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📄 pepcoil.txt

📁 emboss的linux版本的源代码
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                                  pepcoil Function   Predicts coiled coil regionsDescription   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 252:1162-4Usage   Here is a sample session with pepcoil% pepcoil Predicts coiled coil regionsInput protein sequence(s): tsw:gcn4_yeastWindow size [28]: Output file [gcn4_yeast.pepcoil]:    Go to the input files for this example   Go to the output files for this exampleCommand 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 messagesInput 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_yeastID   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 REGULATORYDE   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 generalRT   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 controlRT   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 activatorRT   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, parallelRT   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 collaborationCC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -CC   the European Bioinformatics Institute.  There are no  restrictions on  itsCC   use  by  non-profit  institutions as long  as its content  is  in  no  wayCC   modified and this statement is not removed.  Usage  by  and for commercialCC   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       ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGFT                                ER -> PGVLVRESCKE (IN REF. 2).FT   HELIX       227    276FT   TURN        277    277SQ   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.pepcoilPEPCOIL of GCN4_YEAST   using a window of 28 residuesOther structures from 1 to 232 (232 residues)   Max score: 1.283 (probability 0.21)Prediction starts at 233Probable 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 regionsAuthor(s)   Alan Bleasby (ajb 

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