ID POLG_EC11G STANDARD; PRT; 2195 AA. AC P29813; Q66785; DT 01-APR-1993 (Rel. 25, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, 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 Echovirus 11 (strain Gregory). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornaviridae; OC Enterovirus. OX NCBI_TaxID=31705; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95282506; PubMed=7762294; RA Dahllund L., Nissinen L., Pulli T., Hyttinen V.P., Stanway G., RA Hyypiae T.; RT "The genome of echovirus 11."; RL Virus Res. 35:215-222(1995). RN [2] RP SEQUENCE OF 822-2195 FROM N.A. RX MEDLINE=91011360; PubMed=2170575; RA Auvinen P., Hyypiae T.; RT "Echoviruses include genetically distinct serotypes."; RL J. Gen. Virol. 71:2133-2139(1990). 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 -!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the CC poliovirus polyprotein. In other picornavirus reactions Glu may be CC substituted for Gln, and Ser or Thr for Gly. CC -!- CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the CC picornavirus polyprotein. In other picornavirus reactions Glu may CC be substituted for Gln, and Ser or Thr for Gly. CC -!- CATALYTIC ACTIVITY: N nucleoside triphosphate = N diphosphate + CC {RNA}(N). 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 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X80059; CAA56365.1; -. DR EMBL; D10582; BAA01439.1; -. DR PIR; A36642; GNNYEC. DR PDB; 1H8T; 11-JUL-02. DR MEROPS; C03.011; -. DR MEROPS; C03.022; -. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR004004; Calici_pol_hel. DR InterPro; IPR009003; Cys_Ser_trypsin. DR InterPro; IPR000199; Pept_3C_picorn. DR InterPro; IPR000081; Peptidase_C3. DR InterPro; IPR003138; Pico_P1A. DR InterPro; IPR002527; Pico_P2B. DR InterPro; IPR001676; Rhv. DR InterPro; IPR000605; RNA_helicase. DR InterPro; IPR007095; RNA_pol_DS_PS. DR InterPro; IPR001205; RNA_pol_P3D. DR InterPro; IPR007094; RNA_pol_PSvir. DR InterPro; IPR008975; Viral_cap_coat. DR Pfam; PF00548; Cys-protease-3C; 1. DR Pfam; PF02226; Pico_P1A; 1. DR Pfam; PF00947; Pico_P2A; 1. DR Pfam; PF01552; Pico_P2B; 1. DR Pfam; PF00073; rhv; 3. DR Pfam; PF00680; RNA_dep_RNA_pol; 1. DR Pfam; PF00910; RNA_helicase; 1. DR PRINTS; PR00918; CALICVIRUSNS. DR ProDom; PD001125; Cys_protease_3C; 1. DR ProDom; PD001306; Pico_P2A; 1. DR ProDom; PD001274; Pico_P2B; 1. DR SMART; SM00382; AAA; 1. KW Polyprotein; Coat protein; Core protein; Transferase; Myristate; KW RNA-directed RNA polymerase; Hydrolase; Thiol protease; 3D-structure; KW Lipoprotein. FT CHAIN 2 69 COAT PROTEIN VP4. FT CHAIN 70 331 COAT PROTEIN VP2. FT CHAIN 332 569 COAT PROTEIN VP3. FT CHAIN 570 861 COAT PROTEIN VP1. FT CHAIN 862 1011 PICORNAIN 2A. FT CHAIN 1012 1110 CORE PROTEIN P2B. FT CHAIN 1111 1439 CORE PROTEIN P2C. FT CHAIN 1440 1528 CORE PROTEIN P3A. FT CHAIN 1529 1550 GENOME-LINKED PROTEIN VPG. FT CHAIN 1551 1733 PICORNAIN 3C. FT CHAIN 1734 2195 RNA-DIRECTED RNA POLYMERASE. FT LIPID 2 2 N-myristoyl glycine (in host) (By FT similarity). FT ACT_SITE 1697 1697 PROTEASE 3C (POTENTIAL). FT ACT_SITE 1711 1711 PROTEASE 3C (POTENTIAL). FT CONFLICT 823 827 RLCQY -> SYANT (IN REF. 2). SQ SEQUENCE 2195 AA; 245405 MW; 1CFC5DF288831AF0 CRC64; MGAQVSTQKT GAHETGLNAS GSSIIHYTNI NYYKDAASNS ANRQEFSQDP GKFTEPVKDI MVKSLPALNS PSAEECGYSD RVRSITLGNS TITTQESANV VVGYGRWPEY LKDNEATAED QPTQPDVATC RFYTLESVTW ERDSPGWWWK FPDALKDMGL FGQNMYYHYL GRAGYTLHVQ CNASKFHQGC LLVVCVPEAE MGCSQVDGTV NEHGLSEGET AKKFSSTSTN GTNTVQTIVT NAGMGVGVGN LTIYPHQWIN LRTNNCATIV MPYINNVPMD NMFRHHNFTL MIIPFVPLDY SSDSSTYVPI TVTVAPMCAE YNGLRLSTSL QGLPVMNTPG SNQFLTSDDF QSPSAMPQFD VTPELNIPGE VQNLMEIAEV DSVVPVNNVE GKLDTMEVYR IPVQSGNHQS DQVFGFQVQP GLDSVFKHTL LGEILNYFAH WSGSIKLTFV FCGSAMATGK FLLAYAPPGA NAPKNRKDAM LGTHIIWDVG LQSSCVLCVP WISQTHYRLV QQDEYTSAGN VTCWYQTGIV VPAGTPTSCS IMCFVSACND FSVRLLKDTP FIEQTALLQG DVVEAVENAV ARVADTIGSG PSNSQAVPAL TAVETGHTSQ VTPSDTMQTR HVKNYHSRSE SSIENFLSRS ACVYMGGYHT TNTDQTKLFA SWTISARRMV QMRRKLEIFT YVRFDVEVTF VITSKQDQGS RLGQDMPPLT HQIMYIPPGG PIPKSVTDYA WQTSTNPSIF WTEGNAPPRM SIPFISIGNA YSNFYDGWSH FSQNGVYGYN TLNHMGQIYV RHVNGSSPLP MTSTVRMYFK PKHVKAWVPR PPRLCQYKNA STVNFTPTNV TDKRTSINYI PETVKPDLSN YGAFGYQSGA VYVVNYRVVN RHLATHTDWQ NCVWEDYNRD LLISTTTAHG CDVIARCRCS TGVYYCQSKG KHYPVNFEGP GLVEVQESEY YPKRYQSHVL LAAGFSEPGD CGGILRCEHG VIGIVTMGGE GVVGFADVRD LLWLEDDAME QGVKDYVEQL GNAFGSGFTN QICEQVNLLK ESLVGQDSIL EKSLKALVKI ISALVIVVRN HDDLITVTAT LALIGCTSSP WRWLKQKVSQ YYGIPMAERQ NNGWLKKFTE MTNSCKGMEW ISIKIQKFIE WLKVKILPEV REKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYASEAKR VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL NSSVYTLPPD PDHFDGYKQQ AVVIVDDLCQ NPDGKDVSLF CQMVSSVDFV PPMAALEEKG ILFTSLFVLA STNAGSINAP TVSDSRALAR RFHFDMNIEV ISMYSQNGKI NMPMSEKTCD EECCPVNFKR CCPLVCGKAI QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GATLEALFQG PPIYREIKIS VAPETPPPPA IADLLKSVDS EAVREYCKEK GWLVPEVNST LQIEKHVSRA FICLQALTTF VSVAGIIYII YKLFAGFQGA YTGMPNQKPK VPTLRQAKVQ GPAFEFAVAM MKRNSSTVKT EYREFTMLGI YDRWAVLPRH AKPGPTILMN NQEVGVLDAK ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AKEEVEANQA VLAINTSKFP NMYIPVGQVT DYGFLNLGGT PTKRMLMSNF PTRAGQCGGV LMSTGKVLGI HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPII NTPSKTKLEP SVFHQVFEGD KEPAVLRNGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA VDHYAGQLAT LDISTEPMRL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSRRTRD LTKLKECMDK YGLNLPMVTY VKDELRSADK VAKGKSRLIE ASSLNDSVAM RQTFGNLYRT FHLNPGIVTG SAVGCDPDLF WSKIPVMLDG HLIAFDYSGY DASLSPVWFA CLKLLLEKLG YTHKETNYID YLCNSHHLYR DKHYFERGGM PSGYSGTSMF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY GDDVIASYPW PIDASLLAET GKGYGLIMTP ADKGECFNEV TWTNVTFLKR YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE HEYEEFIRKI RSVPVGRCLT LPAFSTLRRK WLDSF //