ID POLG_SVDVU STANDARD; PRT; 2185 AA. AC P13900; Q84794; Q84795; Q84796; Q84797; Q84798; Q84799; Q84800; AC Q84801; Q84802; Q84803; Q84804; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE GENOME POLYPROTEIN [CONTAINS: COAT PROTEINS VP1 TO VP4; CORE PROTEINS DE P2A TO P2C, P3A; GENOME-LINKED PROTEIN VPG; PICORNAIN 3C DE (EC 3.4.22.28) (PROTEASE 3C) (P3C); RNA-DIRECTED RNA POLYMERASE P3D DE (EC 2.7.7.48)]. OS Swine vesicular disease virus (strain UKG/27/72). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornaviridae; OC Enterovirus. OX NCBI_TaxID=12077; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90364770; PubMed=2168111; RA Seechurn P., Knowles N.J., McCauley J.W.; RT "The complete nucleotide sequence of a pathogenic swine vesicular RT disease virus."; RL Virus Res. 16:255-274(1990). CC -!- FUNCTION: IT IS THOUGHT THAT THE P2C PROTEIN ATTACHES TO VESICULAR CC MEMBRANES AND IS ASSOCIATED WITH VIRAL RNA SYNTHESIS. CC -!- FUNCTION: P3C POLYPEPTIDE IS A PROTEASE THAT CLEAVES AT CERTAIN CC Q/G SITES IN THE POLYPROTEIN. IT MAY BE A CYSTEINE PROTEASE. 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 -!- SIMILARITY: THE 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; X54521; CAA38377.1; -. DR PIR; A30061; GNNYSV. DR PIR; S11670; S11670. DR HSSP; P03313; 1COV. DR MEROPS; C03.001; -. DR MEROPS; C03.020; -. 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; KW RNA-directed RNA polymerase; Hydrolase; Thiol protease; Myristate. FT CHAIN 2 69 COAT PROTEIN VP4 (P1A). FT CHAIN 70 330 COAT PROTEIN VP2 (P1B). FT CHAIN 331 568 COAT PROTEIN VP3 (P1C). FT CHAIN 569 851 COAT PROTEIN VP1 (P1D). FT CHAIN 852 1001 CORE PROTEIN P2A (P2-3B). FT CHAIN 1002 1100 CORE PROTEIN P2B (P2-5B). FT CHAIN 1101 1429 CORE PROTEIN P2C (P2-X). FT CHAIN 1430 1518 CORE PROTEIN P3A (P3-1B). FT CHAIN 1519 1540 GENOME-LINKED PROTEIN VPG (P3B). FT CHAIN 1541 1723 PICORNAIN 3C. FT CHAIN 1724 2185 RNA-DEPENDENT RNA POLYMERASE P3D. FT LIPID 2 2 MYRISTATE (BY SIMILARITY). FT ACT_SITE 1687 1687 PROTEASE (POTENTIAL). FT ACT_SITE 1701 1701 PROTEASE (POTENTIAL). SQ SEQUENCE 2185 AA; 243363 MW; C9B103052934E1B8 CRC64; MGAQVSTQKT GAHETSLSAA GNSVIHYTNI NYYKDAASNS ANRQDFTQDP GKFTEPVKDI MVKSMPALNS PSAEECGYSD RVRSITLGNS TITTQECANV VVGYGVWPTY LKDEEATAED QPTQPDVATC RFYTLESVMW QQSSPGWWWK FPDALSNMGL FGQNMQYHYL GRAGYTIHVQ CNASKFHQGC LLVVCVPEAE MGCATLANKP DPKSLSKGEI ANMFESQNST GETAVQANVI NAGMGVGVGN LTIFPHQWIN LRTNNSATIV MPYINSVPMD NMFRHNNFTL MVIPFAPLSY STGATTYVPI TVTVAPMCAE YNGLRLAGKQ GLPTLSTPGS NQFLTSDDFQ SPSAMPQFDV TPEMDIPGQV NNLMEIAEVD SVVPVNNTEG KVMSIEAYQI PVQSNPTNGS QVFGFPLTPG ANSVLNRTLL GEILNYYAHW SGSIKLTFMF CGSAMATGKF LLAYSPPGAG APTTRKEAML GTHVIWDVGL QSSCVLCIPW ISQTHYRYVV MDEYTAGGYI TCWYQTNIVV PADAQSDCKI LCFVSACNDF SVRMLKDTPF IKQDNFFQGP PGEVMGRAIA RVADTIGSGP VNSESIPALT AAETGHTSQV VPSDTMQTRH VKNYHSRSES TVENFLCRSA CVFYTTYKNH DSDGDNFAYW VINTRQVAQL RRKLEMFTYA RFDLELTFVI TSTQEQPTVR GQDAPVLTHQ IMYVPPGGPV PTKVNSYSWQ TSTNPSVFWT EGSAPPRMSI PFIGIGNAYS MFYDGWARFD KQGTYGISTL NNMGTLYMRH VNDGGPGPIV STVRIYFKPK HVKTWVPRPP RLCQYQKAGN VNFEPTGVTE GRTDITTMKT TGAFGQQSGA VYVGNYRVVN RHLATRADWQ NCVWEDYNRD LLVSTTTAHG CDTIARCDCT AGVYFCASRN KHYPVTFEGP GLVEVQESEY YPKKYQSHVL LAAGFAEPGD CGGILRCQHG VIGIVTVGGE GVVGFADVRD LLWLEDDAME QGVRDYVEQL GNCFGSGFTN QICEQVTLLK ESLIGQDSIL EKSLKALVKI VSALVIVVRN HDDLITVTAT LALIGCTTSP WRWLKQKVSQ YYGIPMAERQ NSGWLKKFTE MTNACKGMEW IAIKIQKFIE WLKVKILPEV KEKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL NSSVYSLPPD PDHFDGYKQQ AVVIMDDLCQ NPDGKDVSLF CQMVSSVDFV PPMAALEEKG ILFTSPFVLA STNAGSVNAP TVSDSRALVR RFHFDMNIEV VSMYSQNGKI NMPMAVKTCD EECCPVNFKK CCPLVCGKAI QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GATLEALFQG PPVYREIKIS VAPETPPPPA VADLLKSVDS EAVREYCKEK GWLIPEVDST LQIEKHVNRA FICLQALTTF VSVAGIIYII YKLFAGFQGA YTGMPNQKPR VPTLRQAKVQ GPAFEFAVAM MKRNASTVKT EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQVVGVLDAK ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AREEVEVNEA VLAINTSKFP NMYIPVGRVT DYGFLNLGGT PTKRMLMYNF PTRAGQCGGV LMSTGKVLGI HVGGNGHQGF SAALLRHYFN EEQGEIEFIE SSKDAGFPVI NTPSKTKLEP SVFHHVFEGN KEPAVLRNGD PRLKANFEEA IFSKYIGNVN THVDEYMMEA VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSKKTRD LTKLKECMDK YGLNLPMVTY VKDELRSADK VAKGKSRLIE ASSLNDSVAM RQTFGNLYKT FHLNPGIVTG SAVGCDPDVF WSKIPVMLDG HLIAFDYSGY DASLSPVWFT CLKLLLEKLG YTNKETNYID YLCNSHHLYR DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY GDDVIASYPW PIDASLLAEA GKDYGLIMTP ADKGECFNEV TWTNVTFLKR YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE HEYEEFIRKI RSVRVGRCLS LPAFSTLRRK WLDSF //