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<HTML>
<HEAD>
<TITLE>
EMBOSS: patmatmotifs
</TITLE>
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<BODY BGCOLOR="#FFFFFF" text="#000000">
<table align=center border=0 cellspacing=0 cellpadding=0>
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<A HREF="/" ONMOUSEOVER="self.status='Go to the EMBOSS home page';return true"><img border=0 src="emboss_icon.jpg" alt="" width=150 height=48></a>
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<td align=left valign=middle>
<b><font size="+6">
patmatmotifs
</font></b>
</td></tr>
</table>
<br>
<p>
<H2>
Function
</H2>
Search a PROSITE motif database with a protein sequence
<H2>
Description
</H2>
<b>patmatmotifs</b> takes a protein sequence and compares it to the
PROSITE database of motifs.
<p>
For a description of PROSITE, we can do no better than to quote the
PROSITE user's documentation:
<i>
<p>
PROSITE is a method of determining what is the function of uncharacterized
proteins translated from genomic or cDNA sequences. It consists of a
database of biologically significant sites and patterns formulated in such
a way that with appropriate computational tools it can rapidly and
reliably identify to which known family of protein (if any) the new
sequence belongs.
<p>
In some cases the sequence of an unknown protein is too distantly related
to any protein of known structure to detect its resemblance by overall
sequence alignment, but it can be identified by the occurrence in its
sequence of a particular cluster of residue types which is variously known
as a pattern, motif, signature, or fingerprint. These motifs arise because
of particular requirements on the structure of specific region(s) of a
protein which may be important, for example, for their binding properties
or for their enzymatic activity. These requirements impose very tight
constraints on the evolution of those limited (in size) but important
portion(s) of a protein sequence. To paraphrase Orwell, in Animal Farm, we
can say that "some regions of a protein sequence are more equal than
others" !
<p>
The use of protein sequence patterns (or motifs) to determine the
function(s) of proteins is becoming very rapidly one of the essential
tools of sequence analysis. This reality has been recognized by many
authors, as it can be illustrated from the following citations from two of
the most well known experts of protein sequence analysis, R.F. Doolittle
and A.M. Lesk:
<pre>
"There are many short sequences that are often (but not always)
diagnostics of certain binding properties or active sites. These can be
set into a small subcollection and searched against your sequence (1)".
"In some cases, the structure and function of an unknown protein which
is too distantly related to any protein of known structure to detect
its affinity by overall sequence alignment may be identified by its
possession of a particular cluster of residues types classified as a
motifs. The motifs, or templates, or fingerprints, arise because of
particular requirements of binding sites that impose very tight
constraint on the evolution of portions of a protein sequence (2)."
</pre>
</i>
<p>
The home web page of PROSITE is: <a
href="http://www.expasy.ch/prosite/">http://www.expasy.ch/prosite/</a>
<p>
It is common to find that a search of the PROSITE database against a
protein sequence will report many matches to the short motifs that are
indicative of the post-translational modification sites, such as
glycolsylation, myristylation and phosphorylation sites. These reports
are often unwanted and are not normally reported. You can turn
reporting of these short motifs on by giving the '-noprune' option on
the command-line.
<p>
Your EMBOSS administrator must have set up the local EMBOSS PROSITE
database using the utility '<b>prosextract</b>' before this program will run.
<H2>
Usage
</H2>
<b>Here is a sample session with patmatmotifs</b>
<p>
<p>
<table width="90%"><tr><td bgcolor="#CCFFFF"><pre>
% <b>patmatmotifs -full </b>
Search a PROSITE motif database with a protein sequence
Input protein sequence: <b>tsw:opsd_human</b>
Output report [opsd_human.patmatmotifs]: <b></b>
</pre></td></tr></table><p>
<p>
<a href="#input.1">Go to the input files for this example</a><br><a href="#output.1">Go to the output files for this example</a><p><p>
<H2>
Command line arguments
</H2>
<table CELLSPACING=0 CELLPADDING=3 BGCOLOR="#f5f5ff" ><tr><td>
<pre>
Standard (Mandatory) qualifiers:
[-sequence] sequence Protein sequence filename and optional
format, or reference (input USA)
[-outfile] report [*.patmatmotifs] Output report file name
Additional (Optional) qualifiers:
-full boolean [N] Provide full documentation for matching
patterns
-[no]prune boolean [Y] Ignore simple patterns. If this is true
then these simple post-translational
modification sites are not reported:
myristyl, asn_glycosylation,
camp_phospho_site, pkc_phospho_site,
ck2_phospho_site, and tyr_phospho_site.
Advanced (Unprompted) qualifiers: (none)
Associated qualifiers:
"-sequence" associated qualifiers
-sbegin1 integer Start of the sequence to be used
-send1 integer End of the 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
-rformat2 string Report format
-rname2 string Base file name
-rextension2 string File name extension
-rdirectory2 string Output directory
-raccshow2 boolean Show accession number in the report
-rdesshow2 boolean Show description in the report
-rscoreshow2 boolean Show the score in the report
-rusashow2 boolean Show the full USA in the report
-rmaxall2 integer Maximum total hits to report
-rmaxseq2 integer Maximum hits to report for one sequence
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
</pre>
</td></tr></table>
<P>
<table border cellspacing=0 cellpadding=3 bgcolor="#ccccff">
<tr bgcolor="#FFFFCC">
<th align="left" colspan=2>Standard (Mandatory) qualifiers</th>
<th align="left">Allowed values</th>
<th align="left">Default</th>
</tr>
<tr>
<td>[-sequence]<br>(Parameter 1)</td>
<td>Protein sequence filename and optional format, or reference (input USA)</td>
<td>Readable sequence</td>
<td><b>Required</b></td>
</tr>
<tr>
<td>[-outfile]<br>(Parameter 2)</td>
<td>Output report file name</td>
<td>Report output file</td>
<td><i><*></i>.patmatmotifs</td>
</tr>
<tr bgcolor="#FFFFCC">
<th align="left" colspan=2>Additional (Optional) qualifiers</th>
<th align="left">Allowed values</th>
<th align="left">Default</th>
</tr>
<tr>
<td>-full</td>
<td>Provide full documentation for matching patterns</td>
<td>Boolean value Yes/No</td>
<td>No</td>
</tr>
<tr>
<td>-[no]prune</td>
<td>Ignore simple patterns. If this is true then these simple post-translational modification sites are not reported: myristyl, asn_glycosylation, camp_phospho_site, pkc_phospho_site, ck2_phospho_site, and tyr_phospho_site.</td>
<td>Boolean value Yes/No</td>
<td>Yes</td>
</tr>
<tr bgcolor="#FFFFCC">
<th align="left" colspan=2>Advanced (Unprompted) qualifiers</th>
<th align="left">Allowed values</th>
<th align="left">Default</th>
</tr>
<tr>
<td colspan=4>(none)</td>
</tr>
</table>
<H2>
Input file format
</H2>
<b>patmatmotifs</b> reads a protein sequence USA.
<p>
<a name="input.1"></a>
<h3>Input files for usage example </h3>
'tsw:opsd_human' is a sequence entry in the example protein database 'tsw'
<p>
<p><h3>Database entry: tsw:opsd_human</h3>
<table width="90%"><tr><td bgcolor="#FFCCFF">
<pre>
ID OPSD_HUMAN Reviewed; 348 AA.
AC P08100; Q16414; Q2M249;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 20-MAR-2007, entry version 91.
DE Rhodopsin (Opsin-2).
GN Name=RHO; Synonyms=OPN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=84272729; PubMed=6589631;
RA Nathans J., Hogness D.S.;
RT "Isolation and nucleotide sequence of the gene encoding human
RT rhodopsin.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4851-4855(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RG The German cDNA consortium;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120.
RX PubMed=8566799; DOI=10.1016/0378-1119(95)00688-5;
RA Bennett J., Beller B., Sun D., Kariko K.;
RT "Sequence analysis of the 5.34-kb 5' flanking region of the human
RT rhodopsin-encoding gene.";
RL Gene 167:317-320(1995).
RN [6]
RP REVIEW ON RP4 VARIANTS.
RX MEDLINE=94004905; PubMed=8401533;
RA Al-Maghtheh M., Gregory C., Inglehearn C., Hardcastle A.,
RA Bhattacharya S.;
<font color=red> [Part of this file has been deleted for brevity]</font>
FT /FTId=VAR_004816.
FT VARIANT 209 209 V -> M (effect not known).
FT /FTId=VAR_004817.
FT VARIANT 211 211 H -> P (in RP4).
FT /FTId=VAR_004818.
FT VARIANT 211 211 H -> R (in RP4).
FT /FTId=VAR_004819.
FT VARIANT 216 216 M -> K (in RP4).
FT /FTId=VAR_004820.
FT VARIANT 220 220 F -> C (in RP4).
FT /FTId=VAR_004821.
FT VARIANT 222 222 C -> R (in RP4).
FT /FTId=VAR_004822.
FT VARIANT 255 255 Missing (in RP4).
FT /FTId=VAR_004823.
FT VARIANT 264 264 Missing (in RP4).
FT /FTId=VAR_004824.
FT VARIANT 267 267 P -> L (in RP4).
FT /FTId=VAR_004825.
FT VARIANT 267 267 P -> R (in RP4).
FT /FTId=VAR_004826.
FT VARIANT 292 292 A -> E (in CSNBAD1).
FT /FTId=VAR_004827.
FT VARIANT 296 296 K -> E (in RP4).
FT /FTId=VAR_004828.
FT VARIANT 297 297 S -> R (in RP4).
FT /FTId=VAR_004829.
FT VARIANT 342 342 T -> M (in RP4).
FT /FTId=VAR_004830.
FT VARIANT 345 345 V -> L (in RP4).
FT /FTId=VAR_004831.
FT VARIANT 345 345 V -> M (in RP4).
FT /FTId=VAR_004832.
FT VARIANT 347 347 P -> A (in RP4).
FT /FTId=VAR_004833.
FT VARIANT 347 347 P -> L (in RP4; common variant).
FT /FTId=VAR_004834.
FT VARIANT 347 347 P -> Q (in RP4).
FT /FTId=VAR_004835.
FT VARIANT 347 347 P -> R (in RP4).
FT /FTId=VAR_004836.
FT VARIANT 347 347 P -> S (in RP4).
FT /FTId=VAR_004837.
SQ SEQUENCE 348 AA; 38893 MW; 6F4F6FCBA34265B2 CRC64;
MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY
VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH GYFVFGPTGC NLEGFFATLG
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLAGWSRYIP
EGLQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES
ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI
YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA
//
</pre>
</td></tr></table><p>
<H2>
Output file format
</H2>
<p>
The output is a standard EMBOSS report file.
<p>
The results can be output in one of several styles by using the
command-line qualifier <b>-rformat xxx</b>, where 'xxx' is replaced by
the name of the required format. The available format names are: embl,
genbank, gff, pir, swiss, trace, listfile, dbmotif, diffseq, excel,
feattable, motif, regions, seqtable, simple, srs, table, tagseq
<p>
See:
<A href="http://emboss.sf.net/docs/themes/ReportFormats.html">
http://emboss.sf.net/docs/themes/ReportFormats.html</A>
for further information on report formats.
<p>
<p>
By default <b>patmatmotifs</b> writes a 'dbmotif' report file.
<p>
<a name="output.1"></a>
<h3>Output files for usage example </h3>
<p><h3>File: opsd_human.patmatmotifs</h3>
<table width="90%"><tr><td bgcolor="#CCFFCC">
<pre>
########################################
# Program: patmatmotifs
# Rundate: Sun 15 Jul 2007 12:00:00
# Commandline: patmatmotifs
# -full
# -sequence tsw:opsd_human
# Report_format: dbmotif
# Report_file: opsd_human.patmatmotifs
########################################
#=======================================
#
# Sequence: OPSD_HUMAN from: 1 to: 348
# HitCount: 2
#
# Full: Yes
# Prune: Yes
# Data_file: ../prosextract-keep/PROSITE/prosite.lines
#
#=======================================
Length = 17
Start = position 123 of sequence
End = position 139 of sequence
Motif = G_PROTEIN_RECEP_F1_1
TLGGEIALWSLVVLAIERYVVVCKPMS
| |
123 139
Length = 17
Start = position 290 of sequence
End = position 306 of sequence
Motif = OPSIN
PIFMTIPAFFAKSAAIYNPVIYIMMNK
| |
290 306
#---------------------------------------
#
# Motif: G_PROTEIN_RECEP_F1_1
# Count: 1
#
# *****************************************
# * G-protein coupled receptors signature *
# *****************************************
<font color=red> [Part of this file has been deleted for brevity]</font>
# Count: 1
#
# *************************************************
# * Visual pigments (opsins) retinal binding site *
# *************************************************
#
# Visual pigments [1,2] are the light-absorbing molecules that mediate vision.
# They consist of an apoprotein, opsin, covalently linked to the chromophore
# cis-retinal. Vision is effected through the absorption of a photon by cis-
# retinal which is isomerized to trans-retinal. This isomerization leads to a
# change of conformation of the protein. Opsins are integral membrane proteins
# with seven transmembrane regions that belong to family 1 of G-protein coupled
# receptors (see <PDOC00210>).
#
# In vertebrates four different pigments are generally found. Rod cells, which
# mediate vision in dim light, contain the pigment rhodopsin. Cone cells, which
# function in bright light, are responsible for color vision and contain three
# or more color pigments (for example, in mammals: red, blue and green).
#
# In Drosophila, the eye is composed of 800 facets or ommatidia. Each
# ommatidium contains eight photoreceptor cells (R1-R8): the R1 to R6 cells are
# outer cells, R7 and R8 inner cells. Each of the three types of cells (R1-R6,
# R7 and R8) expresses a specific opsin.
#
# Proteins evolutionary related to opsins include squid retinochrome, also known
# as retinal photoisomerase, which converts various isomers of retinal into 11-
# cis retinal and mammalian retinal pigment epithelium (RPE) RGR [3], a protein
# that may also act in retinal isomerization.
#
# The attachment site for retinal in the above proteins is a conserved lysine
# residue in the middle of the seventh transmembrane helix. The pattern we
# developed includes this residue.
#
# -Consensus pattern: [LIVMWAC]-[PGAC]-x(3)-[SAC]-K-[STALIMR]-[GSACPNV]-[STACP]-
# x(2)-[DENF]-[AP]-x(2)-[IY]
# [K is the retinal binding site]
# -Sequences known to belong to this class detected by the pattern: ALL.
# -Other sequence(s) detected in SWISS-PROT: NONE.
# -Last update: July 1998 / Pattern and text revised.
#
# [ 1] Applebury M.L., Hargrave P.A.
# Vision Res. 26:1881-1895(1986).
# [ 2] Fryxell K.J., Meyerowitz E.M.
# J. Mol. Evol. 33:367-378(1991).
# [ 3] Shen D., Jiang M., Hao W., Tao L., Salazar M., Fong H.K.W.
# Biochemistry 33:13117-13125(1994).
#
# ***************
#
#
#---------------------------------------
</pre>
</td></tr></table><p>
<H2>
Data files
</H2>
Data and documentation from PROSITE files is automatically read. This
has been generated and formatted by running <b>prosextract</b> before running
<b>patmatmotifs</b>.
<H2>
Notes
</H2>
Program is only useful when <b>prosextract</b> is used beforehand.
<H2>
References
</H2>
If you want to refer to PROSITE in a publication you can do so by citing:
<p>
Bairoch A., Bucher P., Hofmann K.
The PROSITE datatase, its status in 1997.
Nucleic Acids Res. 24:217-221(1997).
<p>
Other references:
<p>
<ol>
<li>Bairoch, A., Bucher P. (1994) PROSITE: recent developments. Nucleic
Acids Research, Vol 22, No.17 3583-3589.
<li>Bairoch, A., (1992) PROSITE: a dictionary of sites and patterns in
proteins. Nucleic Acids Research, Vol 20, Supplement, 2013-2018.
<li>Peek, J., O'Reilly, T., Loukides, M., (1997) Unix Power Tools, 2nd
Edition.
<li>Doolittle R.F. (In) Of URFs and ORFs: a primer on how to analyze
derived amino acid sequences., University Science Books, Mill Valley,
California, (1986).
<li>Lesk A.M. (In) Computational Molecular Biology, Lesk A.M., Ed.,
pp17-26, Oxford University Press, Oxford (1988).
</ol>
<H2>
Warnings
</H2>
Your EMBOSS administrator must have set up the local EMBOSS PROSITE
database using the utility '<b>prosextract</b>' before this program will run.
<H2>
Diagnostic Error Messages
</H2>
The error message:
<p>
<pre>
"Either EMBOSS_DATA undefined or PROSEXTRACT needs running"
</pre>
<p>
indicates that your local EMBOSS administrator has not yet correctly
set up the local EMBOSS PROSITE database using the utility <a
href="prosextract.html">'prosextract'.</a>
<H2>
Exit status
</H2>
It always exits with status 0
<H2>
Known bugs
</H2>
None.
<h2><a name="See also">See also</a></h2>
<table border cellpadding=4 bgcolor="#FFFFF0">
<tr><th>Program name</th><th>Description</th></tr>
<tr>
<td><a href="antigenic.html">antigenic</a></td>
<td>Finds antigenic sites in proteins</td>
</tr>
<tr>
<td><a href="digest.html">digest</a></td>
<td>Protein proteolytic enzyme or reagent cleavage digest</td>
</tr>
<tr>
<td><a href="epestfind.html">epestfind</a></td>
<td>Finds PEST motifs as potential proteolytic cleavage sites</td>
</tr>
<tr>
<td><a href="fuzzpro.html">fuzzpro</a></td>
<td>Protein pattern search</td>
</tr>
<tr>
<td><a href="fuzztran.html">fuzztran</a></td>
<td>Protein pattern search after translation</td>
</tr>
<tr>
<td><a href="helixturnhelix.html">helixturnhelix</a></td>
<td>Report nucleic acid binding motifs</td>
</tr>
<tr>
<td><a href="oddcomp.html">oddcomp</a></td>
<td>Find protein sequence regions with a biased composition</td>
</tr>
<tr>
<td><a href="patmatdb.html">patmatdb</a></td>
<td>Search a protein sequence with a motif</td>
</tr>
<tr>
<td><a href="pepcoil.html">pepcoil</a></td>
<td>Predicts coiled coil regions</td>
</tr>
<tr>
<td><a href="preg.html">preg</a></td>
<td>Regular expression search of a protein sequence</td>
</tr>
<tr>
<td><a href="pscan.html">pscan</a></td>
<td>Scans proteins using PRINTS</td>
</tr>
<tr>
<td><a href="sigcleave.html">sigcleave</a></td>
<td>Reports protein signal cleavage sites</td>
</tr>
</table>
<H2>
Author(s)
</H2>
Sinead O'Leary (current e-mail address unknown)
<br>
while she was at:
<br>
HGMP-RC, Genome Campus, Hinxton, Cambridge CB10 1SB, UK
<H2>
History
</H2>
Completed May 13 1999.
<H2>
Target users
</H2>
This program is intended to be used by everyone and everything, from naive users to embedded scripts.
<H2>
Comments
</H2>
None
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