinase activity and to mediate binding to the
 GTP-bound forms of Rac and Rho.
XX
CC   -!- SIMILARITY: Contains # CNH domain.
XX
FT   From: PS50219
FT   DOMAIN     from     to       CNH #.
XX
Chop: Nter=0; Cter=0;
Size: 263-421;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O95819;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2009/10/16
//
AC   PRU00796;
DC   Domain;
TR   PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1; level=0
XX
Names: Glucose-6-phosphate isomerase family
Function: Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) or phosphoglucose 
 isomerase (PGI) is a glycolytic enzyme that catalyzes the reversible
 isomerization of glucose-6-phosphate and fructose-6-phosphate.
XX
ID   G6PI
DE   + RecName: Full=Glucose-6-phosphate isomerase;
DE            Short=GPI;
DE            EC=5.3.1.9;
DE   AltName: Full=Phosphoglucose isomerase;
DE            Short=PGI;
DE   AltName: Full=Phosphohexose isomerase;
DE            Short=PHI;
GN   Name=pgi;
XX
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6-
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the GPI family.
XX
DR   PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1; trigger=no
case <Feature:PS51463:472=K>
DR   PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1; trigger=no
end case
XX
GO   GO:0004347; F:glucose-6-phosphate isomerase activity
GO   GO:0006096; P:glycolysis
GO   GO:0006094; P:gluconeogenesis
GO   GO:0005737; C:cytoplasm
XX
KW   Gluconeogenesis
KW   Glycolysis
KW   Isomerase
KW   Cytoplasm
XX
FT   From: PS51463
FT   ACT_SITE    328    328       Proton donor (By similarity).
FT   Condition: E
FT   ACT_SITE    360    360       By similarity.
FT   Condition: H
FT   ACT_SITE    472    472       By similarity.
FT   Condition: K
XX
Chop: Nter=0; Cter=0;
Size: 150-600;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q39SU1;
Scope:
 Bacteria
 Eukaryota
 Archaea
Comments: None;
XX
# Revision 1.1  2009/09/10
//
AC   PRU00797;
DC   Domain;
TR   PROSITE; PS51464; SIS; 1; level=0
XX
Names: SIS domain
Function: The sugar isomerase (SIS) domain is a phosphosugar-binding module 
 that is found in a variety of eubacterial, archaebacterial and eukaryotic 
 glycolytic proteins that have a role in phosphosugar isomerization or
 regulation.
XX
CC   -!- SIMILARITY: Contains # SIS domain.
XX
GO   GO:0005529; F:sugar binding
GO   GO:0005975; P:carbohydrate metabolic process
XX
KW   Carbohydrate metabolism
XX
FT   From: PS51464
FT   DOMAIN    entry   exit       SIS #.
XX
Chop: Nter=0; Cter=0;
Size: 90-150;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: B0BP79;
Scope:
 Bacteria
 Eukaryota
 Archaea
 Viruses; dsDNA viruses, no RNA stage
Comments: None;
XX
# Revision 1.1  2009/09/17
//
AC   PRU00799;
DC   Domain;
TR   PROSITE; PS51466; PINIT; 1; level=0
XX
Names: PINIT domain
Function: The PINIT domain serves as a scaffold to coordinate PCNA to promote
 SUMO conjugation to both consensus and nonconsensus lysine side chains.
XX
CC   -!- SIMILARITY: Contains # PINIT domain.
XX
KW   Ubl conjugation pathway
KW   Ubl conjugation
XX
FT   From: PS51466
FT   DOMAIN     from     to       PINIT #.
XX
Chop: Nter=0; Cter=0;
Size: 143-176;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q04195;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/04/22
//
AC   PRU00801;
DC   Domain;
TR   PROSITE; PS51468; VIT; 1; level=0
XX
Names: VIT domain
Function: The VIT domain can be regarded as the characteristic domain of the
 inter-alpha-trypsin inhibitor heavy chain (ITIH) family.
XX
CC   -!- SIMILARITY: Contains # VIT domain.
XX
FT   From: PS51468
FT   DOMAIN     from     to       VIT #.
XX
Chop: Nter=0; Cter=0;
Size: 117-159;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O02668;
Scope:
 Eukaryota; Eutheria
Comments: None;
XX
# Revision 1.1  2009/11/25
//
AC   PRU00802;
DC   Domain;
TR   PROSITE; PS51469; SUN; 1; level=0
XX
Names: SUN domain
Function: SUN proteins are anchored in the inner nuclear envelope by their
 transmembrane segment and oriented in the membrane such that the C-terminal
 SUN domain is located in the space between the inner and outer nuclear
 membrane. Here, the SUN domain can interact with the C-terminal tail of an
 outer nuclear envelope protein that binds to the cytoskeleton, including the
 centrosome.
XX
CC   -!- SIMILARITY: Contains # SUN domain.
XX
FT   From: PS51469
FT   DOMAIN     from     to       SUN #.
XX
Chop: Nter=0; Cter=0;
Size: 148-200;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q12232;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/01/08
//
AC   PRU00804;
DC   Domain;
TR   PROSITE; PS51472; RRM_NUP35; 1; level=0
XX
Names: RNA-recognition motif (RRM) Nup35-type domain
Function: The vertebrate nuclear pore protein Nup35, the ortholog of
 Saccharomyces cerevisiae Nup53p, is suggested to interact with the NE
 membrane and to be required for nuclear morphology. The highly conserved
 region between vertebrate Nup35 and yeast Nup53p is predicted to contain an
 RNA-recognition motif (RRM) domain.
XX
CC   -!- SIMILARITY: Contains # RRM Nup35-type domain.
XX
GO   GO:0005643; C:nuclear pore
GO   GO:0005634; C:nucleus
GO   GO:0006810; P:transport
GO   GO:0051028; P:mRNA transport
XX
KW   Nuclear pore complex
KW   Nucleus
KW   Transport
KW   mRNA transport
XX
FT   From: PS51472
FT   DOMAIN     from     to       RRM Nup35-type #.
XX
Chop: Nter=0; Cter=0;
Size: 71-140;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q03790;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/07/20
//
AC   PRU00805;
DC   Domain;
TR   PROSITE; PS51471; FE2OG_OXY; 1; level=0
XX
Names: Fe(2+) 2-oxoglutarate dioxygenase domain
 Fe(II) 2-oxoglutarate dioxygenase domain
 PKHD (prolyl/lysyl hydroxylase) domain
 P4Hc domain
 2-oxoglutarate and Fe(II)-dependent oxygenases
 2OG-Fe(II) oxygenase superfamily
 2OG oxygenase families
Function: Enzymes with the Fe(2+) and 2-oxoglutarate (2OG)-dependent 
 dioxygenase domain typically catalyse the oxidation of an organic substrate
 using a dioxygen molecule, mostly by using ferrous iron as the active site
 cofactor and 2OG as a cosubstrate which is decarboxylated to succinate and 
 CO2.
XX
case <FTGroup:2>
DE   + RecName: EC 1.14.11.-;
else case <FTGroup:1>
DE   + RecName: EC 1.14.-.-;
end case
XX
case <FTGroup:1>
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
end case
CC   -!- SIMILARITY: Contains # Fe2OG dioxygenase domain.
XX
case <FTGroup:1>
GO   GO:0005506; F:iron ion binding
GO   GO:0055114; P:oxidation-reduction process
end case
case <FTGroup:2>
GO   GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
else case <FTGroup:1>
GO   GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
end case
XX
case <FTGroup:1>
KW   Dioxygenase
KW   Iron
KW   Metal-binding
KW   Oxidoreductase
end case
XX
FT   From: PS51471
FT   DOMAIN     from     to       Fe2OG dioxygenase #.
FT   METAL        20     20       Iron (By similarity).
FT   Group: 1; Group: 2; Condition: H
FT   METAL        22     22       Iron (By similarity).
FT   Group: 1; Group: 2; Condition: D
FT   METAL        70     70       Iron (By similarity).
FT   Group: 1; Group: 2; Condition: H
FT   BINDING      80     80       2-oxoglutarate (Potential).
FT   Group: 2; Condition: [RK]
XX
Chop: Nter=0; Cter=0;
Size: 80-160;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: A1K320;
Scope:
 Bacteria
 Eukaryota
 Viruses
Comments: None;
XX
# Revision 1.3  2010/12/02
//
AC   PRU00806;
DC   Domain;
TR   PROSITE; PS51473; GNK2; 1; level=0
XX
Names: Gnk2-homologous domain
Function: The Gnk2-homologous domain is composed of two alpha-helices and a
 five stranded beta-sheet, which forms a compact single-domain architecture
 with an alpha+beta-fold. It contains a C-X(8)-C-X(2)-C motif. Cysteine
 residues form three intramolecular disulfide bridges: C1-C5, C2-C3, and
 C4-C6.
XX
CC   -!- SIMILARITY: Contains # Gnk2-homologous domain.
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51473
FT   DOMAIN     from     to       Gnk2-homologous #.
FT   DISULFID      8     84       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     60     69       By similarity.
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID     72     97       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 88-135;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q9ZU94;
Scope:
 Eukaryota; Viridiplantae
Comments: None;
XX
# Revision 1.2  2010/01/20
//
AC   PRU00810;
DC   Domain;
TR   PROSITE; PS51477; PAH; 1; level=0
XX
Names: PAH domain
Function: The paired amphipathic helix (PAH) domain is a protein-protein
 interaction domain present in eukaryotic proteins implied in transcription
 down-regulation, such as the SIN3 family of proteins.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains # PAH (paired amphipathic helix) domain.
XX
KW   Nucleus
XX
FT   From: PS51477
FT   DOMAIN     from     to       PAH #.
XX
Chop: Nter=0; Cter=0;
Size: 59-96;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q60520;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/02/10
//
AC   PRU00813;
DC   Domain;
TR   PROSITE; PS51480; DHAL; 1; level=0
XX
Names: DhaL domain
Function: The DhaL domain is a nucleotide-binding domain found in
 dihydroxyacetone (Dha) kinases.
XX
CC   -!- SIMILARITY: Contains # DhaL domain.
XX
FT   From: PS51480
FT   DOMAIN     from     to       DhaL #.
XX
Chop: Nter=0; Cter=0;
Size: 72-223;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9CIV7;
Scope:
 Bacteria
 Eukaryota
Comments: None;
XX
# Revision 1.2  2010/03/10
//
AC   PRU00814;
DC   Domain;
TR   PROSITE; PS51481; DHAK; 1; level=0
XX
Names: DhaK domain
Function: The DhaK domain is the dihydroxyacetone- (Dha-)binding domain of Dha
 kinases.
XX
CC   -!- SIMILARITY: Contains # DhaK domain.
XX
GO   GO:0016301; F:kinase activity
GO   GO:0016740; F:transferase activity
XX
KW   Kinase
KW   Transferase
XX
FT   From: PS51481
FT   DOMAIN     from     to       DhaK #.
FT   ACT_SITE    212    212       Tele-hemiaminal-histidine intermediate
FT                                (By similarity).
FT   Condition: H
FT   BINDING      50     50       Dihydroxyacetone (By similarity).
FT   Condition: H
FT   BINDING     103    103       Dihydroxyacetone (By similarity).
FT   Condition: D
XX
Chop: Nter=0; Cter=0;
Size: 310-395;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P76015;
Scope:
 Eukaryota
 Bacteria
Comments: None;
XX
# Revision 1.3  2010/05/06
//
AC   PRU00815;
DC   Domain;
TR   PROSITE; PS51482; DEGV; 1; level=0
XX
Names: DegV domain
Function: The function of DegV proteins is not yet completely understood, but
 structural evidence indicates that they can bind different fatty acids.
XX
CC   -!- SIMILARITY: Contains # DegV domain.
XX
FT   From: PS51482
FT   DOMAIN     from     to       DegV #.
XX
Chop: Nter=0; Cter=0;
Size: 127-315;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q97RQ6;
Scope:
 Bacteria
Comments: None;
XX
# Revision 1.1  2010/07/19
//
AC   PRU00816;
DC   Domain;
TR   PROSITE; PS51483; B5; 1; level=0
XX
Names: B5 domain
Function: The B5 domain has been shown to bind DNA.
XX
CC   -!- SIMILARITY: Contains # B5 domain.
XX
GO   GO:0006432; P:phenylalanyl-tRNA aminoacylation
XX
KW   Aminoacyl-tRNA synthetase
KW   Protein biosynthesis
XX
FT   From: PS51483
FT   DOMAIN     from     to       B5 #.
XX
Chop: Nter=0; Cter=0;
Size: 59-174;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9PP35;
Scope:
 Bacteria
 Archaea
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/04/21
//
AC   PRU00817;
DC   Domain;
TR   PROSITE; PS51484; G8; 1; level=0
XX
Names: G8 domain
Function: The G8 domain may be involved in extracellular ligand binding and
 progress of catalysis.
XX
CC   -!- SIMILARITY: Contains # G8 domain.
XX
FT   From: PS51484
FT   DOMAIN     from     to       G8 #.
XX
Chop: Nter=0; Cter=0;
Size: 111-149;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: A3KPQ7;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/06/04
//
AC   PRU00818;
DC   Domain;
TR   PROSITE; PS51485; PHYTOCYANIN; 1; level=0
XX
Names: Phytocyanin domain
Function: Phytocyanins are blue copper proteins found in chloropasts of higher
 plants.
XX
CC   -!- SIMILARITY: Contains # phytocyanin domain.
XX
case <FTGroup:1>
DR   PROSITE; PS00196; COPPER_BLUE; 1; trigger=no
end case
XX
case <FTGroup:1>
GO   GO:0005507; F:copper ion binding
end case
XX
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51485
FT   DOMAIN     from     to       Phytocyanin #.
FT   METAL        43     43       Copper.
FT   Group: 1; Condition: H
FT   METAL        84     84       Copper.
FT   Group: 1; Condition: C
FT   METAL        89     89       Copper.
FT   Group: 1; Condition: H
FT   METAL        94     94       Copper.
FT   Group: 1; Condition: [MQ]
FT   DISULFID     56     90       By similarity.
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 57-116;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P29602;
Scope:
 Eukaryota; Magnoliophyta
Comments: None;
XX
# Revision 1.3  2010/08/31
//
AC   PRU00819;
DC   Domain;
TR   PROSITE; PS51486; REKLES; 1; level=0
XX
Names: REKLES domain
Function: REKLES consists of two subdomains: a modestly conserved N-terminal
 REKLESalpha and a highly conserved C-terminal REKLESbeta. REKLESalpha and
 -beta are required, respectively, for nuclear entry and export of Bright
 during its nucleoplasmic shuttling. In addition to its function in nuclear
 export, the REKLESbeta subdomain regulates the binding of Bright to nuclear
 matrix association (or attachment) regions (MARs), its self- and paralogous
 (Bdp) association and stoichiometry, and its retention within the nuclear
 matrix.
XX
CC   -!- SIMILARITY: Contains # REKLES domain.
XX
FT   From: PS51486
FT   DOMAIN     from     to       REKLES #.
XX
Chop: Nter=0; Cter=0;
Size: 76-119;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: A2BEA6;
Scope:
 Eukaryota; Metazoa
Comments: None;
XX
# Revision 1.1  2010/06/24
//
AC   PRU00820;
DC   Domain;
TR   PROSITE; PS51487; NBD; 1; level=0
XX
Names: NBD domain
Function: The Rag-1 nonamer binding domain (NBD) is a DNA-binding domain
 involved in the somatic site-specific recombination reaction known as V(D)J
 recombination.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DOMAIN: The NBD (nonamer binding) DNA-binding domain mediates the
CC       specific binding to the nonamer RSS motif by forming a tightly
CC       interwoven homodimer that binds and synapses 2 nonamer elements,
CC       with each NBD making contact with both DNA molecules. Each RSS is
CC       composed of well-conserved heptamer (consensus 5'-CACAGTG-3') and
CC       nonamer (consensus 5'-ACAAAAACC-3') sequences separated by a
CC       spacer of either 12 bp or 23 bp (By similarity).
CC   -!- SIMILARITY: Belongs to the RAG1 family.
CC   -!- SIMILARITY: Contains # NBD (nonamer binding) DNA-binding domain.
XX
GO   GO:0005634; C:nucleus
GO   GO:0043565; F:sequence-specific DNA binding
GO   GO:0033151; P:V(D)J recombination
XX
KW   DNA recombination
KW   DNA-binding
KW   Nucleus
XX
FT   From: PS51487
FT   DNA_BIND      1     68       NBD.
XX
Chop: Nter=0; Cter=0;
Size: 58-78;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q91829;
Scope:
 Eukaryota; Euteleostomi
Comments: None;
XX
# Revision 1.1  2010/07/16
//
AC   PRU00821;
DC   Domain;
TR   PROSITE; PS51488; KBD; 1; level=0
XX
Names: KBD domain
Function: The c-Kit-binding domain (KBD) composed of about 50 amino acids is
 found in a family of membrane-bound molecules, Spreds, which contain an EVH1
 domain in the N-terminus and a Sprouty-related cysteine rich region (SPR
 domain) in the C-terminus.
XX
CC   -!- SIMILARITY: Contains # KBD domain.
XX
FT   From: PS51488
FT   DOMAIN     from     to       KBD #.
XX
Chop: Nter=0; Cter=0;
Size: 40-67;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6P6N5;
Scope:
 Eukaryota; Euteleostomi
Comments: None;
XX
# Revision 1.1  2010/06/24
//
AC   PRU00822;
DC   Domain;
TR   PROSITE; PS51489; BUB1_N; 1; level=0
XX
Names: BUB1 N-terminal domain
Function: The BUB1 N-terminal domain mediates the binding of BUB1 and BUBR1 to
 the mitotic kinetochore protein Blinkin.
XX
CC   -!- SIMILARITY: Contains # BUB1 N-terminal domain.
XX
KW   Cell cycle
KW   Nucleus
XX
FT   From: PS51489
FT   DOMAIN     from     to       BUB1 N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 152-182;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O59767;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/12/16
//
AC   PRU00823;
DC   Domain;
TR   PROSITE; PS51490; KHA; 1; level=0
XX
Names: KHA domain
Function: The KHA domain is essential for interaction of plant inward
 rectifying potassium (K(+)in) channels. The KHA domain mediates
 tetramerization and/or stabilization of the heteromers.
XX
CC   -!- SIMILARITY: Contains # KHA domain.
XX
FT   From: PS51490
FT   DOMAIN     from     to       KHA #.
XX
Chop: Nter=0; Cter=0;
Size: 56-91;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q7L273;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/06/25
//
AC   PRU00824;
DC   Domain;
TR   PROSITE; PS51491; TAU_MAP_2; 1; level=0
XX
Names: Tau and MAP proteins tubulin-binding repeat
Function: The C-terminal region of a subset of Microtubule Associated Proteins
 (MAPs) contain three or four tandem repeats of a conserved domain of about
 thirty amino acid residues which is implicated in tubulin- binding and which
 seems to have a stiffening effect on microtubules.
XX
CC   -!- SIMILARITY: Contains # Tau/MAP repeat.
XX
DR   PROSITE; PS00229; TAU_MAP_1; 1; trigger=no
XX
GO   GO:0005874; C:microtubule
GO   GO:0007026; P:negative regulation of microtubule depolymerization
XX
KW   Microtubule
KW   Repeat
XX
FT   From: PS51491
FT   REPEAT     from     to       Tau/MAP #.
XX
Chop: Nter=0; Cter=0;
Size: 21-42;
Related: None;
Repeats: 3-4;
Topology: Undefined;
Example: Q5S6V2;
Scope:
 Eukaryota; Eutheria
Comments: None;
XX
# Revision 1.1  2010/07/20
//
AC   PRU00829;
DC   Domain;
TR   PROSITE; PS51496; CVC; 1; level=0
XX
Names: CVC domain
Function: The CVC (standing for Chx10/Vsx-1 and ceh-10) domain consists of
 approximately 50-60 amino acid residues. The CVC domain is predicted to
 influence transcriptional regulation through DNA-binding, protein-protein
 interaction and/or protein degradation processes. It is possible that the CVC
 domain is necessary for protein folding or protein-protein interactions
 because this domain is hydrophobic.
XX
CC   -!- SIMILARITY: Contains # CVC domain.
XX
GO   GO:0030528; F:transcription regulator activity
XX
FT   From: PS51496
FT   DOMAIN     from     to       CVC #.
XX
Chop: Nter=0; Cter=0;
Size: 43-85;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9IAL2;
Scope:
 Eukaryota; Metazoa
Comments: None;
XX
# Revision 1.1  2010/12/22
//
AC   PRU00830;
DC   Domain;
TR   PROSITE; PS51497; UMA; 1; level=0
XX
Names: UMA domain
Function: The UMA domain found in MVB12 and UBAP1 defines a novel adaptor that
 might recruit diverse targets to ESCRT-I.
XX
CC   -!- SIMILARITY: Contains # UMA domain.
XX
FT   From: PS51497
FT   DOMAIN     from     to       UMA #.
XX
Chop: Nter=0; Cter=0;
Size: 37-62;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q7SXX7;
Scope:
 Eukaryota; Euteleostomi
Comments: None;
XX
# Revision 1.1  2010/12/08
//
AC   PRU00831;
DC   Domain;
TR   PROSITE; PS51498; MABP; 1; level=0
XX
Names: MABP domain
Function: It is plausible that the eukaryotic MABP domains are adaptators that
 help linking other associated domains found in the same polypeptide to
 vesicular membranes
XX
CC   -!- SIMILARITY: Contains # MABP domain.
XX
FT   From: PS51498
FT   DOMAIN     from     to       MABP #.
XX
Chop: Nter=0; Cter=0;
Size: 129-170;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q7SXX7;
Scope:
 Eukaryota; Euteleostomi
Comments: None;
XX
# Revision 1.1  2010/12/21
//
AC   PRU00832;
DC   Domain;
TR   PROSITE; PS51499; APO; 1; level=0
XX
Names: APO domain
Function: All members of the APO gene family contain an ~100 amino acid
 residue-spanning region (APO motif 1) with conserved Cys, His, Gly,
 and acidic and basic amino acids. This highly conserved APO1 motif is
 duplicated at the C terminus (designated APO motif 2). The conserved  Cys in
 both motifs could provide ligands for tetranuclear Fe-S centers.
XX
CC   -!- SIMILARITY: Belongs to the APO family.
CC   -!- SIMILARITY: Contains # APO domain.
XX
FT   From: PS51499
FT   DOMAIN     from     to       APO #.
XX
Chop: Nter=0; Cter=0;
Size: 76-97;
Related: None;
Repeats: 2;
Topology: Undefined;
Example: Q9FH50;
Scope:
 Eukaryota; Arabidopsis
Comments: None;
XX
# Revision 1.1  2010/12/08
//
AC   PRU00833;
DC   Domain;
TR   PROSITE; PS51500; SIN; 1; level=0
XX
Names: Sin domain
Function: SinR and SinI share a multimerisation domain of ~40 amino acids.
XX
CC   -!- SIMILARITY: Contains # Sin domain.
XX
GO   GO:0045449; P:regulation of transcription
XX
FT   From: PS51500
FT   DOMAIN     from     to       Sin #.
XX
Chop: Nter=0; Cter=0;
Size: 28-49;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P22755;
Scope:
 Bacteria; Bacillus
Comments: None;
XX
# Revision 1.1  2010/12/08
//
AC   PRU00834;
DC   Domain;
TR   PROSITE; PS51501; ZF_DNL; 1; level=0
XX
Names: Zinc finger DNL-type
Function: Tim15 contains a zinc-finger motif (CXXC and CXXC) of ~100 residues,
 which has been named DNL after a short C-terminal motif of D(N/H)L.
XX
CC   -!- SIMILARITY: Contains # DNL-type zinc finger.
XX
GO   GO:0046872; F:metal ion binding
XX
KW   Metal-binding
KW   Zinc
KW   Zinc-finger
XX
FT   From: PS51501
FT   ZN_FING       1     98       DNL-type.
XX
Chop: Nter=0; Cter=0;
Size: 86-108;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: B5VQB0;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/12/08
//
AC   PRU00835;
DC   Domain;
TR   PROSITE; PS51502; S_R_A_B_BARREL; 1; level=0
XX
Names: Stress-response A/B barrel domain
Function: The stress-response A/B barrel domain is found in a class of stress-
 response proteins in plants and in some bacterial fructose-bisphosphate
 aldolase. The function of the stress-response A/B barrel domain is unknown.
XX
CC   -!- SIMILARITY: Contains # stress-response A/B barrel domain.
XX
FT   From: PS51502
FT   DOMAIN     from     to       Stress-response A/B barrel #.
XX
Chop: Nter=0; Cter=0;
Size: 34-105;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9LUV2;
Scope:
 Eukaryota; rosids
 Bacteria; Streptomyces
Comments: None;
XX
# Revision 1.2  2010/12/07
//
AC   PRU00836;
DC   Domain;
TR   PROSITE; PS51503; HIG1; 1; level=0
XX
Names: HIG1 domain
Function: HIG1 is a member of a well conserved eukaryote protein family. The
 predicted transmembrane helice (TMH) and loop regions represent the most
 highly conserved regions in these proteins.
XX
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Contains # HIG1 domain.
XX
DR   General; Transmembrane; -; 2; trigger=yes
XX
GO   GO:0016021; C:integral to membrane
GO   GO:0031966; C:mitochondrial membrane
XX
KW   Mitochondrion
XX
FT   From: PS51503
FT   DOMAIN     from     to       HIG1 #.
XX
Chop: Nter=0; Cter=0;
Size: 63-134;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6CWT4;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.3  2010/12/07
//
AC   PRU00837;
DC   Domain;
TR   PROSITE; PS51504; H15; 1; level=0
XX
Names: Linker histone H1/H5 globular (H15) domain
Function: The highly conserved H15 domain is essential for the binding of H1
 or H5 to the nucleosome.
XX
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- SIMILARITY: Contains # H15 (linker histone H1/H5 globular) domain.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family.
XX
GO   GO:0003677; F:DNA binding
GO   GO:0006334; P:nucleosome assembly
GO   GO:0000786; C:nucleosome
GO   GO:0005634; C:nucleus
XX
KW   Nucleus
KW   Chromosome
KW   DNA-binding
XX
FT   From: PS51504
FT   DOMAIN     from     to       H15 #.
XX
Chop: Nter=0; Cter=0;
Size: 18-89;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q94555;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/11/17
//
AC   PRU00838;
DC   Domain;
TR   PROSITE; PS51505; SCA7; 1; level=0
XX
Names: SCA7 domain
Function: ATXN7/Sgf73 and ATXN7L3, two subunits of the SAGA deubiquitination
 module, contain an ~50-residue SCA7 domain characterized by an atypical zinc-
 finger (ZnF) with a Cys-X(9,10)-Cys-X(5)-Cys-X(2)-His motif, which is
 characterized by a long sequence insertion between the first two zinc
 coordinating residues.
XX
CC   -!- SIMILARITY: Contains # SCA7 domain.
XX
FT   From: PS51505
FT   DOMAIN     from     to       SCA7 #.
XX
Chop: Nter=0; Cter=0;
Size: 57-78;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: A1L209;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/11/04
//
AC   PRU00839;
DC   Domain;
TR   PROSITE; PS51506; CBL_PTB; 1; level=0
XX
Names: Cbl-type phosphotyrosine-binding (Cbl-PTB) domain
 Cbl N-terminal (Cbl-N) domain
 Tyrosine kinase binding (TKB) domain
Function: Cbl-PTB is composed of three interacting domains: a four-helix
 bundle (4H), an EF-hand calcium-binding domain, and a divergent  SH2 domain.
 The calcium-bound EF-hand wedges between the 4H and SH2 domains,  and roughly
 determines their relative orientation. The three domains together form an
 integrated phosphoprotein-recognition module.
XX
CC   -!- DOMAIN: The N-terminus is composed of the phosphotyrosine binding
CC       (PTB) domain, a short linker region and the RING-type zinc finger.
CC       The PTB domain, which is also called TKB (tyrosine kinase binding)
CC       domain, is composed of three different subdomains: a four-helix
CC       bundle (4H), a calcium-binding EF hand and a divergent SH2 domain
CC       (By similarity).
CC   -!- SIMILARITY: Contains # Cbl-PTB (Cbl-type phosphotyrosine-binding)
CC       domain.
XX
GO   GO:0005509; F:calcium ion binding
GO   GO:0007166; P:cell surface receptor linked signaling pathway
XX
KW   Calcium
KW   Metal-binding
XX
FT   From: PS51506
FT   DOMAIN     from     to       Cbl-PTB #.
FT   REGION     from    131       4H #.
FT   REGION      132    204       EF-hand-like #.
FT   REGION      205     to       SH2-like #.
FT   CA_BIND     183    194       # (Potential).
XX
Chop: Nter=0; Cter=0;
Size: 282-325;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q557E7;
Scope:
 Eukaryota
 Viruses; Murine leukemia virus
Comments: None;
XX
# Revision 1.2  2010/09/01
//
AC   PRU00840;
DC   Domain;
TR   PROSITE; PS51507; IRF_2; 1; level=0
XX
Names: IRF tryptophan pentad repeat DNA-binding domain
Function: The IRF tryptophan pentad repeat DNA-binding domain has an alpha/
 beta architecture comprising a cluster of three alpha-helices (alpha1-alpha3)
 flanked on one side by a mixed four-stranded beta-sheet (beta1-beta4). It
 forms a helix-turn-helix motif that binds to ISRE consensus sequences found
 in target promoters.
XX
CC   -!- SIMILARITY: Belongs to the IRF family.
CC   -!- SIMILARITY: Contains # IRF tryptophan pentad repeat DNA-binding
CC       domain.
XX
DR   PROSITE; PS00601; IRF_1; 1; trigger=no
XX
GO   GO:0006350; P:transcription
GO   GO:0061019; P:regulation of transcription
GO   GO:0005634; C:nucleus
GO   GO:0003677; F:DNA binding
XX
KW   DNA-binding
KW   Nucleus
KW   Transcription
KW   Transcription regulation
XX
FT   From: PS51507
FT   DNA_BIND      1    107       IRF tryptophan pentad repeat.
XX
Chop: Nter=0; Cter=0;
Size: 95-128;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O14896;
Scope:
 Eukaryota; Euteleostomi
Comments: None;
XX
# Revision 1.1  2010/11/08
//
AC   PRU00841;
DC   Domain;
TR   PROSITE; PS51508; CKK; 1; level=0
XX
Names: CKK domain
Function: The CKK domain binds microtubules.
XX
CC   -!- DOMAIN: The CKK domain binds microtubules (By similarity).
CC   -!- SIMILARITY: Belongs to the CAMSAP1 family.
CC   -!- SIMILARITY: Contains # CKK domain.
XX
GO   GO:0005874; C:microtubule
XX
KW   Microtubule
XX
FT   From: PS51508
FT   DOMAIN     from     to       CKK #.
XX
Chop: Nter=0; Cter=0;
Size: 124-145;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: A2AHC3;
Scope:
 Eukaryota; Metazoa
Comments: None;
XX
# Revision 1.1  2010/11/10
//
AC   PRU00842;
DC   Domain;
TR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1; level=0
XX
Names: Phosphagen kinase N-terminal domain
Function: The phosphagen kinase N-terminal domain is involved in dimer
 formation.
XX
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC   -!- SIMILARITY: Contains # phosphagen kinase N-terminal domain.
XX
FT   From: PS51509
FT   DOMAIN     from     to       Phosphagen kinase N-terminal #.
XX
Chop: Nter=0; Cter=0;
Size: 42-98;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: Q5R7B5;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.1  2010/12/16
//
AC   PRU00843;
DC   Domain;
TR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1; level=0
XX
Names: Phosphagen kinase C-terminal domain
Function: The phosphagen kinase C-terminal alpha/beta saddle domain contains
 many key residues involved in catalysis.
XX
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC   -!- SIMILARITY: Contains # phosphagen kinase C-terminal domain.
XX
GO   GO:0005524; F:ATP binding
XX
KW   ATP-binding
KW   Kinase
KW   Nucleotide-binding
KW   Transferase
XX
FT   From: PS51510
FT   DOMAIN     from     to       Phosphagen kinase C-terminal #.
FT   NP_BIND       4      8       ATP (By similarity).
FT   NP_BIND     157    161       ATP (By similarity).
FT   NP_BIND     188    193       ATP (By similarity).
FT   BINDING      67     67       ATP (By similarity).
FT   Condition: H
FT   BINDING     106    106       ATP (By similarity).
FT   Condition: R
XX
Chop: Nter=0; Cter=0;
Size: 6-254;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: A4IJG0;
Scope:
 Bacteria
 Eukaryota
Comments: None;
XX
# Revision 1.2  2010/12/16
//
AC   PRU00844;
DC   Domain;
TR   PROSITE; PS51511; FIP_RBD; 1; level=0
XX
Names: FIP-RBD domain
Function: A family of Rab11 interacting proteins (FIPs) that conserve a C-
 terminal Rab-binding domain (RBD) selectively recognize the active form of
 Rab11.
XX
CC   -!- SIMILARITY: Contains # FIP-RBD domain.
XX
GO   GO:0015031; P:protein transport
XX
KW   Membrane
KW   Transport
KW   Endosome
XX
FT   From: PS51511
FT   DOMAIN     from     to       FIP-RBD #.
XX
Chop: Nter=0; Cter=0;
Size: 53-73;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9D620;
Scope:
 Eukaryota; Euteleostomi
Comments: None;
XX
# Revision 1.1  2011/01/19
//
AC   PRU00854;
DC   Domain;
TR   PROSITE; PS51521; HTUSP; 1; level=0
XX
Names: Herpesvirus tegument ubiquitin-specific protease (htUSP) domain
Function: All herpesviruses contain a Ubiquitin (Ub)-specific cysteine
 protease (USP) domain embedded within their large tegument protein.
XX
CC   -!- SIMILARITY: Belongs to the herpesviridae large tegument protein
CC       family.
CC   -!- SIMILARITY: Contains # peptidase C76 domain.
XX
GO   GO:0019033; C:viral tegument
XX
KW   Virion
KW   Virion tegument
XX
FT   From: PS51521
FT   DOMAIN     from     to       Peptidase C76 #.
case <FTGroup:1>
FT   SITE          8      8       Important for catalytic activity (By
FT                                similarity).
FT   Condition: Q
end case
FT   ACT_SITE     21     21       By similarity.
FT   Group: 1; Condition: C
FT   ACT_SITE    156    156       By similarity.
FT   Group: 1; Condition: D
FT   ACT_SITE    158    158       By similarity.
FT   Group: 1; Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 203-236;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P52340;
Scope:
 Viruses; Herpesviridae
Comments: None;
XX
# Revision 1.2  2011/02/07
//
AC   PRU00855;
DC   Domain;
TR   PROSITE; PS51522; ZF_NANOS; 1; level=0
XX
Names: Zinc finger nanos-type
Function: The nanos-type zinc finger has two conserved Cys-Cys-His-Cys (CCHC)-
 type zinc-finger motifs that are indispensable for nanos function.
XX
case <Feature:PS51522:2=C> and <Feature:PS51522:5=C> and <Feature:PS51522:18=H> and <Feature:PS51522:29=C> and <Feature:PS51522:37=C> and <Feature:PS51522:40=C> and <Feature:PS51522:48=H> and <Feature:PS51522:53=C>
CC   -!- DOMAIN: The Nanos-type zinc finger is composed of two C2HC motifs,
CC       each motif binding one molecule of zinc. It is essential for the
CC       translation repression activity of the protein.
end case
CC   -!- SIMILARITY: Belongs to the nanos family.
CC   -!- SIMILARITY: Contains # nanos-type zinc finger.
XX
case (<Feature:PS51522:2=CH> and <Feature:PS51522:5=CH> and <Feature:PS51522:18=HC> and <Feature:PS51522:29=CH>) or (<Feature:PS51522:37=CH> and <Feature:PS51522:40=CH> and <Feature:PS51522:48=HC> and <Feature:PS51522:53=CH>)
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0006417; P:regulation of translation
GO   GO:0003723; F:RNA binding
XX
case (<Feature:PS51522:2=CH> and <Feature:PS51522:5=CH> and <Feature:PS51522:18=HC> and <Feature:PS51522:29=CH>) or (<Feature:PS51522:37=CH> and <Feature:PS51522:40=CH> and <Feature:PS51522:48=HC> and <Feature:PS51522:53=CH>)
KW   Metal-binding
end case
KW   RNA-binding
KW   Translation regulation
case (<Feature:PS51522:2=CH> and <Feature:PS51522:5=CH> and <Feature:PS51522:18=HC> and <Feature:PS51522:29=CH>) or (<Feature:PS51522:37=CH> and <Feature:PS51522:40=CH> and <Feature:PS51522:48=HC> and <Feature:PS51522:53=CH>)
KW   Zinc
end case
KW   Zinc-finger
XX
FT   From: PS51522
case <Feature:PS51522:2=C> and <Feature:PS51522:5=C> and <Feature:PS51522:18=H> and <Feature:PS51522:29=C> and <Feature:PS51522:37=C> and <Feature:PS51522:40=C> and <Feature:PS51522:48=H> and <Feature:PS51522:53=C>
FT   ZN_FING    from     to       Nanos-type #.
else case <Feature:PS51522:2=[CH]> and <Feature:PS51522:5=[CH]> and <Feature:PS51522:18=[HC]> and <Feature:PS51522:29=[CH]> and <Feature:PS51522:37=[CH]> and <Feature:PS51522:40=[CH]> and <Feature:PS51522:48=[HC]> and <Feature:PS51522:53=[CH]>
FT   ZN_FING    from     to       Nanos-type #; atypical.
else
FT   ZN_FING    from     to       Nanos-type #; degenerate.
end case
case <Feature:PS51522:2=C> and <Feature:PS51522:5=C> and <Feature:PS51522:18=H> and <Feature:PS51522:29=C>
FT   MOTIF         2     29       C2HC #1.
end case
case <Feature:PS51522:37=C> and <Feature:PS51522:40=C> and <Feature:PS51522:48=H> and <Feature:PS51522:53=C>
FT   MOTIF        37     53       C2HC #2.
end case
XX
Chop: Nter=0; Cter=0;
Size: 45-65;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P60323;
Scope:
 Eukaryota; Metazoa
Comments: None;
XX
# Revision 1.4  2011/02/04
//
AC   PRU01700;
DC   Domain;
TR   Metamotif; -; <PS50893=PS50893>
XX
Names: ABC transporter superfamily
 ATP binding cassette superfamily
Function: Uses the hydrolysis of ATP to energize diverse biological systems
XX
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
XX
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1; trigger=no
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1; trigger=yes
XX
GO   GO:0043190; C:ATP-binding cassette (ABC) transporter complex
GO   GO:0006810; P:transport
GO   GO:0005524; F:ATP binding
XX
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
KW   Membrane
end case
XX
Chop: Nter=0; Cter=0;
Size: 200-2438;
Related: None;
Repeats: 1-2;
case (<OC:Bacteria> or <OC:Archaea>) and defined <Property:Membrane> and <Property:Membrane=2>
Topology: Inner membrane associated;
else
Topology: Membrane associated;
end case
Example: P02915; P60752; P13569;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Plastid
 Bacteriophage
Comments: Contains ABC cassette but lost transport capability in UvrA subfamily.
XX
# Revision 1.17  2009/06/22
//
AC   PRU10001;
DC   Domain;
TR   PROSITE; PS00061; ADH_SHORT; 1; level=0
XX
Names: Short-chain dehydrogenases/reductases family
Function: Undefined
XX
DE   + AltName: Full=Alcohol dehydrogenase;
DE            EC=1.1.1.1;
XX
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
XX
FT   From: PS00061
FT   ACT_SITE      3      3       Proton acceptor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P48814;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10002;
DC   Domain;
TR   PROSITE; PS00064; L_LDH; 1; level=0
XX
Names: L-lactate dehydrogenase active site
Function: Undefined
XX
DE   + AltName: Full=L-lactate dehydrogenase;
DE            EC=1.1.1.27;
XX
CC   -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
XX
FT   From: PS00064
FT   ACT_SITE      4      4       Proton acceptor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9PW06;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10003;
DC   Domain;
TR   PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1; level=0
XX
Names: Hydroxymethylglutaryl-coenzyme A reductases
Function: Undefined
XX
DE   + AltName: Full=Hydroxymethylglutaryl-CoA reductase;
DE   AltName: Full=NADPH;
DE            EC=1.1.1.34;
XX
CC   -!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3-
CC       hydroxy-3-methylglutaryl-CoA + 2 NADPH.
XX
FT   From: PS01192
FT   ACT_SITE      7      7       Proton donor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P00347;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10004;
DC   Domain;
TR   PROSITE; PS00068; MDH; 1; level=0
XX
Names: Malate dehydrogenase active site
Function: Undefined
XX
DE   + AltName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
XX
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
XX
FT   From: PS00068
FT   ACT_SITE      5      5       Proton relay (By similarity).
FT   BINDING       6      6       Substrate (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5U907;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10005;
DC   Domain;
TR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1; level=0
XX
Names: Glucose-6-phosphate dehydrogenase active site
Function: Undefined
XX
DE   + AltName: Full=Glucose 1-dehydrogenase;
DE            EC=1.1.1.47;
XX
CC   -!- CATALYTIC ACTIVITY: Beta-D-glucose + NAD(P)(+) = D-glucono-1,5-
CC       lactone + NAD(P)H.
XX
FT   From: PS00069
FT   BINDING       6      6       Substrate (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q00612;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10007;
DC   Domain;
TR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1; level=0
XX
Names: Aldehyde dehydrogenases glutamic acid active site
Function: Undefined
XX
DE   + AltName: Full=Aldehyde dehydrogenase;
DE   AltName: Full=NAD(+);
DE            EC=1.2.1.3;
XX
CC   -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = an acid + NADH.
XX
FT   From: PS00687
FT   ACT_SITE      2      2       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9K9B2;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10008;
DC   Domain;
TR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1; level=0
XX
Names: Aldehyde dehydrogenases cysteine active site
Function: Undefined
XX
DE   + AltName: Full=Aldehyde dehydrogenase;
DE   AltName: Full=NAD(+);
DE            EC=1.2.1.3;
XX
CC   -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = an acid + NADH.
XX
FT   From: PS00070
FT   ACT_SITE      7      7       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9K9B2;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10009;
DC   Domain;
TR   PROSITE; PS00071; GAPDH; 1; level=0
XX
Names: Glyceraldehyde 3-phosphate dehydrogenase active site
Function: Undefined
XX
DE   + AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE   AltName: Full=phosphorylating;
DE            EC=1.2.1.12;
XX
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
XX
FT   From: PS00071
FT   ACT_SITE      3      3       Nucleophile (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P09124;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10010;
DC   Domain;
TR   PROSITE; PS01224; ARGC; 1; level=0
XX
Names: N-acetyl-gamma-glutamyl-phosphate reductase active site
Function: Undefined
XX
FT   From: PS01224
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P57156;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10011;
DC   Domain;
TR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1; level=0
XX
Names: Glu / Leu / Phe / Val dehydrogenases active site
Function: Undefined
XX
DE   + AltName: Full=Glutamate dehydrogenase;
DE   AltName: Full=NAD(P)(+);
DE            EC=1.4.1.3;
XX
CC   -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(P)(+) = 2-
CC       oxoglutarate + NH(3) + NAD(P)H.
XX
FT   From: PS00074
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q43314;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10012;
DC   Domain;
TR   PROSITE; PS00436; PEROXIDASE_2; 1; level=0
XX
Names: Peroxidases active site
Function: Undefined
XX
DE   + AltName: Full=NAD(P)H oxidase;
DE            EC=1.6.3.1;
XX
CC   -!- CATALYTIC ACTIVITY: NAD(P)H + O(2) = NAD(P)(+) + H(2)O(2).
XX
FT   From: PS00436
FT   ACT_SITE      7      7       Proton acceptor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P20010;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10013;
DC   Domain;
TR   PROSITE; PS00438; CATALASE_2; 1; level=0
XX
Names: Catalase proximal active site
Function: Undefined
XX
DE   + AltName: Full=Catalase;
DE            EC=1.11.1.6;
XX
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
XX
FT   From: PS00438
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q96528;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10014;
DC   Domain;
TR   PROSITE; PS00368; RIBORED_SMALL; 1; level=0
XX
Names: Ribonucleotide reductase small subunit
Function: Undefined
XX
DE   + AltName: Full=Ribonucleoside-diphosphate reductase;
DE            EC=1.17.4.1;
XX
CC   -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate +
CC       thioredoxin disulfide + H(2)O = ribonucleoside diphosphate +
CC       thioredoxin.
XX
FT   From: PS00368
FT   METAL         2      2       Iron 1 (By similarity).
FT   METAL         4      4       Iron 1 (By similarity).
FT   ACT_SITE      7      7       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P26713;
Scope:
 Eukaryota
 Bacteria
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10015;
DC   Domain;
TR   PROSITE; PS01230; TRMA_1; 1; level=0
XX
Names: RNA methyltransferase trmA family
Function: Undefined
XX
FT   From: PS01230
FT   ACT_SITE     10     10       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q97R12;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10016;
DC   Domain;
TR   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1; level=0
XX
Names: Thymidylate synthase active site
Function: Undefined
XX
FT   From: PS00091
FT   ACT_SITE      7      7       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P54081;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10017;
DC   Domain;
TR   PROSITE; PS00374; MGMT; 1; level=0
XX
Names: Methylated-DNA--protein-cysteine methyltransferase active site
Function: Undefined
XX
DE   + AltName: Full=Methylated-DNA--[protein]-cysteine S-methyltransferase;
DE            EC=2.1.1.63;
XX
CC   -!- CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein
CC       L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-
CC       cysteine.
XX
FT   From: PS00374
FT   ACT_SITE      3      3       Nucleophile; methyl group acceptor (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q4J9C6;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10018;
DC   Domain;
TR   PROSITE; PS00094; C5_MTASE_1; 1; level=0
XX
Names: C-5 cytosine-specific DNA methylases active site
Function: Undefined
XX
DE   + AltName: Full=DNA (cytosine-5-)-methyltransferase;
DE            EC=2.1.1.37;
XX
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
CC       homocysteine + DNA containing 5-methylcytosine.
XX
FT   From: PS00094
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P25262;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10019;
DC   Domain;
TR   PROSITE; PS00958; TRANSALDOLASE_2; 1; level=0
XX
Names: Transaldolase active site
Function: Undefined
XX
DE   + AltName: Full=Transaldolase;
DE            EC=2.2.1.2;
XX
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
XX
FT   From: PS00958
FT   ACT_SITE      3      3       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q57TP8;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10020;
DC   Domain;
TR   PROSITE; PS00099; THIOLASE_3; 1; level=0
XX
Names: Thiolases active site
Function: Undefined
XX
DE   + AltName: Full=Acetyl-CoA C-acetyltransferase;
DE            EC=2.3.1.9;
XX
CC   -!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
XX
FT   From: PS00099
FT   ACT_SITE      6      6       Proton acceptor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8X8J4;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10021;
DC   Domain;
TR   PROSITE; PS00100; CAT; 1; level=0
XX
Names: Chloramphenicol acetyltransferase active site
Function: Undefined
XX
DE   + AltName: Full=Chloramphenicol O-acetyltransferase;
DE            EC=2.3.1.28;
XX
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + chloramphenicol = CoA +
CC       chloramphenicol 3-acetate.
XX
FT   From: PS00100
FT   ACT_SITE      4      4       Proton acceptor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P00485;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10022;
DC   Domain;
TR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1; level=0
XX
Names: Beta-ketoacyl synthases active site
Function: Undefined
XX
DE   + AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I;
DE            EC=2.3.1.41;
XX
CC   -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
CC       carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) +
CC       [acyl-carrier-protein].
XX
FT   From: PS00606
FT   ACT_SITE      7      7       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0A954;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10023;
DC   Domain;
TR   PROSITE; PS00441; CHALCONE_SYNTH; 1; level=0
XX
Names: Chalcone and stilbene synthases active site
Function: Undefined
XX
DE   + AltName: Full=Naringenin-chalcone synthase;
DE            EC=2.3.1.74;
XX
CC   -!- CATALYTIC ACTIVITY: 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA +
CC       naringenin chalcone + 3 CO(2).
XX
FT   From: PS00441
FT   ACT_SITE      6      6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9FSC0;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10024;
DC   Domain;
TR   PROSITE; PS00547; TRANSGLUTAMINASES; 1; level=0
XX
Names: Transglutaminases active site
Function: Undefined
XX
DE   + AltName: Full=Protein-glutamine gamma-glutamyltransferase;
DE            EC=2.3.2.13;
XX
CC   -!- CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N(5)-
CC       alkylglutamine + NH(3).
XX
FT   From: PS00547
FT   ACT_SITE      3      3       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P51176;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.3  2009/02/27
//
AC   PRU10027;
DC   Domain;
TR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1; level=0
XX
Names: Serine/Threonine protein kinases active-site
Function: Undefined
XX
DE   + AltName: Full=Receptor protein-tyrosine kinase;
DE            EC=2.7.10.1;
XX
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
XX
FT   From: PS00108
FT   ACT_SITE      3      3       Proton acceptor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P00546;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10028;
DC   Domain;
TR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1; level=0
XX
Names: Tyrosine protein kinases specific active-site
Function: Undefined
XX
DE   + AltName: Full=Receptor protein-tyrosine kinase;
DE            EC=2.7.10.1;
XX
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
XX
FT   From: PS00109
FT   ACT_SITE      4      4       Proton acceptor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P15054;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10029;
DC   Domain;
TR   PROSITE; PS00112; GUANIDO_KINASE; 1; level=0
XX
Names: ATP:guanido phosphotransferases active site
Function: Undefined
XX
DE   + AltName: Full=Creatine kinase;
DE            EC=2.7.3.2;
XX
CC   -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
XX
FT   From: PS00112
FT   ACT_SITE      1      1       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q95V58;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10030;
DC   Domain;
TR   PROSITE; PS00469; NDP_KINASES; 1; level=0
XX
Names: Nucleoside diphosphate kinases active site
Function: Undefined
XX
DE   + AltName: Full=Nucleoside-diphosphate kinase;
DE            EC=2.7.4.6;
XX
CC   -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC       nucleoside triphosphate.
XX
FT   From: PS00469
FT   ACT_SITE      2      2       Pros-phosphohistidine intermediate (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P81766;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10031;
DC   Domain;
TR   PROSITE; PS00900; RNA_POL_PHAGE_1; 1; level=0
XX
Names: Bacteriophage-type RNA polymerase family active site
Function: Undefined
XX
DE   + AltName: Full=DNA-directed RNA polymerase;
DE            EC=2.7.7.6;
XX
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
XX
FT   From: PS00900
FT   ACT_SITE      3      3       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P69243;
Scope:
 Eukaryota
 Bacteriophage
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10032;
DC   Domain;
TR   PROSITE; PS00489; RNA_POL_PHAGE_2; 1; level=0
XX
Names: Bacteriophage-type RNA polymerase family active site
Function: Undefined
XX
DE   + AltName: Full=DNA-directed RNA polymerase;
DE            EC=2.7.7.6;
XX
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
XX
FT   From: PS00489
FT   ACT_SITE      3      3       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P69243;
Scope:
 Eukaryota
 Bacteriophage
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10033;
DC   Domain;
TR   PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1; level=0
XX
Names: Galactose-1-phosphate uridyl transferase family 1 active site
Function: Undefined
XX
DE   + AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase;
DE            EC=2.7.7.12;
XX
CC   -!- CATALYTIC ACTIVITY: UDP-glucose + alpha-D-galactose 1-phosphate =
CC       alpha-D-glucose 1-phosphate + UDP-galactose.
XX
FT   From: PS00117
FT   METAL         7      7       Zinc (Potential).
FT   ACT_SITE      9      9       Tele-UMP-histidine intermediate (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P31764;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10034;
DC   Domain;
TR   PROSITE; PS01274; COA_TRANSF_2; 1; level=0
XX
Names: Coenzyme A transferases
Function: Undefined
XX
DE   + AltName: Full=3-oxoacid CoA-transferase;
DE            EC=2.8.3.5;
XX
CC   -!- CATALYTIC ACTIVITY: Succinyl-CoA + a 3-oxo acid = succinate + a 3-
CC       oxoacyl-CoA.
XX
FT   From: PS01274
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q59091;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10035;
DC   Domain;
TR   PROSITE; PS00118; PA2_HIS; 1; level=0
XX
Names: Phospholipase A2 histidine active site
Function: Undefined
XX
DE   + AltName: Full=Phospholipase A(2);
DE            EC=3.1.1.4;
XX
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
XX
FT   From: PS00118
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P45881;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10036;
DC   Domain;
TR   PROSITE; PS00119; PA2_ASP; 1; level=0
XX
Names: Phospholipase A2 aspartic acid active site
Function: Undefined
XX
DE   + AltName: Full=Phospholipase A(2);
DE            EC=3.1.1.4;
XX
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
XX
FT   From: PS00119
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P45881;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10037;
DC   Domain;
TR   PROSITE; PS00120; LIPASE_SER; 1; level=0
XX
Names: Lipases, serine active site
Function: Undefined
XX
DE   + AltName: Full=Phosphatidylcholine--sterol O-acyltransferase;
DE            EC=2.3.1.43;
XX
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + a sterol = 1-
CC       acylglycerophosphocholine + a sterol ester.
XX
FT   From: PS00120
FT   ACT_SITE      7      7       Charge relay system (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8VBX1;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10038;
DC   Domain;
TR   PROSITE; PS01174; LIPASE_GDXG_SER; 1; level=0
XX
Names: Lipolytic enzymes "G-D-X-G" family, putative serine active site
Function: Undefined
XX
DE   + AltName: Full=Hormone-sensitive lipase;
DE            EC=3.1.1.79;
XX
CC   -!- CATALYTIC ACTIVITY: (1) Diacylglycerol + H(2)O = monoacylglycerol
CC       + a carboxylate. (2) Triacylglycerol + H(2)O = diacylglycerol + a
CC       carboxylate. (3) Monoacylglycerol + H(2)O = glycerol + a
CC       carboxylate.
XX
FT   From: PS01174
FT   ACT_SITE      6      6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q99PG0;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10039;
DC   Domain;
TR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1; level=0
XX
Names: Carboxylesterases type-B serine active site
Function: Undefined
XX
DE   + AltName: Full=Carboxylesterase;
DE            EC=3.1.1.1;
XX
CC   -!- CATALYTIC ACTIVITY: A carboxylic ester + H(2)O = an alcohol + a
CC       carboxylate.
XX
FT   From: PS00122
FT   ACT_SITE      7      7       Acyl-ester intermediate (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8VCT4;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10040;
DC   Domain;
TR   PROSITE; PS00503; PECTINESTERASE_2; 1; level=0
XX
Names: Pectinesterase
Function: Undefined
XX
FT   From: PS00503
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O04886;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10041;
DC   Domain;
TR   PROSITE; PS01328; 4HBCOA_THIOESTERASE; 1; level=0
XX
Names: 4-hydroxybenzoyl-CoA thioesterase family active site
Function: Undefined
XX
DE   + AltName: Full=4-hydroxybenzoyl-CoA thioesterase;
DE            EC=3.1.2.23;
XX
CC   -!- CATALYTIC ACTIVITY: 4-hydroxybenzoyl-CoA + H(2)O = 4-
CC       hydroxybenzoate + CoA.
XX
FT   From: PS01328
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P44679;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10042;
DC   Domain;
TR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1; level=0
XX
Names: Alkaline phosphatase active site
Function: Undefined
XX
DE   + AltName: Full=Alkaline phosphatase;
DE            EC=3.1.3.1;
XX
CC   -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
CC       phosphate.
XX
FT   From: PS00123
FT   ACT_SITE      3      3       Phosphoserine intermediate (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P35483;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10043;
DC   Domain;
TR   PROSITE; PS00124; FBPASE; 1; level=0
XX
Names: Fructose-1-6-bisphosphatase active site
Function: Undefined
XX
DE   + AltName: Full=Fructose-bisphosphatase;
DE            EC=3.1.3.11;
XX
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate.
XX
FT   From: PS00124
FT   ACT_SITE      2      2       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9MA79;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10044;
DC   Domain;
TR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1; level=0
XX
Names: Tyrosine specific protein phosphatases active site
Function: Undefined
XX
DE   + AltName: Full=Protein-tyrosine-phosphatase;
DE            EC=3.1.3.48;
XX
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
XX
FT   From: PS00383
FT   ACT_SITE      3      3       Phosphocysteine intermediate (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5BIP9;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10045;
DC   Domain;
TR   PROSITE; PS00530; RNASE_T2_1; 1; level=0
XX
Names: Ribonuclease T2 family histidine active site 1
Function: Undefined
XX
DE   + AltName: Full=Ribonuclease T(2);
DE            EC=3.1.27.1;
XX
CC   -!- CATALYTIC ACTIVITY: Two-stage endonucleolytic cleavage to
CC       nucleoside 3'-phosphates and 3'-phosphooligonucleotides with
CC       2',3'-cyclic phosphate intermediates.
XX
FT   From: PS00530
FT   ACT_SITE      3      3       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O80322;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10046;
DC   Domain;
TR   PROSITE; PS00531; RNASE_T2_2; 1; level=0
XX
Names: Ribonuclease T2 family histidine active site 2
Function: Undefined
XX
DE   + AltName: Full=Ribonuclease T(2);
DE            EC=3.1.27.1;
XX
CC   -!- CATALYTIC ACTIVITY: Two-stage endonucleolytic cleavage to
CC       nucleoside 3'-phosphates and 3'-phosphooligonucleotides with
CC       2',3'-cyclic phosphate intermediates.
XX
FT   From: PS00531
FT   ACT_SITE      6      6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P81296;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10047;
DC   Domain;
TR   PROSITE; PS01070; NUCLEASE_NON_SPEC; 1; level=0
XX
Names: DNA/RNA non-specific endonucleases active site
Function: Undefined
XX
DE   + AltName: Full=Serratia marcescens nuclease;
DE            EC=3.1.30.2;
XX
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomononucleotide and 5'-phosphooligonucleotide end-products.
XX
FT   From: PS01070
FT   ACT_SITE      4      4       Proton acceptor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P08466;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10048;
DC   Domain;
TR   PROSITE; PS01123; TNASE_1; 1; level=0
XX
Names: Thermonuclease family
Function: Undefined
XX
DE   + AltName: Full=Micrococcal nuclease;
DE            EC=3.1.31.1;
XX
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to nucleoside 3'-
CC       phosphates and 3'-phosphooligonucleotide end-products.
XX
FT   From: PS01123
FT   ACT_SITE      7      7       By similarity.
FT   ACT_SITE     12     12       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5HHM4;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10049;
DC   Domain;
TR   PROSITE; PS01284; TNASE_2; 1; level=0
XX
Names: Thermonuclease family
Function: Undefined
XX
DE   + AltName: Full=Micrococcal nuclease;
DE            EC=3.1.31.1;
XX
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to nucleoside 3'-
CC       phosphates and 3'-phosphooligonucleotide end-products.
XX
FT   From: PS01284
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5HHM4;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10050;
DC   Domain;
TR   PROSITE; PS00679; BETA_AMYLASE_2; 1; level=0
XX
Names: Beta-amylase active site 2
Function: Undefined
XX
DE   + AltName: Full=Beta-amylase;
DE            EC=3.2.1.2;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of 1,4-alpha-D-glucosidic linkages
CC       in polysaccharides so as to remove successive maltose units from
CC       the non-reducing ends of the chains.
XX
FT   From: PS00679
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P16098;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10051;
DC   Domain;
TR   PROSITE; PS00820; GLUCOAMYLASE; 1; level=0
XX
Names: Glucoamylase active site region
Function: Undefined
XX
DE   + AltName: Full=Glucan 1,4-alpha-glucosidase;
DE            EC=3.2.1.3;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal 1,4-linked alpha-D-
CC       glucose residues successively from non-reducing ends of the chains
CC       with release of beta-D-glucose.
XX
FT   From: PS00820
FT   ACT_SITE      3      3       Proton acceptor (By similarity).
FT   ACT_SITE      5      5       Proton donor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P23176;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10052;
DC   Domain;
TR   PROSITE; PS00502; POLYGALACTURONASE; 1; level=0
XX
Names: Polygalacturonase active site
Function: Undefined
XX
FT   From: PS00502
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q00446;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10053;
DC   Domain;
TR   PROSITE; PS01095; CHITINASE_18; 1; level=0
XX
Names: Chitinases family 18 active site
Function: Undefined
XX
DE   + AltName: Full=Chitinase;
DE            EC=3.2.1.14;
XX
CC   -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-
CC       glucosaminide 1,4-beta-linkages in chitin and chitodextrins.
XX
FT   From: PS01095
FT   ACT_SITE      8      8       Proton donor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q95M17;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10054;
DC   Domain;
TR   PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1; level=0
XX
Names: Alpha-L-fucosidase putative active site
Function: Undefined
XX
DE   + AltName: Full=Alpha-L-fucosidase;
DE            EC=3.2.1.51;
XX
CC   -!- CATALYTIC ACTIVITY: An alpha-L-fucoside + H(2)O = L-fucose + an
CC       alcohol.
XX
FT   From: PS00385
FT   SITE          6      6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P49713;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10055;
DC   Domain;
TR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1; level=0
XX
Names: Glycosyl hydrolases family 1 active site
Function: Undefined
XX
DE   + AltName: Full=Beta-glucosidase;
DE            EC=3.2.1.21;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-
CC       glucose residues with release of beta-D-glucose.
XX
FT   From: PS00572
FT   ACT_SITE      5      5       Nucleophile (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P50977;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10056;
DC   Domain;
TR   PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1; level=0
XX
Names: Glycosyl hydrolases family 6
Function: Undefined
XX
DE   + AltName: Full=Cellulase;
DE            EC=3.2.1.4;
XX
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
XX
FT   From: PS00655
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P26414;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10057;
DC   Domain;
TR   PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1; level=0
XX
Names: Glycosyl hydrolases family 6
Function: Undefined
XX
DE   + AltName: Full=Cellulase;
DE            EC=3.2.1.4;
XX
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
XX
FT   From: PS00656
FT   ACT_SITE      7      7       Proton donor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P33682;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10058;
DC   Domain;
TR   PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1; level=0
XX
Names: Glycosyl hydrolases family 8
Function: Undefined
XX
DE   + AltName: Full=Cellulase;
DE            EC=3.2.1.4;
XX
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
XX
FT   From: PS00812
FT   ACT_SITE      3      3       Nucleophile (Potential).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P27032;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10059;
DC   Domain;
TR   PROSITE; PS00592; GLYCOSYL_HYDROL_F9_1; 1; level=0
XX
Names: Glycosyl hydrolases family 9 active sites
Function: Undefined
XX
DE   + AltName: Full=Cellulase;
DE            EC=3.2.1.4;
XX
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
XX
FT   From: PS00592
FT   ACT_SITE      7      7       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P28622;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10060;
DC   Domain;
TR   PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1; level=0
XX
Names: Glycosyl hydrolases family 9 active sites
Function: Undefined
XX
DE   + AltName: Full=Cellulase;
DE            EC=3.2.1.4;
XX
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
XX
FT   From: PS00698
FT   ACT_SITE      2      2       By similarity.
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P28622;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10061;
DC   Domain;
TR   PROSITE; PS00591; GLYCOSYL_HYDROL_F10; 1; level=0
XX
Names: Glycosyl hydrolases family 10 active site
Function: Undefined
XX
FT   From: PS00591
FT   ACT_SITE      7      7       Nucleophile (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O60206;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10062;
DC   Domain;
TR   PROSITE; PS00776; GLYCOSYL_HYDROL_F11_1; 1; level=0
XX
Names: Glycosyl hydrolases family 11 active site
Function: Undefined
XX
DE   + AltName: Full=Endo-1,4-beta-xylanase;
DE            EC=3.2.1.8;
XX
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-xylosidic
CC       linkages in xylans.
XX
FT   From: PS00776
FT   ACT_SITE      3      3       Nucleophile (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P55334;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10063;
DC   Domain;
TR   PROSITE; PS00777; GLYCOSYL_HYDROL_F11_2; 1; level=0
XX
Names: Glycosyl hydrolases family 11 active site
Function: Undefined
XX
DE   + AltName: Full=Endo-1,4-beta-xylanase;
DE            EC=3.2.1.8;
XX
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-xylosidic
CC       linkages in xylans.
XX
FT   From: PS00777
FT   ACT_SITE      2      2       Proton donor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P55334;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10064;
DC   Domain;
TR   PROSITE; PS01034; GLYCOSYL_HYDROL_F16; 1; level=0
XX
Names: Glycosyl hydrolases family 16 active sites
Function: Undefined
XX
DE   + AltName: Full=Endo-1,3(4)-beta-glucanase;
DE            EC=3.2.1.6;
XX
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,3- or 1,4-linkages in
CC       beta-D-glucans when the glucose residue whose reducing group is
CC       involved in the linkage to be hydrolyzed is itself substituted at
CC       C-3.
XX
FT   From: PS01034
FT   ACT_SITE      1      1       Nucleophile (By similarity).
FT   ACT_SITE      5      5       Proton donor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P07883;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10065;
DC   Domain;
TR   PROSITE; PS00953; GLYCOSYL_HYDROL_F25; 1; level=0
XX
Names: Glycosyl hydrolases family 25 active sites
Function: Undefined
XX
DE   + AltName: Full=Lysozyme;
DE            EC=3.2.1.17;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of 1,4-beta-linkages between N-
CC       acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC       peptidoglycan and between N-acetyl- D-glucosamine residues in
CC       chitodextrins.
XX
FT   From: PS00953
FT   ACT_SITE      1      1       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P19385;
Scope:
 Eukaryota
 Bacteria
 Bacteriophage
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10066;
DC   Domain;
TR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1; level=0
XX
Names: Glycosyl hydrolases family 31 active site
Function: Undefined
XX
DE   + AltName: Full=Glucan 1,4-alpha-glucosidase;
DE            EC=3.2.1.3;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal 1,4-linked alpha-D-
CC       glucose residues successively from non-reducing ends of the chains
CC       with release of beta-D-glucose.
XX
FT   From: PS00129
FT   ACT_SITE      4      4       Nucleophile (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9BE70;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10067;
DC   Domain;
TR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1; level=0
XX
Names: Glycosyl hydrolases family 32 active site
Function: Undefined
XX
DE   + AltName: Full=Beta-fructofuranosidase;
DE            EC=3.2.1.26;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       fructofuranoside residues in beta-D-fructofuranosides.
XX
FT   From: PS00609
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P10594;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10068;
DC   Domain;
TR   PROSITE; PS01027; GLYCOSYL_HYDROL_F39; 1; level=0
XX
Names: Glycosyl hydrolases family 39 active site
Function: Undefined
XX
DE   + AltName: Full=Xylan 1,4-beta-xylosidase;
DE            EC=3.2.1.37;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of 1,4-beta-D-xylans, to remove
CC       successive D-xylose residues from the non-reducing termini.
XX
FT   From: PS01027
FT   ACT_SITE      6      6       Proton donor (Potential).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9ZFM2;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10069;
DC   Domain;
TR   PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1; level=0
XX
Names: Glycosyl hydrolases family 45 active site
Function: Undefined
XX
DE   + AltName: Full=Cellulase;
DE            EC=3.2.1.4;
XX
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
XX
FT   From: PS01140
FT   ACT_SITE      6      6       Nucleophile (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P43317;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10070;
DC   Domain;
TR   PROSITE; PS60000; CHITOSANASE_46_80; 1; level=0
XX
Names: Chitosanases families 46 and 80 active sites
Function: Undefined
XX
DE   + AltName: Full=Chitosanase;
DE            EC=3.2.1.132;
XX
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of beta-1,4-linkages between D-
CC       glucosamine residues in a partly acetylated chitosan.
XX
FT   From: PS60000
FT   ACT_SITE      1      1       Proton donor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P48846;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10071;
DC   Domain;
TR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1; level=0
XX
Names: Prokaryotic transglycosylases
Function: Undefined
XX
FT   From: PS00922
FT   ACT_SITE      2      2       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0AEZ8;
Scope:
 Bacteria
 Bacteriophage
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10072;
DC   Domain;
TR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1; level=0
XX
Names: Uracil-DNA glycosylase
Function: Undefined
XX
FT   From: PS00130
FT   ACT_SITE      7      7       Proton acceptor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5LA67;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10073;
DC   Domain;
TR   PROSITE; PS00869; RENAL_DIPEPTIDASE_1; 1; level=0
TR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1; level=0
XX
Names: Renal dipeptidase family
 microsomal dipeptidase
 membrane dipeptidase
Function: Renal  dipeptidase (rDP) (EC 3.4.13.19) and related enzymes are
 zinc-dependent metalloenzymes which hydrolyze a wide range of dipeptides.
XX
case <FTGroup:1> or <FTGroup:2> or not <AnyFeature:PS51365>
DE   + AltName: Full=dipeptidase;
DE            EC=3.4.13.19;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of dipeptides.
CC   -!- COFACTOR: Zinc (By similarity).
end case
case <Feature:PS51365:365=C> and <FTGroup:3> and <FTGroup:4>
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity).
end case
CC   -!- SIMILARITY: Belongs to the peptidase M19 family.
XX
case <FTGroup:1> or <FTGroup:2>
GO   GO:0016805; F:dipeptidase activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0046872; F:metal ion binding
GO   GO:0008237; F:metallopeptidase activity
GO   GO:0008233; F:peptidase activity
GO   GO:0008270; F:zinc ion binding
XX
KW   Dipeptidase
KW   Hydrolase
KW   Metal-binding
KW   Metalloprotease
KW   Protease
KW   Zinc
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51365
FT   METAL        20     20       Zinc #1; catalytic (By similarity).
FT   Group: 1; Condition: H
FT   METAL        22     22       Zinc #1; catalytic (By similarity).
FT   Group: 1; Condition: D
FT   METAL       125    125       Zinc #1; catalytic (By similarity).
FT   Group: 1; Condition: E
FT   METAL       125    125       Zinc #2; catalytic (By similarity).
FT   Group: 2; Condition: E
FT   METAL       198    198       Zinc #2; catalytic (By similarity).
FT   Group: 2; Condition: Y
FT   METAL       219    219       Zinc #2; catalytic (By similarity).
FT   Group: 2; Condition: H
FT   BINDING     152    152       Substrate (By similarity).
FT   Condition: H
FT   BINDING     230    230       Substrate (By similarity).
FT   Condition: R
FT   BINDING     290    290       Substrate (By similarity).
FT   Condition: D
FT   DISULFID     71    154       By similarity.
FT   Tag: disulf; Group: 3; Condition: C-x*-C
FT   DISULFID    226    258       By similarity.
FT   Tag: disulf; Group: 4; Condition: C-x*-C
FT   DISULFID    365    365       Interchain (By similarity).
FT   Tag: disulf; Condition: C-x*-C
FT   From: PS00869
case not <AnyFeature:PS51365>
FT   METAL         2      2       Zinc #1; catalytic (By similarity).
end case
XX
Chop: Nter=0; Cter=1;
Size: 260-380;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q3SZM7;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.5  2009/02/27
//
AC   PRU10074;
DC   Domain;
TR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1; level=0
XX
Names: Serine carboxypeptidases, serine active site
Function: Undefined
XX
DE   + AltName: Full=Carboxypeptidase C;
DE            EC=3.4.16.5;
XX
CC   -!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with broad
CC       specificity.
XX
FT   From: PS00131
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9HB40;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10075;
DC   Domain;
TR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1; level=0
XX
Names: Serine carboxypeptidases, histidine active site
Function: Undefined
XX
DE   + AltName: Full=Carboxypeptidase C;
DE            EC=3.4.16.5;
XX
CC   -!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with broad
CC       specificity.
XX
FT   From: PS00560
FT   ACT_SITE      7      7       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P37891;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10076;
DC   Domain;
TR   PROSITE; PS01333; PYRASE_GLU; 1; level=0
XX
Names: Pyrrolidone-carboxylate peptidase glutamic acid active site
Function: Undefined
XX
DE   + AltName: Full=Pyroglutamyl-peptidase I;
DE            EC=3.4.19.3;
XX
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal pyroglutamyl group
CC       from a polypeptide, the second amino acid generally not being Pro.
XX
FT   From: PS01333
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P65678;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10077;
DC   Domain;
TR   PROSITE; PS01334; PYRASE_CYS; 1; level=0
XX
Names: Pyrrolidone-carboxylate peptidase cysteine active site
Function: Undefined
XX
DE   + AltName: Full=Pyroglutamyl-peptidase I;
DE            EC=3.4.19.3;
XX
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal pyroglutamyl group
CC       from a polypeptide, the second amino acid generally not being Pro.
XX
FT   From: PS01334
FT   ACT_SITE     10     10       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P65678;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10078;
DC   Domain;
TR   PROSITE; PS00134; TRYPSIN_HIS; 1; level=0
XX
Names: Serine proteases, trypsin family, histidine active site
Function: Undefined
XX
DE   + AltName: Full=Chymotrypsin;
DE            EC=3.4.21.1;
XX
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa,
CC       Phe-|-Xaa, Leu-|-Xaa.
XX
FT   From: PS00134
FT   ACT_SITE      5      5       Charge relay system (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P09582;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10079;
DC   Domain;
TR   PROSITE; PS00135; TRYPSIN_SER; 1; level=0
XX
Names: Serine proteases, trypsin family, serine active site
Function: Undefined
XX
DE   + AltName: Full=Chymotrypsin;
DE            EC=3.4.21.1;
XX
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa,
CC       Phe-|-Xaa, Leu-|-Xaa.
XX
FT   From: PS00135
FT   ACT_SITE      5      5       Charge relay system (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P04187;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10080;
DC   Domain;
TR   PROSITE; PS00136; SUBTILASE_ASP; 1; level=0
XX
Names: Serine proteases, subtilase family, aspartic acid active site
Function: Undefined
XX
DE   + AltName: Full=Tripeptidyl-peptidase II;
DE            EC=3.4.14.10;
XX
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal tripeptide from a
CC       polypeptide.
XX
FT   From: PS00136
FT   ACT_SITE      5      5       Charge relay system (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P29120;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10081;
DC   Domain;
TR   PROSITE; PS00137; SUBTILASE_HIS; 1; level=0
XX
Names: Serine proteases, subtilase family, histidine active site
Function: Undefined
XX
DE   + AltName: Full=Tripeptidyl-peptidase II;
DE            EC=3.4.14.10;
XX
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal tripeptide from a
CC       polypeptide.
XX
FT   From: PS00137
FT   ACT_SITE      1      1       Charge relay system (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P58099;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10082;
DC   Domain;
TR   PROSITE; PS00138; SUBTILASE_SER; 1; level=0
XX
Names: Serine proteases, subtilase family, serine active site
Function: Undefined
XX
DE   + AltName: Full=Tripeptidyl-peptidase II;
DE            EC=3.4.14.10;
XX
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal tripeptide from a
CC       polypeptide.
XX
FT   From: PS00138
FT   ACT_SITE      3      3       Charge relay system (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P08594;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10083;
DC   Domain;
TR   PROSITE; PS00673; V8_SER; 1; level=0
XX
Names: Serine proteases, V8 family, serine active site
Function: Undefined
XX
DE   + AltName: Full=Glutamyl endopeptidase;
DE            EC=3.4.21.19;
XX
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
XX
FT   From: PS00673
FT   ACT_SITE      4      4       Charge relay system (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5HH35;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10084;
DC   Domain;
TR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1; level=0
XX
Names: Prolyl endopeptidase family serine active site
Function: Undefined
XX
DE   + AltName: Full=Dipeptidyl-peptidase IV;
DE            EC=3.4.14.5;
XX
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide, Xaa-Yaa-|-
CC       Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided
CC       Zaa is neither Pro nor hydroxyproline.
XX
FT   From: PS00708
FT   ACT_SITE      5      5       Charge relay system (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9XTA2;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10085;
DC   Domain;
TR   PROSITE; PS00381; CLP_PROTEASE_SER; 1; level=0
XX
Names: Endopeptidase Clp serine active site
Function: Undefined
XX
DE   + AltName: Full=Endopeptidase Clp;
DE            EC=3.4.21.92;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in
CC       the presence of ATP and magnesium. Alpha-casein is the usual test
CC       substrate. In the absence of ATP, only oligopeptides shorter than
CC       five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec;
CC       and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu-
CC       and -Tyr-|-Trp bonds also occurs).
XX
FT   From: PS00381
FT   ACT_SITE      6      6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9K709;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10086;
DC   Domain;
TR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1; level=0
XX
Names: Endopeptidase Clp histidine active site
Function: Undefined
XX
DE   + AltName: Full=Endopeptidase Clp;
DE            EC=3.4.21.92;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in
CC       the presence of ATP and magnesium. Alpha-casein is the usual test
CC       substrate. In the absence of ATP, only oligopeptides shorter than
CC       five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec;
CC       and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu-
CC       and -Tyr-|-Trp bonds also occurs).
XX
FT   From: PS00382
FT   ACT_SITE      6      6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q81PL4;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10087;
DC   Domain;
TR   PROSITE; PS01046; LON_SER; 1; level=0
XX
Names: ATP-dependent serine proteases, lon family, serine active site
Function: Undefined
XX
DE   + AltName: Full=Endopeptidase La;
DE            EC=3.4.21.53;
XX
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP.
XX
FT   From: PS01046
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P57549;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10088;
DC   Domain;
TR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1; level=0
XX
Names: Eukaryotic thiol (cysteine) proteases cysteine active site
Function: Undefined
XX
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
XX
GO   GO:0004197; F:cysteine-type endopeptidase activity
GO   GO:0006508; P:proteolysis
XX
KW   Hydrolase
KW   Protease
KW   Thiol protease
XX
FT   From: PS00139
FT   ACT_SITE      6      6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P00786;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.3  2009/04/06
//
AC   PRU10089;
DC   Domain;
TR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1; level=0
XX
Names: Eukaryotic thiol (cysteine) proteases histidine active site
Function: Undefined
XX
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
XX
GO   GO:0004197; F:cysteine-type endopeptidase activity
GO   GO:0006508; P:proteolysis
XX
KW   Hydrolase
KW   Protease
KW   Thiol protease
XX
FT   From: PS00639
FT   ACT_SITE      3      3       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9R014;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.3  2009/04/06
//
AC   PRU10090;
DC   Domain;
TR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1; level=0
XX
Names: Eukaryotic thiol (cysteine) proteases asparagine active site
Function: Undefined
XX
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
XX
GO   GO:0004197; F:cysteine-type endopeptidase activity
GO   GO:0006508; P:proteolysis
XX
KW   Hydrolase
KW   Protease
KW   Thiol protease
XX
FT   From: PS00640
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O97397;
Scope:
 Eukaryota
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.3  2009/04/06
//
AC   PRU10091;
DC   Domain;
TR   PROSITE; PS00140; UCH_1; 1; level=0
XX
Names: Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site
Function: Undefined
XX
DE   + AltName: Full=Ubiquitin thiolesterase;
DE            EC=3.1.2.15;
XX
CC   -!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H(2)O =
CC       ubiquitin + a thiol.
XX
FT   From: PS00140
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9GM50;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10092;
DC   Domain;
TR   PROSITE; PS00972; UCH_2_1; 1; level=0
XX
Names: Ubiquitin carboxyl-terminal hydrolases family 2
Function: Undefined
XX
DE   + AltName: Full=Ubiquitin thiolesterase;
DE            EC=3.1.2.15;
XX
CC   -!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H(2)O =
CC       ubiquitin + a thiol.
XX
FT   From: PS00972
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P54578;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10093;
DC   Domain;
TR   PROSITE; PS00973; UCH_2_2; 1; level=0
XX
Names: Ubiquitin carboxyl-terminal hydrolases family 2
Function: Undefined
XX
DE   + AltName: Full=Ubiquitin thiolesterase;
DE            EC=3.1.2.15;
XX
CC   -!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H(2)O =
CC       ubiquitin + a thiol.
XX
FT   From: PS00973
FT   ACT_SITE      5      5       By similarity.
FT   ACT_SITE      8      8       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9UUD6;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10094;
DC   Domain;
TR   PROSITE; PS00141; ASP_PROTEASE; 1; level=0
XX
Names: Eukaryotic and viral aspartyl proteases active site
Function: Undefined
XX
DE   + AltName: Full=Pepsin A;
DE            EC=3.4.23.1;
XX
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: hydrophobic, preferably
CC       aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2,
CC       4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16,
CC       16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-
CC       Tyr-26 bonds in the B chain of insulin.
XX
FT   From: PS00141
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P56817;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10095;
DC   Domain;
TR   PROSITE; PS00142; ZINC_PROTEASE; 1; level=0
XX
Names: Neutral zinc metallopeptidases, zinc-binding region
Function: Undefined
XX
FT   From: PS00142
FT   METAL         4      4       Zinc; catalytic (By similarity).
FT   ACT_SITE      5      5       By similarity.
FT   METAL         8      8       Zinc; catalytic (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q56H28;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.4  2009/05/07
//
AC   PRU10096;
DC   Domain;
TR   PROSITE; PS00143; INSULINASE; 1; level=0
XX
Names: Insulinase family, zinc-binding region
Function: Undefined
XX
DE   + AltName: Full=Pitrilysin;
DE            EC=3.4.24.55;
XX
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage of 16-Tyr-|-Leu-17 and
CC       25-Phe-|-Tyr-26 bonds of oxidized insulin B chain. Also acts on
CC       other substrates of Mw less than 7 kDa such as insulin and
CC       glucagon.
XX
FT   From: PS00143
FT   METAL         4      4       Zinc (By similarity).
FT   ACT_SITE      7      7       Proton acceptor (By similarity).
FT   METAL         8      8       Zinc (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P27508;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10097;
DC   Domain;
TR   Metamotif; -; PS00501=(PS00760){,1}=PS00761
XX
Names: Signal peptidases I serine active sites
Function: Signal peptidases (SPases) (also known as leader peptidases) remove
 the signal peptides from secretory proteins.
XX
DE   + AltName: Full=Signal peptidase I;
DE            EC=3.4.21.89;
XX
CC   -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or
CC       leader sequences from secreted and periplasmic proteins.
XX
DR   PROSITE; PS00501; SPASE_I_1; 1; trigger=no
DR   PROSITE; PS00760; SPASE_I_2; 0-1; trigger=no
DR   PROSITE; PS00761; SPASE_I_3; 1; trigger=no
XX
GO   GO:0016787; F:hydrolase activity
GO   GO:0008233; F:peptidase activity
XX
KW   Hydrolase
KW   Protease
XX
FT   From: PS00501
FT   ACT_SITE      3      3       By similarity.
XX
FT   From: PS00760
FT   ACT_SITE      1      1       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5HHB9;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.6  2009/02/27
//
AC   PRU10099;
DC   Domain;
TR   PROSITE; PS00144; ASN_GLN_ASE_1; 1; level=0
XX
Names: Asparaginase / glutaminase active site
Function: Undefined
XX
DE   + AltName: Full=Glutamin-(asparagin-)ase;
DE            EC=3.5.1.38;
XX
CC   -!- CATALYTIC ACTIVITY: (1) L-glutamine + H(2)O = L-glutamate + NH(3).
CC       (2) L-asparagine + H(2)O = L-aspartate + NH(3).
XX
FT   From: PS00144
FT   ACT_SITE      6      6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P26900;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10100;
DC   Domain;
TR   PROSITE; PS00917; ASN_GLN_ASE_2; 1; level=0
XX
Names: Asparaginase / glutaminase active site
Function: Undefined
XX
DE   + AltName: Full=Glutamin-(asparagin-)ase;
DE            EC=3.5.1.38;
XX
CC   -!- CATALYTIC ACTIVITY: (1) L-glutamine + H(2)O = L-glutamate + NH(3).
CC       (2) L-asparagine + H(2)O = L-aspartate + NH(3).
XX
FT   From: PS00917
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9V0T9;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10101;
DC   Domain;
TR   PROSITE; PS00146; BETA_LACTAMASE_A; 1; level=0
XX
Names: Beta-lactamase class-A active site
Function: Undefined
XX
DE   + AltName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
XX
CC   -!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
CC       amino acid.
XX
FT   From: PS00146
FT   ACT_SITE      4      4       Acyl-ester intermediate (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9S424;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10102;
DC   Domain;
TR   PROSITE; PS00336; BETA_LACTAMASE_C; 1; level=0
XX
Names: Beta-lactamase class-C active site
Function: Undefined
XX
DE   + AltName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
XX
CC   -!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
CC       amino acid.
XX
FT   From: PS00336
FT   ACT_SITE      5      5       Acyl-ester intermediate (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P18539;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10103;
DC   Domain;
TR   PROSITE; PS00337; BETA_LACTAMASE_D; 1; level=0
XX
Names: Beta-lactamase class-D active site
Function: Undefined
XX
DE   + AltName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
XX
CC   -!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
CC       amino acid.
XX
FT   From: PS00337
FT   ACT_SITE      2      2       Acyl-ester intermediate (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P0A1V9;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10104;
DC   Domain;
TR   PROSITE; PS00485; A_DEAMINASE; 1; level=0
XX
Names: Adenosine and AMP deaminase
Function: Undefined
XX
DE   + AltName: Full=Adenosine deaminase;
DE            EC=3.5.4.4;
XX
CC   -!- CATALYTIC ACTIVITY: Adenosine + H(2)O = inosine + NH(3).
XX
FT   From: PS00485
FT   ACT_SITE      5      5       By similarity.
FT   ACT_SITE      6      6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8X661;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10105;
DC   Domain;
TR   PROSITE; PS00921; NITRIL_CHT_2; 1; level=0
XX
Names: Nitrilases / cyanide hydratase active site
Function: Undefined
XX
DE   + AltName: Full=Nitrilase;
DE            EC=3.5.5.1;
XX
CC   -!- CATALYTIC ACTIVITY: A nitrile + 2 H(2)O = a carboxylate + NH(3).
XX
FT   From: PS00921
FT   ACT_SITE      3      3       Nucleophile (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P32961;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10106;
DC   Domain;
TR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1; level=0
XX
Names: ATP synthase alpha and beta subunits
Function: Undefined
XX
DE   + AltName: Full=H(+)-transporting two-sector ATPase;
DE            EC=3.6.3.14;
XX
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
XX
FT   From: PS00152
FT   SITE          8      8       Required for activity (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q2LQZ7;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10107;
DC   Domain;
TR   PROSITE; PS01205; T4_DEIODINASE; 1; level=0
XX
Names: Iodothyronine deiodinases active site
Function: Undefined
XX
DE   + AltName: Full=Thyroxine 5'-deiodinase;
DE            EC=1.97.1.10;
XX
CC   -!- CATALYTIC ACTIVITY: 3,5,3'-triiodo-L-thyronine + iodide + A + H(+)
CC       = L-thyroxine + AH(2).
XX
FT   From: PS01205
FT   ACT_SITE     11     11       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5I3B1;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10108;
DC   Domain;
TR   PROSITE; PS00155; CUTINASE_1; 1; level=0
XX
Names: Cutinase, serine active site
Function: Undefined
XX
DE   + AltName: Full=Cutinase;
DE            EC=3.1.1.74;
XX
CC   -!- CATALYTIC ACTIVITY: Cutin + H(2)O = cutin monomers.
XX
FT   From: PS00155
FT   ACT_SITE      8      8       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P63880;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10109;
DC   Domain;
TR   PROSITE; PS00931; CUTINASE_2; 1; level=0
XX
Names: Cutinase, aspartate and histidine active sites
Function: Undefined
XX
DE   + AltName: Full=Cutinase;
DE            EC=3.1.1.74;
XX
CC   -!- CATALYTIC ACTIVITY: Cutin + H(2)O = cutin monomers.
XX
FT   From: PS00931
FT   ACT_SITE      8      8       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P63880;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10110;
DC   Domain;
TR   PROSITE; PS00156; OMPDECASE; 1; level=0
XX
Names: Orotidine 5'-phosphate decarboxylase active site
Function: Undefined
XX
DE   + AltName: Full=Orotidine-5'-phosphate decarboxylase;
DE            EC=4.1.1.23;
XX
CC   -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2).
XX
FT   From: PS00156
FT   ACT_SITE      4      4       Proton donor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5J2D0;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10111;
DC   Domain;
TR   PROSITE; PS00781; PEPCASE_1; 1; level=0
XX
Names: Phosphoenolpyruvate carboxylase active site 1
Function: Undefined
XX
FT   From: PS00781
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q93MH3;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10112;
DC   Domain;
TR   PROSITE; PS00393; PEPCASE_2; 1; level=0
XX
Names: Phosphoenolpyruvate carboxylase active site 2
Function: Undefined
XX
FT   From: PS00393
FT   ACT_SITE      9      9       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8X743;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10113;
DC   Domain;
TR   PROSITE; PS00505; PEPCK_GTP; 1; level=0
XX
Names: Phosphoenolpyruvate carboxykinase (GTP)
Function: Undefined
XX
DE   + AltName: Full=Phosphoenolpyruvate carboxykinase;
DE   AltName: Full=GTP;
DE            EC=4.1.1.32;
XX
CC   -!- CATALYTIC ACTIVITY: GTP + oxaloacetate = GDP + phosphoenolpyruvate
CC       + CO(2).
XX
FT   From: PS00505
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6F8P2;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10114;
DC   Domain;
TR   PROSITE; PS00157; RUBISCO_LARGE; 1; level=0
XX
Names: Ribulose bisphosphate carboxylase large chain active site
Function: Undefined
XX
DE   + AltName: Full=Ribulose-bisphosphate carboxylase;
DE            EC=4.1.1.39;
XX
CC   -!- CATALYTIC ACTIVITY: D-ribulose 1,5-bisphosphate + CO(2) + H(2)O =
CC       2 3-phospho-D-glycerate.
XX
FT   From: PS00157
FT   MOD_RES       4      4       N6-carboxylysine (By similarity).
FT   METAL         5      5       Magnesium (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P24671;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10115;
DC   Domain;
TR   PROSITE; PS01062; HMG_COA_LYASE; 1; level=0
XX
Names: Hydroxymethylglutaryl-coenzyme A lyase active site
Function: Undefined
XX
DE   + RecName: Full=Hydroxymethylglutaryl-CoA lyase;
DE            EC=4.1.3.4;
XX
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-
CC       CoA + acetoacetate.
XX
FT   From: PS01062
FT   ACT_SITE      8      8       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P35914;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/26
//
AC   PRU10116;
DC   Domain;
TR   PROSITE; PS01226; HMG_COA_SYNTHASE; 1; level=0
XX
Names: Hydroxymethylglutaryl-coenzyme A synthase active site
Function: Undefined
XX
DE   + AltName: Full=Hydroxymethylglutaryl-CoA synthase;
DE            EC=2.3.3.10;
XX
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + acetoacetyl-CoA = (S)-3-
CC       hydroxy-3-methylglutaryl-CoA + CoA.
XX
FT   From: PS01226
FT   ACT_SITE     10     10       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P23228;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10117;
DC   Domain;
TR   PROSITE; PS00480; CITRATE_SYNTHASE; 1; level=0
XX
Names: Citrate synthase
Function: Undefined
XX
DE   + AltName: Full=Citrate (Si)-synthase;
DE            EC=2.3.3.1;
XX
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate +
CC       CoA.
XX
FT   From: PS00480
FT   ACT_SITE      4      4       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q59136;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10118;
DC   Domain;
TR   PROSITE; PS00159; ALDOLASE_KDPG_KHG_1; 1; level=0
XX
Names: KDPG and KHG aldolases active site
Function: Undefined
XX
DE   + AltName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase;
DE            EC=4.1.2.14;
XX
CC   -!- CATALYTIC ACTIVITY: 2-dehydro-3-deoxy-D-gluconate 6-phosphate =
CC       pyruvate + D-glyceraldehyde 3-phosphate.
XX
FT   From: PS00159
FT   ACT_SITE      7      7       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P38448;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10119;
DC   Domain;
TR   PROSITE; PS00161; ISOCITRATE_LYASE; 1; level=0
XX
Names: Isocitrate lyase
Function: Undefined
XX
DE   + AltName: Full=Isocitrate lyase;
DE            EC=4.1.3.1;
XX
CC   -!- CATALYTIC ACTIVITY: Isocitrate = succinate + glyoxylate.
XX
FT   From: PS00161
FT   ACT_SITE      3      3       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P45456;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10120;
DC   Domain;
TR   PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1; level=0
XX
Names: Tryptophan synthase alpha chain
Function: Undefined
XX
DE   + AltName: Full=Indole-3-glycerol-phosphate lyase;
DE            EC=4.1.2.8;
XX
CC   -!- CATALYTIC ACTIVITY: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate =
CC       indole + D-glyceraldehyde 3-phosphate.
XX
FT   From: PS00167
FT   ACT_SITE      2      2       Proton acceptor (By similarity).
FT   ACT_SITE     11     11       Proton acceptor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6FEE6;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10121;
DC   Domain;
TR   PROSITE; PS01335; METHYLGLYOXAL_SYNTH; 1; level=0
XX
Names: Methylglyoxal synthase active site
Function: Undefined
XX
DE   + AltName: Full=Methylglyoxal synthase;
DE            EC=4.2.3.3;
XX
CC   -!- CATALYTIC ACTIVITY: Glycerone phosphate = methylglyoxal +
CC       phosphate.
XX
FT   From: PS01335
FT   ACT_SITE      7      7       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q81ST9;
Scope:
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10122;
DC   Domain;
TR   PROSITE; PS00488; PAL_HISTIDASE; 1; level=0
XX
Names: Phenylalanine and histidine ammonia-lyases
Function: Undefined
XX
DE   + AltName: Full=Histidine ammonia-lyase;
DE            EC=4.3.1.3;
XX
CC   -!- CATALYTIC ACTIVITY: L-histidine = urocanate + NH(3).
XX
FT   From: PS00488
FT   MOD_RES       6      6       2,3-didehydroalanine (Ser) (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5NZX8;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10123;
DC   Domain;
TR   PROSITE; PS00987; PTPS_1; 1; level=0
XX
Names: 6-pyruvoyl tetrahydropterin synthase
Function: Undefined
XX
DE   + AltName: Full=6-pyruvoyltetrahydropterin synthase;
DE            EC=4.2.3.12;
XX
CC   -!- CATALYTIC ACTIVITY: 6-((1S,2R)-1,2-dihydroxy-3-
CC       triphosphooxypropyl)-7,8-dihydropterin = 6-pyruvoyl-5,6,7,8-
CC       tetrahydropterin + triphosphate.
XX
FT   From: PS00987
FT   ACT_SITE      1      1       Proton acceptor (By similarity).
FT   METAL         5      5       Zinc (By similarity).
FT   METAL         7      7       Zinc (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O02058;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10124;
DC   Domain;
TR   PROSITE; PS00988; PTPS_2; 1; level=0
XX
Names: 6-pyruvoyl tetrahydropterin synthase
Function: Undefined
XX
DE   + AltName: Full=6-pyruvoyltetrahydropterin synthase;
DE            EC=4.2.3.12;
XX
CC   -!- CATALYTIC ACTIVITY: 6-((1S,2R)-1,2-dihydroxy-3-
CC       triphosphooxypropyl)-7,8-dihydropterin = 6-pyruvoyl-5,6,7,8-
CC       tetrahydropterin + triphosphate.
XX
FT   From: PS00988
FT   ACT_SITE      2      2       Charge relay system (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P80081;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10125;
DC   Domain;
TR   PROSITE; PS01326; DAP_EPIMERASE; 1; level=0
XX
Names: Diaminopimelate epimerase
Function: Undefined
XX
FT   From: PS01326
FT   ACT_SITE      5      5       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q8YVD0;
Scope:
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10126;
DC   Domain;
TR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1; level=0
XX
Names: Aldose 1-epimerase putative active site
Function: Undefined
XX
DE   + AltName: Full=Aldose 1-epimerase;
DE            EC=5.1.3.3;
XX
CC   -!- CATALYTIC ACTIVITY: Alpha-D-glucose = beta-D-glucose.
XX
FT   From: PS00545
FT   ACT_SITE      4      4       Proton donor (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5EA79;
Scope:
 Eukaryota
 Bacteria
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10127;
DC   Domain;
TR   PROSITE; PS00171; TIM_1; 1; level=0
TR   PROSITE; PS51440; TIM_2; 1; level=0
XX
Names: Triosephosphate isomerase (TIM) family
Function: Triosephosphate isomerase (EC 5.3.1.1) (TIM) is the glycolytic 
 enzyme that catalyzes the reversible interconversion of glyceraldehyde 
 3-phosphate and dihydroxyacetone phosphate.
XX
case <Feature:PS51440:91=H> and <Feature:PS51440:162=E>
ID   TPIS
DE   + RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=tpiA;
XX
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
end case
case <OC:Viridiplantae>
CC   -!- MISCELLANEOUS: In plants, there are two types of TPIS, cytosolic
CC       and plastid.
end case
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
XX
case <Feature:PS51440:91=H> and <Feature:PS51440:162=E>
GO   GO:0004807; F:triose-phosphate isomerase activity
GO   GO:0006096; P:glycolysis
GO   GO:0006094; P:gluconeogenesis
GO   GO:0006098; P:pentose-phosphate shunt
GO   GO:0005737; C:cytoplasm
end case
XX
case <Feature:PS51440:91=H> and <Feature:PS51440:162=E>
KW   Isomerase
KW   Gluconeogenesis
KW   Glycolysis
KW   Pentose shunt
KW   Cytoplasm
end case
XX
FT   From: PS51440
FT   ACT_SITE     91     91       Electrophile (By similarity).
FT   Group: 1; Condition: H
FT   ACT_SITE    162    162       Proton acceptor (By similarity).
FT   Group: 1; Condition: E
FT   BINDING       7      7       Substrate (By similarity).
FT   Group: 1; Condition: N
FT   BINDING       9      9       Substrate (By similarity).
FT   Group: 1; Condition: K
FT   From: PS00171
case not <AnyFeature:PS51440>
FT   ACT_SITE      3      3       Proton acceptor (By similarity).
end case
XX
Chop: Nter=0; Cter=0;
Size: 200-290;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q928I1; P34937;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.3  2009/04/03
//
AC   PRU10130;
DC   Domain;
TR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1; level=0
XX
Names: Eukaryotic DNA topoisomerase I active site
Function: Undefined
XX
DE   + AltName: Full=DNA topoisomerase;
DE            EC=5.99.1.2;
XX
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining.
XX
FT   From: PS00176
FT   ACT_SITE      6      6       O-(3'-phospho-DNA)-tyrosine intermediate
FT                                (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q76ZS7;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10131;
DC   Domain;
TR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1; level=0
XX
Names: Prokaryotic DNA topoisomerase I active site
Function: Undefined
XX
DE   + AltName: Full=DNA topoisomerase;
DE            EC=5.99.1.2;
XX
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining.
XX
FT   From: PS00396
FT   ACT_SITE      7      7       For DNA cleavage activity (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9KA23;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10132;
DC   Domain;
TR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1; level=0
XX
Names: Ubiquitin-activating enzyme active site
Function: Undefined
XX
FT   From: PS00865
FT   ACT_SITE      3      3       Glycyl thioester intermediate (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P22314;
Scope:
 Eukaryota
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10133;
DC   Domain;
TR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1; level=0
XX
Names: Ubiquitin-conjugating enzymes active site
Function: Undefined
XX
DE   + AltName: Full=Ubiquitin--protein ligase;
DE            EC=6.3.2.19;
XX
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
XX
FT   From: PS00183
FT   ACT_SITE      8      8       Glycyl thioester intermediate (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P25865;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10134;
DC   Domain;
TR   PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1; level=0
XX
Names: Adenylosuccinate synthetase active site
Function: Undefined
XX
FT   From: PS00513
FT   ACT_SITE      6      6       By similarity.
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q39PN9;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10135;
DC   Domain;
TR   PROSITE; PS00697; DNA_LIGASE_A1; 1; level=0
XX
Names: ATP-dependent DNA ligase AMP-binding site
Function: Undefined
XX
DE   + AltName: Full=DNA ligase;
DE   AltName: Full=ATP;
DE            EC=6.5.1.1;
XX
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + diphosphate +
CC       (deoxyribonucleotide)(n+m).
XX
FT   From: PS00697
FT   ACT_SITE      3      3       N6-AMP-lysine intermediate (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: O29632;
Scope:
 Eukaryota
 Bacteria
 Archaea
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10136;
DC   Domain;
TR   PROSITE; PS01055; DNA_LIGASE_N1; 1; level=0
XX
Names: NAD-dependent DNA ligase
Function: Undefined
XX
DE   + AltName: Full=DNA ligase;
DE   AltName: Full=NAD(+);
DE            EC=6.5.1.2;
XX
CC   -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide +
CC       (deoxyribonucleotide)(n+m).
XX
FT   From: PS01055
FT   ACT_SITE      1      1       N6-AMP-lysine intermediate (By
FT                                similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q9ZLM1;
Scope:
 Bacteria
 Viruses
Comments: None
XX
# Revision 1.2  2009/02/27
//
AC   PRU10137;
DC   Domain;
TR   PROSITE; PS00397; RECOMBINASES_1; 1; level=0
XX
Names: Site-specific recombinases active site
Function: Undefined
XX
FT   From: PS00397
FT   ACT_SITE      5      5       O-(5'-phospho-DNA)-serine intermediate
FT                                (By similarity).
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P21703;
Scope:
 Bacteria
 Viruses
 Bacteriophage
Comments: None
XX
# Revision 1.1  2006/10/16
//
AC   PRU10138;
DC   Domain;
TR   PROSITE; PS00014; ER_TARGET; 1; level=0
XX
Names: Endoplasmic reticulum targeting sequence
Function: Proteins that permanently reside in the lumen of the endoplasmic
 reticulum (ER) seem to be distinguished from newly synthesized secretory
 proteins by the presence of the C-terminal sequence Lys-Asp-Glu-Leu (KDEL).
XX
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (Potential).
XX
GO   GO:0005783; C:endoplasmic reticulum
XX
KW   Endoplasmic reticulum
XX
FT   From: PS00014
FT   MOTIF      from     to       Prevents secretion from ER (Potential).
XX
Chop: Nter=0; Cter=0;
Size: 4;
Related: None;
Repeats: 1;
Topology: Not cytoplasmic;
Example: Q9Y2B0;
Scope:
 Eukaryota
 Viruses
Comments: None;
XX
# Revision 1.1  2009/08/21
//
