ID POLG_EC11G Reviewed; 2195 AA. AC P29813; Q66785; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 29-MAY-2007, entry version 73. DE Genome polyprotein [Contains: Capsid protein VP4 (P1A) (Virion protein DE 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 DE (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); DE Picornain 2A (EC 3.4.22.29) (Core protein P2A); Core protein P2B; Core DE protein P2C; Core protein P3A; Genome-linked protein VPg (P3B); DE Picornain 3C (EC 3.4.22.28) (Protease 3C) (P3C); RNA-directed RNA DE 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; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX MEDLINE=95282506; PubMed=7762294; DOI=10.1016/0168-1702(94)00104-K; 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 NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 822-2195. RX MEDLINE=91011360; PubMed=2170575; RA Auvinen P., Hyypiae T.; RT "Echoviruses include genetically distinct serotypes."; RL J. Gen. Virol. 71:2133-2139(1990). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-859. RC STRAIN=Isolate clinical EV11-207; RX PubMed=12097583; DOI=10.1128/JVI.76.15.7694-7704.2002; RA Stuart A.D., McKee T.A., Williams P.A., Harley C., Shen S., RA Stuart D.I., Brown T.D., Lea S.M.; RT "Determination of the structure of a decay accelerating factor-binding RT clinical isolate of echovirus 11 allows mapping of mutants with RT altered receptor requirements for infection."; RL J. Virol. 76:7694-7704(2002). CC -!- FUNCTION: Capsid proteins VP1, VP2, VP3 and VP4 form a closed CC capsid enclosing the viral positive strand RNA genome. VP4 lies on CC the inner surface of the protein shell formed by VP1, VP2 and VP3. CC All the three latter proteins contains a beta-sheet structure CC called beta-barrel jelly roll (By similarity). CC -!- FUNCTION: P2A and P3C polypeptides are cysteine proteases that CC cleave at certain Gln-|-Gly and Tyr-|-Gly sites in the CC polyprotein. CC -!- FUNCTION: RNA-directed RNA polymerase replicates genomic and CC antigenomic RNA by recognizing replications specific signals. 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. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- PTM: VPg is covalently linked to the genomic RNA (By similarity). CC -!- PTM: Specific enzymatic cleavages yield mature proteins. Cleavage CC between VP4 and VP2 is autocatalytic; VP1/P2A is catalyzed by P2A; CC all other cleavages are catalyzed by P3C (By similarity). CC -!- PTM: Myristoylation of VP4 is required during RNA encapsidation CC and formation of the mature virus particle (By similarity). CC -!- MISCELLANEOUS: The virus capsid is composed of 60 icosahedral CC units, each of which is composed of one copy each of proteins VP1, CC VP2, VP3, and VP4. CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family. CC -!- SIMILARITY: Contains 2 peptidase C3 domains. CC -!- SIMILARITY: Contains 1 RdRp catalytic domain. CC -!- SIMILARITY: Contains 1 SF3 helicase domain. 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; -; Genomic_RNA. DR EMBL; D10582; BAA01439.1; -; Genomic_RNA. DR PIR; A36642; GNNYEC. DR PDB; 1H8T; X-ray; A=570-860, B=70-331, C=332-569, D=1-69. DR PDB; 2C8I; EM; A/B/C/D=-. DR SMR; P29813; 862-1011. DR MEROPS; C03.011; -. DR MEROPS; C03.022; -. DR InterPro; IPR003593; AAA+_ATPase_core. DR InterPro; IPR000605; Helic_SF3_ssDNA/RNA_vir. DR InterPro; IPR000199; Pept_C3_picorn. DR InterPro; IPR004004; Pept_Calici. DR InterPro; IPR009003; Pept_Ser_Cys. DR InterPro; IPR000081; Peptidase_C3. DR InterPro; IPR011565; Peptidase_C3_2. DR InterPro; IPR003138; Pico_P1A. DR InterPro; IPR002527; Pico_P2B. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR001205; RNA_pol_P3D. DR InterPro; IPR007094; RNA_pol_PSvir. DR Gene3D; G3DSA:1.20.960.20; G3DSA:1.20.960.20; 1. DR Gene3D; G3DSA:2.40.10.10; G3DSA:2.40.10.10; 2. DR Gene3D; G3DSA:2.60.120.20; G3DSA:2.60.120.20; 3. DR Gene3D; G3DSA:3.30.70.270; G3DSA:3.30.70.270; 1. DR Gene3D; G3DSA:4.10.880.10; G3DSA:4.10.880.10; 2. DR Pfam; PF08727; P3A; 1. DR Pfam; PF00548; Peptidase_C3; 1. DR Pfam; PF02226; Pico_P1A; 1. DR Pfam; PF00947; Pico_P2A; 1. DR Pfam; PF01552; Pico_P2B; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00073; Rhv; 3. DR Pfam; PF00910; RNA_helicase; 1. DR PRINTS; PR00918; CALICVIRUSNS. DR ProDom; PD001125; Pept_C3_picorn; 1. DR ProDom; PD001306; Peptidase_C3_2; 1. DR ProDom; PD001274; Pico_P2B; 1. DR SMART; SM00382; AAA; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. KW 3D-structure; Capsid protein; Core protein; KW Covalent protein-RNA linkage; Hydrolase; Lipoprotein; Myristate; KW Nucleotide-binding; Nucleotidyltransferase; Protease; RNA replication; KW RNA-directed RNA polymerase; Thiol protease; Transferase; KW Virion protein. FT INIT_MET 1 1 Removed; by host (By similarity). FT CHAIN 2 69 Capsid protein VP4. FT /FTId=PRO_0000039703. FT CHAIN 70 331 Capsid protein VP2. FT /FTId=PRO_0000039704. FT CHAIN 332 569 Capsid protein VP3. FT /FTId=PRO_0000039705. FT CHAIN 570 861 Capsid protein VP1. FT /FTId=PRO_0000039706. FT CHAIN 862 1011 Picornain 2A. FT /FTId=PRO_0000039707. FT CHAIN 1012 1110 Core protein P2B. FT /FTId=PRO_0000039708. FT CHAIN 1111 1439 Core protein P2C. FT /FTId=PRO_0000039709. FT CHAIN 1440 1528 Core protein P3A. FT /FTId=PRO_0000039710. FT CHAIN 1529 1550 Genome-linked protein VPg. FT /FTId=PRO_0000039711. FT CHAIN 1551 1733 Picornain 3C. FT /FTId=PRO_0000039712. FT CHAIN 1734 2195 RNA-directed RNA polymerase. FT /FTId=PRO_0000039713. FT DOMAIN 1215 1371 SF3 helicase. FT DOMAIN 1960 2076 RdRp catalytic. FT ACT_SITE 882 882 For picornain 2A activity (By FT similarity). FT ACT_SITE 900 900 For picornain 2A activity (By FT similarity). FT ACT_SITE 971 971 For picornain 2A activity (By FT similarity). FT ACT_SITE 1590 1590 For picornain 3C activity (Potential). FT ACT_SITE 1621 1621 For picornain 3C activity (Potential). FT ACT_SITE 1697 1697 For picornain 3C activity (By FT similarity). FT BINDING 1531 1531 5'-phospho-RNA (covalent) (By FT similarity). FT LIPID 2 2 N-myristoyl glycine; by host (By FT similarity). FT CONFLICT 823 827 RLCQY -> SYANT (in Ref. 2). FT STRAND 4 7 FT STRAND 26 29 FT HELIX 36 38 FT TURN 43 44 FT HELIX 50 52 FT TURN 53 53 FT STRAND 57 58 FT STRAND 83 87 FT TURN 88 89 FT STRAND 90 94 FT STRAND 100 102 FT TURN 103 104 FT TURN 113 115 FT STRAND 123 123 FT HELIX 126 128 FT TURN 129 129 FT STRAND 133 134 FT STRAND 138 140 FT TURN 142 143 FT STRAND 147 150 FT TURN 153 154 FT TURN 156 157 FT HELIX 159 167 FT STRAND 168 180 FT TURN 185 186 FT STRAND 188 197 FT TURN 198 198 FT STRAND 203 203 FT TURN 206 207 FT STRAND 210 210 FT HELIX 212 215 FT STRAND 222 223 FT STRAND 225 225 FT STRAND 233 233 FT STRAND 235 235 FT STRAND 238 238 FT HELIX 239 241 FT TURN 242 245 FT HELIX 248 253 FT STRAND 256 260 FT TURN 261 263 FT STRAND 266 271 FT STRAND 280 280 FT TURN 282 284 FT STRAND 285 285 FT STRAND 288 299 FT STRAND 308 324 FT TURN 339 342 FT TURN 346 347 FT STRAND 354 354 FT TURN 357 358 FT STRAND 370 371 FT STRAND 373 373 FT HELIX 374 378 FT TURN 379 379 FT STRAND 382 383 FT TURN 386 387 FT STRAND 389 389 FT TURN 390 391 FT TURN 393 394 FT HELIX 396 399 FT STRAND 401 405 FT TURN 409 410 FT STRAND 412 417 FT TURN 420 422 FT HELIX 424 427 FT TURN 428 428 FT HELIX 430 435 FT TURN 436 437 FT STRAND 438 442 FT STRAND 445 451 FT TURN 455 456 FT STRAND 458 466 FT HELIX 476 479 FT TURN 480 481 FT STRAND 483 488 FT STRAND 494 499 FT STRAND 508 509 FT TURN 515 516 FT STRAND 520 530 FT TURN 533 534 FT STRAND 538 547 FT TURN 549 550 FT STRAND 552 556 FT TURN 560 561 FT TURN 572 573 FT STRAND 582 582 FT STRAND 586 586 FT TURN 598 599 FT STRAND 600 601 FT HELIX 603 605 FT HELIX 613 616 FT STRAND 622 622 FT STRAND 627 627 FT HELIX 629 631 FT STRAND 632 632 FT HELIX 633 637 FT STRAND 641 649 FT HELIX 656 658 FT STRAND 659 663 FT HELIX 670 676 FT TURN 677 678 FT STRAND 679 696 FT STRAND 710 716 FT TURN 718 719 FT TURN 726 727 FT HELIX 729 732 FT STRAND 738 742 FT TURN 743 744 FT STRAND 749 752 FT STRAND 761 762 FT STRAND 767 768 FT TURN 771 772 FT STRAND 777 777 FT HELIX 779 782 FT STRAND 787 792 FT STRAND 801 819 FT STRAND 844 844 FT TURN 847 848 SQ SEQUENCE 2195 AA; 245407 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 //