pepcoil

 

Function

Predicts coiled coil regions

Description

Coiled coils are formed by two or three alpha helices in parallel and in register that cross at an angle of approximately 20 degrees, are strongly amphipathic and display a pattern of hydrophilic and hydrophobic residues that is repeated every seven residues. The seven positions of the heptad repeat are designated a through g, a and d being generally hydrophobic, while the others are hydrophilic.

The parallel two-stranded alpha-helical coiled coil is the most frequently encountered subunit-oligomerization motif in proteins.

pepcoil calculates the probability of a coiled-coil structure for windows of 28 residues through a protein sequence using the method of Lupas A, van Dyke M & Stock J (1991); Science 252:1162-4

Usage

Here is a sample session with pepcoil


% pepcoil 
Predicts coiled coil regions
Input protein sequence(s): tsw:gcn4_yeast
Window size [28]: 
Output file [gcn4_yeast.pepcoil]: 

Go to the input files for this example
Go to the output files for this example

Command line arguments

   Standard (Mandatory) qualifiers:
  [-sequence]          seqall     Protein sequence(s) filename and optional
                                  format, or reference (input USA)
   -window             integer    [28] Window size (Integer from 7 to 28)
  [-outfile]           outfile    [*.pepcoil] Output file name

   Additional (Optional) qualifiers: (none)
   Advanced (Unprompted) qualifiers:
   -[no]coil           boolean    [Y] Report coiled coil regions
   -frame              boolean    [Yes if -coil is true] Show coil frameshifts
   -[no]other          boolean    [Y] Report non coiled coil regions

   Associated qualifiers:

   "-sequence" associated qualifiers
   -sbegin1            integer    Start of each sequence to be used
   -send1              integer    End of each sequence to be used
   -sreverse1          boolean    Reverse (if DNA)
   -sask1              boolean    Ask for begin/end/reverse
   -snucleotide1       boolean    Sequence is nucleotide
   -sprotein1          boolean    Sequence is protein
   -slower1            boolean    Make lower case
   -supper1            boolean    Make upper case
   -sformat1           string     Input sequence format
   -sdbname1           string     Database name
   -sid1               string     Entryname
   -ufo1               string     UFO features
   -fformat1           string     Features format
   -fopenfile1         string     Features file name

   "-outfile" associated qualifiers
   -odirectory2        string     Output directory

   General qualifiers:
   -auto               boolean    Turn off prompts
   -stdout             boolean    Write standard output
   -filter             boolean    Read standard input, write standard output
   -options            boolean    Prompt for standard and additional values
   -debug              boolean    Write debug output to program.dbg
   -verbose            boolean    Report some/full command line options
   -help               boolean    Report command line options. More
                                  information on associated and general
                                  qualifiers can be found with -help -verbose
   -warning            boolean    Report warnings
   -error              boolean    Report errors
   -fatal              boolean    Report fatal errors
   -die                boolean    Report dying program messages

Standard (Mandatory) qualifiers Allowed values Default
[-sequence]
(Parameter 1)
Protein sequence(s) filename and optional format, or reference (input USA) Readable sequence(s) Required
-window Window size Integer from 7 to 28 28
[-outfile]
(Parameter 2)
Output file name Output file  
Additional (Optional) qualifiers Allowed values Default
(none)
Advanced (Unprompted) qualifiers Allowed values Default
-[no]coil Report coiled coil regions Boolean value Yes/No Yes
-frame Show coil frameshifts Boolean value Yes/No Yes if -coil is true
-[no]other Report non coiled coil regions Boolean value Yes/No Yes

Input file format

pepcoil reads in a protein sequence USA.

Input files for usage example

'tsw:gcn4_yeast' is a sequence entry in the example protein database 'tsw'

Database entry: tsw:gcn4_yeast

ID   GCN4_YEAST     STANDARD;      PRT;   281 AA.
AC   P03069; P03068;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   GENERAL CONTROL PROTEIN GCN4 (AMINO ACID BIOSYNTHESIS REGULATORY
DE   PROTEIN).
GN   GCN4 OR ARG9 OR AAS3 OR YEL009C.
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Ascomycota; Hemiascomycetes; Saccharomycetales;
OC   Saccharomycetaceae; Saccharomyces.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 85038531.
RA   HINNEBUSCH A.G.;
RT   "Evidence for translational regulation of the activator of general
RT   amino acid control in yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:6442-6446(1984).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 84298088.
RA   THIREOS G., PENN M.D., GREER H.;
RT   "5' untranslated sequences are required for the translational control
RT   of a yeast regulatory gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5096-5100(1984).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=S288C / AB972;
RA   DIETRICH F.S., MULLIGAN J.T., HENNESSEY K.M., ALLEN E., ARAUJO R.,
RA   AVILES E., BERNO A., BRENNAN T., CARPENTER J., CHEN E., CHERRY J.M.,
RA   CHUNG E., DUNCAN M., GUZMAN E., HARTZELL G., HUNICKE-SMITH S.,
RA   HYMAN R., KAYSER A., KOMP C., LASHKARI D., LEW H., LIN D.,
RA   MOSEDALE D., NAKAHARA K., NAMATH A., NORGREN R., OEFNER P., OH C.,
RA   PETEL F.X., ROBERTS D., SEHL P., SCHRAMM S., SHOGREN T., SMITH V.,
RA   TAYLOR P., WEI Y., YELTON M., BOTSTEIN D., DAVIS R.W.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   DOMAINS.
RX   MEDLINE; 87002456.
RA   HOPE I.A., STRUHL K.;
RT   "Functional dissection of a eukaryotic transcriptional activator
RT   protein, GCN4 of yeast.";
RL   Cell 46:885-894(1986).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 250-281.
RX   MEDLINE; 92054531.
RA   O'SHEA E.K., KLEMM J.D., KIM P.S., ALBER T.;
RT   "X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel
RT   coiled coil.";
RL   Science 254:539-544(1991).


  [Part of this file has been deleted for brevity]

CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- SIMILARITY: TO OTHER BZIP PROTEINS.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; K02205; AAA34640.1; -.
DR   EMBL; K02649; AAA65521.1; -.
DR   EMBL; U18530; AAB64486.1; -.
DR   PIR; A03604; RGBYA1.
DR   PIR; A03605; RGBYA2.
DR   PDB; 1ZTA; 15-APR-93.
DR   PDB; 2ZTA; 15-OCT-92.
DR   PDB; 1YSA; 31-OCT-93.
DR   PDB; 1DGC; 22-JUN-94.
DR   PDB; 2DGC; 08-MAR-96.
DR   PDB; 1GCL; 03-JUN-95.
DR   PDB; 1GCM; 29-JAN-96.
DR   PDB; 1SWI; 08-NOV-96.
DR   PDB; 1ZII; 07-JUL-97.
DR   PDB; 1ZIJ; 07-JUL-97.
DR   PDB; 1ZIK; 07-JUL-97.
DR   PDB; 1ZIL; 07-JUL-97.
DR   PDB; 1ZIM; 07-JUL-97.
DR   PDB; 1PIQ; 30-SEP-98.
DR   PDB; 1CE9; 25-MAR-99.
DR   TRANSFAC; T00321; -.
DR   SGD; L0000683; GCN4.
DR   PFAM; PF00170; bZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
KW   Amino-acid biosynthesis; Transcription regulation; Activator;
KW   DNA-binding; Nuclear protein; 3D-structure.
FT   DOMAIN      106    125       REQUIRED FOR TRANSCRIPTIONAL ACTIVATION.
FT   DNA_BIND    231    249       BASIC MOTIF.
FT   DOMAIN      253    274       LEUCINE-ZIPPER.
FT   CONFLICT    239    281       ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVG
FT                                ER -> PGVLVRESCKE (IN REF. 2).
FT   HELIX       227    276
FT   TURN        277    277
SQ   SEQUENCE   281 AA;  31310 MW;  A2155238 CRC32;
     MSEYQPSLFA LNPMGFSPLD GSKSTNENVS ASTSTAKPMV GQLIFDKFIK TEEDPIIKQD
     TPSNLDFDFA LPQTATAPDA KTVLPIPELD DAVVESFFSS STDSTPMFEY ENLEDNSKEW
     TSLFDNDIPV TTDDVSLADK AIESTEEVSL VPSNLEVSTT SFLPTPVLED AKLTQTRKVK
     KPNSVVKKSH HVGKDDESRL DHLGVVAYNR KQRSIPLSPI VPESSDPAAL KRARNTEAAR
     RSRARKLQRM KQLEDKVEEL LSKNYHLENE VARLKKLVGE R
//

Output file format

Output files for usage example

The SwissProt annotation marks the true leucine zipper motif as from 253 to 274. The leucine zipper is a special case of a coiled-coil region.

File: gcn4_yeast.pepcoil

PEPCOIL of GCN4_YEAST
   using a window of 28 residues


Other structures from 1 to 232 (232 residues)
   Max score: 1.283 (probability 0.21)

Prediction starts at 233
Probable coiled-coil from 233 to 281 (49 residues)
   Max score: 1.910 (probability 1.00)

Data files

None.

Notes

None.

References

  1. Lupas A, van Dyke M & Stock J; Predicting Coiled Coils from Protein Sequences. Science 252:1162-4 (1991)

Warnings

None.

Diagnostic Error Messages

None.

Exit status

It always exits with a status of 0.

Known bugs

None.

See also

Program nameDescription
antigenic Finds antigenic sites in proteins
digest Protein proteolytic enzyme or reagent cleavage digest
epestfind Finds PEST motifs as potential proteolytic cleavage sites
fuzzpro Protein pattern search
fuzztran Protein pattern search after translation
garnier Predicts protein secondary structure
helixturnhelix Report nucleic acid binding motifs
hmoment Hydrophobic moment calculation
oddcomp Find protein sequence regions with a biased composition
patmatdb Search a protein sequence with a motif
patmatmotifs Search a PROSITE motif database with a protein sequence
pepnet Displays proteins as a helical net
pepwheel Shows protein sequences as helices
preg Regular expression search of a protein sequence
pscan Scans proteins using PRINTS
sigcleave Reports protein signal cleavage sites
tmap Displays membrane spanning regions

Author(s)

Alan Bleasby (ajb © ebi.ac.uk)
European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK

Original program "PEPCOIL" by Peter Rice (EGCG 1991)

History

Written (1999) - Alan Bleasby

Target users

This program is intended to be used by everyone and everything, from naive users to embedded scripts.

Comments

None