EMBOSS: pepcoil

| 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 | <*>.pepcoil
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              Reviewed;         281 AA.
    AC   P03069; P03068; Q70D88; Q70D91; Q70D96; Q70D99; Q70DA0; Q96UT3;
    DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
    DT   21-JUL-1986, sequence version 1.
    DT   20-MAR-2007, entry version 82.
    DE   General control protein GCN4 (Amino acid biosynthesis regulatory
    DE   protein).
    GN   Name=GCN4; Synonyms=AAS3, ARG9; OrderedLocusNames=YEL009C;
    OS   Saccharomyces cerevisiae (Baker's yeast).
    OC   Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes;
    OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
    OX   NCBI_TaxID=4932;
    RN   [1]
    RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    RX   MEDLINE=85038531; PubMed=6387704;
    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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    RX   MEDLINE=84298088; PubMed=6433345;
    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   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-24; SER-62;
    RP   ALA-82; ALA-91; ALA-125 AND GLU-196.
    RC   STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
    RC   CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
    RX   PubMed=15087486; DOI=10.1093/nar/gkh529;
    RA   Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
    RA   Souciet J.-L.;
    RT   "Differential evolution of the Saccharomyces cerevisiae DUP240
    RT   paralogs and implication of recombination in phylogeny.";
    RL   Nucleic Acids Res. 32:2069-2078(2004).
    RN   [4]
    RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    RC   STRAIN=ATCC 204511 / S288c / AB972;
    RX   MEDLINE=97313264; PubMed=9169868;
    RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
    RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
    RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
    RA   Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
    RA   Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
    RA   Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
    RA   Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
    RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
    RL   Nature 387:78-81(1997).

      [Part of this file has been deleted for brevity]

    FT   CHAIN         1    281       General control protein GCN4.
    FT                                /FTId=PRO_0000076490.
    FT   DOMAIN      253    274       Leucine-zipper.
    FT   DNA_BIND    231    249       Basic motif.
    FT   REGION       89    100       Required for transcriptional activation.
    FT   REGION      106    125       Required for transcriptional activation.
    FT   MOD_RES     165    165       Phosphothreonine (by PHO85).
    FT   VARIANT      24     24       S -> P (in strain: CLIB 219).
    FT   VARIANT      62     62       P -> S (in strain: CLIB 630 haplotype
    FT                                Ha2).
    FT   VARIANT      82     82       T -> A (in strain: CLIB 556 haplotype
    FT                                Ha1).
    FT   VARIANT      91     91       D -> A (in strain: CLIB 95, CLIB 219,
    FT                                CLIB 382, CLIB 388, CLIB 410, CLIB 413,
    FT                                CLIB 556, CLIB 630, K1, R12, R13
    FT                                haplotype Ha2, Sigma 1278B haplotype Ha1,
    FT                                YIIc12 and YIIc17).
    FT   VARIANT     125    125       D -> A (in strain: CLIB 556 haplotype
    FT                                Ha1).
    FT   VARIANT     196    196       D -> E (in strain: CLIB 388, CLIB 410,
    FT                                CLIB 413, CLIB 630 haplotype Ha1, K1,
    FT                                YIIc12 haplotype Ha2 and YIIc17 haplotype
    FT                                Ha1).
    FT   MUTAGEN      97     98       FF->AA: Reduces transcriptional
    FT                                activation activity; when associated with
    FT                                A-107; A-110; A-113; A-120; A-123 and A-
    FT                                124.
    FT   MUTAGEN     107    107       M->A: Reduces transcriptional activation
    FT                                activity; when associated with A-97; A-
    FT                                98; A-110; A-113; A-120; A-123 and A-124.
    FT   MUTAGEN     110    110       Y->A: Reduces transcriptional activation
    FT                                activity; when associated with A-97; A-
    FT                                98; A-107; A-113; A-120; A-123 and A-124.
    FT   MUTAGEN     113    113       L->A: Reduces transcriptional activation
    FT                                activity; when associated with A-97; A-
    FT                                98; A-107; A-110; A-120; A-123 and A-124.
    FT   MUTAGEN     120    124       WTSLF->ATSAA: Reduces transcriptional
    FT                                activation activity; when associated with
    FT                                A-97; A-98; A-107; A-110 and A-113.
    FT   CONFLICT    239    281       ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVG
    FT                                ER -> PGVLVRESCKE (in Ref. 2).
    FT   HELIX       230    276
    FT   HELIX       250    276
    FT   HELIX       251    278
    SQ   SEQUENCE   281 AA;  31310 MW;  2ED1B8E35D509578 CRC64;
         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 name | Description
--- | ---
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