ID POLG_CXB1J STANDARD; PRT; 2182 AA. AC P08291; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, 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 B1 (strain Japan). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornaviridae; OC Enterovirus. OX NCBI_TaxID=103902; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87122157; PubMed=3027969; RA Iizuka N., Kuge S., Nomoto A.; RT "Complete nucleotide sequence of the genome of coxsackievirus B1."; RL Virology 156:64-73(1987). 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; M16560; AAC00531.1; -. DR PIR; A26353; GNNYB1. 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 70 332 COAT PROTEIN VP2. FT CHAIN 333 570 COAT PROTEIN VP3. FT CHAIN 571 848 COAT PROTEIN VP1. FT CHAIN 849 998 PICORNAIN 2A. FT CHAIN 999 1097 CORE PROTEIN P2B. FT CHAIN 1098 1426 CORE PROTEIN P2C. FT CHAIN 1427 1515 CORE PROTEIN P3A. FT CHAIN 1516 1537 GENOME-LINKED PROTEIN VPG. FT CHAIN 1538 1720 PICORNAIN 3C. FT CHAIN 1721 2182 RNA-DIRECTED RNA POLYMERASE. FT LIPID 2 2 MYRISTATE (BY SIMILARITY). FT ACT_SITE 1684 1684 PROTEASE 3C (POTENTIAL). FT ACT_SITE 1698 1698 PROTEASE 3C (POTENTIAL). SQ SEQUENCE 2182 AA; 243945 MW; 387B9391275859B1 CRC64; MGAQVSTQKT GAHETGLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP GKFTEPVKDI MIKSMPALNS PSAEECGYSD RVRSITLGNS TITTQECANV VVGYGVWPEY LKDNEATGED QPTQPDVATC RFYTLESVQW MKNSAGWWWK LPDALSQMGL FGQNMQYHYL GRTGYTIHVQ CNASKFHQGC LLVVCVPEAE MGCSNLNNTP KFAELSGGDN ARMFTDTEVG TSNDKKVQTA VWNAGMGVGV GNLTIFPHQW INLRTNNSAT IVMPYINSVP MDNMYRHNNL TLMIIPFVPL NYSEGSSPYV PITVTIAPMC AEYNGLRLAS SQGLPVMTTP GSTQFLTSDD FQSPSAMPQF DVTPEMQIPG RVNNLMEIAE VDSVVPVNNT DNNVNGLKAY QIPVQSNSDN RRQVFGFPLQ PGANNVLNRT LLGEILNYYT HWSGSIKLTF MFCGSAMATG KFLLAYSPPG AGVPKNRRDA MLGTHVIWDV GLQSSCVLCV PWISQTHYRY VVEDEYTAAG YVTCWYQTNI IVPADVQSTC DILCFVSACN DFSVRMLKDT PFIRQDNFYQ GPVEESVERA MVRVADTVSS KPTNSESIPA LTAAETGHTS QVVPSDTMQT RHVKNYHSRS ESSIENFLCR SACVYYATYN NNSEKGYAEW VINTRQVAQL LRRKLEFTYL RFDLELTFVI TSAQEPSTAT SVDAPVQTQQ IMYVPPGGPV PTKVTDYAWQ TSTNPSVFWT EGNAPPRMSI PFISIGNAYS CFYDGWTQFS RNGVYGINTL NNMGTLYMRH VNEAGQGPIK STVRIYFKPK HVKAWVPRPP RLCQYEKQKN VNFNPTGVTT TRSNITTTGA FGQQSGAVYV GNYRVVNRHL ATREDWQRCV WEDYNRDLLV STTTAHGCDI IARCQCTTGV YFCASRNKHY PVSFEGPGLV EVQESEYYPK RYQSHVLLAA GFSEPGDCGG ILRCEHGVVG IVTMGGEGVV GFADVRDLLW LEDDAMEQGV KDYVEQLGNA FGSGFTNQVC EQVNLLKESL VGQDSILEKS LKALVKIVSA LVIVVRNHDD LITVTATLAL IGCTSSPWRW LKQKVSQYYG IPMAERQNSG WLKKFTEMTN ACKGMEWIAI KIQKFIEWLK VKILPEVKEK HEFLNRLKQL PLLESQIATI EQSAPSQSDQ EQLFSNVQYF AHYCRKYAPL YAAEAKRVFS LEKKMSNYIQ FKSKCRIEPV CLLLHGSPGA GKSVATNLIG RSLAEKLNSS VYSLPPDPDH FDGYKQQAVV IMDDLCQNPD GKDVSLFCQM VSSVDFVPPM AALEEKGILF TSPFVLASTN AGSINAPTVS DSRALARRFH FDMNIEVISM YSQNGKINMP MSVKTCDEEC CPVNFKKCCP LVCGKAIQFI DRRTQVRYSL DMLVTEMFRE YNHRHSVGAT LEALFQGPPI YREIKISIAP ETPPPPAIAD LLKSVDSEAV REYCKEKGWL VPEINSTLQI EKHVSRAFIC LQALTTFVSV AGIIYIIYKL FAGFQGAYTG MPNQKPKVPT LRQAKVQGPV FEFAVAMMKR NSSTVKTEYG EFTMLGIYDR WAVLPRHAKP GPTILMNDQE IGVLDAKELV DKDGTNLELT LLKLNRNEKF RDIRGFLAKE EVEVNEAVLA INTSKFPNMY IPVGQVTEYG FLNLGGTPTK RMLMYNFPTR AGQCGGVLMS TGKVLGIHVG GNGHQGFSAA LLKHYFNDEQ GEIEFIESSK EAGFPVINTP SKTKLEPSVF HQVFEGNKEP AVLRNGDPRL RANFEEAIFS KYIGNVNTHV DEYMLEAVDH YAGQLATLDI STEPMRLEDA VYGTEGLEAL DLTTSAGYPY VALGIKKRDI LSKKTRDLTK LKECMDKYGL NLPMVTYVKD ELRSAEKVAK GKSRLIEASS LNDSVAMRQT FGNLYKTFHL NPGIVTGSAV GCDPDLFWSK IPVMLDGHLV AFDYSGYDAS LSPVWFACLK LLLEKLGYSH KETNYIDYLC NSHHLYRDKH YFVRGGMPSG CSGTSIFNSM INNIIIRTLM LKVYKGIDLD QFRMIAYGDD VIASYPWPID ASLLAEAGRD CGLIMTPADK GDCFNEVTWA NVTFLKRYFR ADEQYPFLVH PVMPMKDIHE SIRWTKDPKN TQDHVRSLCL LAWHNGEHEY EEFIRKIRSV PVGACLTLPA FSTLRRKWLD SF //