ID POLG_CXB5P STANDARD; PRT; 2185 AA. AC Q03053; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE GENOME POLYPROTEIN [CONTAINS: COAT PROTEIN VP4 (P1A); COAT PROTEIN VP2 DE (P1B); COAT PROTEIN VP3 (P1C); COAT PROTEIN VP1 (P1D); PICORNAIN 2A DE (EC 3.4.22.29) (P2A); CORE PROTEIN P2B; CORE PROTEIN P2C; CORE PROTEIN DE P3A; GENOME-LINKED PROTEIN VPG (P3B); PICORNAIN 3C (EC 3.4.22.28) DE (PROTEASE 3C) (P3C); RNA-DIRECTED RNA POLYMERASE (EC 2.7.7.48) (P3D)]. OS Coxsackievirus B5 (strain Peterborough / 1954/UK/85). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornaviridae; OC Enterovirus. OX NCBI_TaxID=103907; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93260398; PubMed=8388019; RA Zhang G., Wilsden G., Knowles N.J., McCauley J.W.; RT "Complete nucleotide sequence of a coxsackie B5 virus and its RT relationship to swine vesicular disease virus."; RL J. Gen. Virol. 74:845-853(1993). CC -!- FUNCTION: P2A AND THE P3C POLYPEPTIDES ARE PROTEASES THAT CLEAVE CC AT CERTAIN Q/G SITES IN THE POLYPROTEIN. THEY ARE CYSTEINE CC PROTEASES. CC -!- FUNCTION: IT IS THOUGHT THAT THE P2C PROTEIN ATTACHES TO VESICULAR CC MEMBRANES AND IS ASSOCIATED WITH VIRAL RNA SYNTHESIS. CC -!- SUBUNIT: THE VIRUS CAPSID IS COMPOSED OF 60 ICOSAHEDRAL UNITS, CC EACH OF WHICH IS COMPOSED OF ONE COPY EACH OF PROTEINS VP1, VP2, CC VP3, AND VP4. CC -!- PTM: SPECIFIC ENZYMATIC CLEAVAGES IN VIVO YIELD MATURE PROTEINS. CC CLEAVAGE BETWEEN VP4 AND VP2 IS AUTOCATALYTIC; VP1/P2A IS CC CATALYZED BY P2A; ALL OTHER CLEAVAGES ARE CATALYZED BY P3C. CC -!- SIMILARITY: P2A PROTEASE BELONGS TO PEPTIDASE FAMILY C3. CC -!- SIMILARITY: P3C PROTEASE BELONGS TO PEPTIDASE FAMILY C3. 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; X67706; CAA47944.1; -. DR PIR; JQ2021; JQ2021. DR HSSP; P03313; 1COV. DR MEROPS; C03.011; -. DR MEROPS; C03.022; -. DR INTERPRO; IPR000081; -. DR INTERPRO; IPR000199; -. DR INTERPRO; IPR000605; -. DR INTERPRO; IPR001205; -. DR INTERPRO; IPR001676; -. DR INTERPRO; IPR002527; -. DR PFAM; PF00548; Cys-protease-3C; 1. DR PFAM; PF00947; Pico_P2A; 1. DR PFAM; PF01552; Pico_P2B; 1. DR PFAM; PF00680; RNA_dep_RNA_pol; 1. DR PFAM; PF00910; RNA_helicase; 1. DR PFAM; PF00073; rhv; 3. KW Polyprotein; Coat protein; Core protein; Transferase; Myristate; KW RNA-directed RNA polymerase; Hydrolase; Thiol protease. FT CHAIN 2 69 COAT PROTEIN VP4. FT CHAIN 70 330 COAT PROTEIN VP2. FT CHAIN 331 568 COAT PROTEIN VP3. FT CHAIN 569 851 COAT PROTEIN VP1. FT CHAIN 852 1001 PICORNAIN 2A. FT CHAIN 1002 1100 CORE PROTEIN P2B. FT CHAIN 1101 1429 CORE PROTEIN P2C. FT CHAIN 1430 1518 CORE PROTEIN P3A. FT CHAIN 1519 1540 GENOME-LINKED PROTEIN VPG. FT CHAIN 1541 1723 PICORNAIN 3C. FT CHAIN 1724 2185 RNA-DIRECTED RNA POLYMERASE. FT LIPID 2 2 MYRISTATE (BY SIMILARITY). FT ACT_SITE 1687 1687 PROTEASE 3C (POTENTIAL). FT ACT_SITE 1701 1701 PROTEASE 3C (POTENTIAL). SQ SEQUENCE 2185 AA; 243298 MW; 3F9EE29F90D59C6F CRC64; MGAQVSTQKT GAHETGLRAS GNSIIHYTNI NYYKDAASNS ANRQEFAQDP GKFTEPVKDI MIKSMPALNS PSAEECGYSD RVRSITLGNS TITTQECANV VVGYGTWPTY LKDEEATAED QPTQPDVATC RFYTLESVMW QQSSPGWWWK FPDALSNMGL FGQNMQYHYL GRAGYTVHVQ CNASKFHQGC LLVVCVPEAE MGCATLANKP DQKSLSNGET ANTFDSQNTT GQTAVQANVI NAGMGVGVGN LTIFPHQWIN LRTNNSATIV MPYINSVPMD NMFRHNNFTL MIIPFAPLSY STGATTYVPI TVTVAPMCAE YNGLRLAGKQ GLPTMLTPGS NQFLTSDDFQ SPSAMPQFDV TPEMAIPGQV NNLMEIAEVD SVVPVNNTEG KVSSIEAYQI PVQSNSTNGS QVFGFPLIPG ASSVLNRTLL GEILNYYTHW SGSIKLTFMF CGSAMATGKF LLAYSPPGAG APTTRKEAML GTHVIWDVGL QSSCVLCIPW ISQTHYRYVV VDEYTAGGYI TCWYQTNIVV PADTQSDCKI LCFVSACNDF SVRMLKDTPF IKQDSFYQGP PGEAVERAIA RVADTISSGP VNSESIPALT AAETGHTSQV VPADTMQTRH VKNYHSRSES TVENFLCRSA CVYYTTYKNH GTDGDNFAYW VINTRQVAQL RRKLEMFTYA RFDLELTFVI TSTQEQSTIQ GQDSPVLTHQ IMYVPPGGPV PTKINSYSWQ TSTNPSVFWT EGSAPPRISI PFISIGNAYS MFYDGWAKFD KQGTYGINTL NNMGTLYMRH VNDGSPGPIV STVRIYFKPK HVKTWVPRPP RLCQYQKAGN VNFEPTGVTE SRTEITAMQT TGVLGQQTGA ICIGNYRVVN RHLATSEDWQ RCVWEDYNRD LLVSTTTAHG CDTIARCRCS TGVYFCASRN KHYPVSFEGP GLVEVQESEY YPKRYQSHVL LAAGFSEPGD CGGILRCEHG VIGLVTMGGE GVVGFADVRD LLWLEDDAME QGVKDYVEQL GNAFGSGFTN QICEQVNLLK ESLVGQDSIL EKSLKALVKI ISALVIVVRN HDDLVTITAT LALIGCTSSP WRWLKQKVSQ YYGIPMAERQ NNNWLKKFTE MTNACKGMEW IAVKIQKFID WLKVKILPEV KEKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL NSSVYSLPPD PDHFDGYKQQ AVVIMDDLCQ NPDGGDISLF CQMVSSVDFV PPMAALEEKG ILFTSPFVLA STNAGSINAP TVSDSRALAR RFHFDMNIEV ISMYSQNGKI NMPMSVRTCD EECCPVNFKR CCPLVCGKAI QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GATLEALFQG PPIYREIKIS VAPDTPPPPA IADLLKSVDS EAVREYCREK GWLVPEINST LQIEKHVSRA FICLQALTTF VSVAGIIYII YKLFAGFQGA YTGMPNQKPK VPTLRQAKVQ GPAFEFAVAM MKRNSSTVKT EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVVDAK ELVDKDGTNL ELTLLKLSRN EKFRDIRGFL AKEEVEVNEA VLAINTSKFP NMYIPVGQVT DYGFLNLGGT PTKRMLMYNF PTRAGQCGGV LMSTGKVLGI HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKEAGLPVI NTPSKTKLEP SVFHQVFEGN KEPAVLRNGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSKKTKD LTKLKECMDK YGLNLPMVTY VKDELRSAEK VAKGKSRLIE ASSLNDSVAM RQTFGNLYKT FHLNPGIVTG SAVGCDPDLF WSKIPVLLDG HLIAFDYSGY DASLSPVWFA CLKLLLEKLG YTHKETNYID YLCNSHHLYR DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY GDDVIASYPW PIDASLLAEA GKDYGLIMTP ADKGECFNEV TWTNVTFLKR YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE HEYEEFIKKI RSVPVGRCLT LPAFSTLRRK WLDSF //