ID   POLG_CXB3W     STANDARD;      PRT;  2185 AA.
AC   Q66282;
DT   15-JUL-1999 (Rel. 38, Created)
DT   15-JUL-1999 (Rel. 38, 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 B3 (strain Woodruff).
OC   Viruses; ssRNA positive-strand viruses, no DNA stage; Picornaviridae;
OC   Enterovirus.
OX   NCBI_TaxID=103904;
RN   [1]
RP   SEQUENCE FROM N.A.
RA   Knowlton K.U., Jeon E.S., Berkley R.W., Wessely R., Huber S.;
RT   "A mutation in the puff region of VP2 attenuates the myocarditic
RT   phenotype of an infectious cDNA of the Woodruff virus.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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   --------------------------------------------------------------------------
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DR   EMBL; U57056; AAB02228.1; -.
DR   MEROPS; C03.011; -.
DR   MEROPS; C03.022; -.
DR   INTERPRO; IPR000081; -.
DR   INTERPRO; IPR000199; -.
DR   INTERPRO; IPR000605; -.
DR   INTERPRO; IPR001205; -.
DR   INTERPRO; IPR001643; -.
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.
DR   PRINTS; PR00918; CALICVIRUSNS.
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    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;  243680 MW;  FD93A677904252FA CRC64;
     MGAQVSTQKT GAHETGLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP SKFTEPVKDI
     MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV VVGYGVWPDY LKDSEATAED
     QPTQPDVATC RFYTLDSVQW QKTSPGWWWK LPDALSNLGL FGQNMQYHYL GRTGYTIHVQ
     CNASKFHQGC LLVVCVPEAE MGCATLNNTP SSAELLGGDS AKEFADKPVA SGSNKLVQRV
     VYNAGMGVGV GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL
     DYCPGSTTYV PITITIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD FQSPSAMPQY
     DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY QIPVRSNEGS GTQVFGFPLQ
     PGYSSVFSRT LLGEILNYYT HWSGSIKLTF MFCGSAMATG KFLLAYSPPG AGAPTKRVDA
     MLGTHVVWDV GLQSSCVLCI PWISQTHYRY VASDEYTAGG FITCWYQTNI VVPADAQSSC
     YIMCFVSACN DFSVRLLKDT PFISQQNFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA
     LTAAETGHTS QVVPSDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYE NSGAKRYAEW
     VITPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ NQDAQILTHQ IMYVPPGGPV
     PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSV PFLSIGNAYS NFYDGWSEFS RNGVYGINTL
     NNMGTLYARH VNAGSTGPIK STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFQPSGVTT
     TRQSITTMTN TGAFGQQSGA VYVGNYRVVN RHLATSADWQ NCVWENYNRD LLVSTTTAHG
     CDIIARCRCT TGVYFCASKN KHYPISFEGP GIVEVQESEY YPRRYQSHVL LAAGFSEPGD
     CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME QGVKDYVEQL GNAFGSGFTN
     QICEQVNLLK ESLVGQDSIL EKSLKALVKI ISALVIVVRN HDDLITVTAT LALIGCTSSP
     WRWLKQKVSQ YYGIPMAERQ NNGWLKKFTE MTNACKGMEW IAIKIQKFIE WLKVKILPEV
     REKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYASEAKR
     VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL NSSVYSLPPD
     PDHFDGYKQQ AVVIMDDLCQ KPDGKDVSLF CQMVSSVDFV PPMAALEEKG ILFTSPFVLA
     STNAGSINAP TVSDSRALAR RFHFDMNIEV ISMYSQNGKI NMPMSVKTCD EECCPVNFKK
     CCPLVCGKAI QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GATLEALFQG PPVYREIKIS
     VAPETPPPPR IADLLKSVDS EAVREYCKEK GWLVPEVNST LQIEKHVSRA FICLQAITTF
     VSVAGIIYII YKLFAGFQGA YTGIPNQKPK VPTLRQAKVQ GPAFEFAVAM MKRNSSTVKT
     EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK ELVDKDGTNL ELTLLKLNRN
     EKFRDIRGFL AKEEVEVNEA VLAINTSKFP NMYIPVGQVT DYGFLNLGGT PTKRMLMYNF
     PTRAGQCGGV LMSTGKVLGI HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKEAGFPII
     NTPSKTKLEP SVFHQVFEGD KEPAVLRNGD PRLKVNFEEA IFSKYIGNVN THVDEYMMEA
     VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSKKTRD
     LTKLKECMDK YGLNLPMVTY VKDELRSAEK VAKGKSRLIE ASSLNDSVAM RQTFGNLYKT
     FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG HLIAFDYSGY DASLSPVWFA CLKLLLEKLG
     YSHKETNYID YLCNSHHLYR DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI
     DLDQFRMIAY GDDVIASYPW PIDASLLAEA GKDYGLIMTP ADKGECFNEV TWTNVTFLKR
     YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE HEYEEFIRKI
     RSVPVGRCLT LPAFSTIRRK WLDSF
//