ID POLG_EC11G STANDARD; PRT; 2194 AA. AC P29813; Q66785; DT 01-APR-1993 (Rel. 25, Created) DT 13-SEP-2005 (Rel. 48, Last sequence update) DT 07-FEB-2006 (Rel. 49, 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) (Core protein P2A); Core protein P2B; Core protein P2C; DE Core protein P3A; Genome-linked protein VPg (P3B); Picornain 3C DE (EC 3.4.22.28) (Protease 3C) (P3C); RNA-directed RNA polymerase DE (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 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 821-2194. 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 1-858. 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: P2A and P3C polypeptides are cysteine proteases that CC cleave at certain Gln-|-Gly and Tyr-|-Gly sites in the CC polyprotein. 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: Contains 2 peptidase C3 domains. CC -!- SIMILARITY: Contains 1 RdRp catalytic 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=569-858, B=69-329, C=331-568, D=1-68. DR MEROPS; C03.011; -. DR MEROPS; C03.022; -. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR000199; Pept_C3_picorn. DR InterPro; IPR004004; Pept_Calici. DR InterPro; IPR000081; Peptidase_C3. DR InterPro; IPR011565; Peptidase_C3_2. 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 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. KW 3D-structure; Capsid protein; Core protein; KW Covalent protein-RNA linkage; Hydrolase; Lipoprotein; Myristate; KW Nucleotidyltransferase; Polyprotein; Protease; KW RNA-directed RNA polymerase; Structural protein; Thiol protease; KW Transferase. FT INIT_MET 0 0 By similarity. FT CHAIN 1 68 Coat protein VP4. FT /FTId=PRO_0000039703. FT CHAIN 69 330 Coat protein VP2. FT /FTId=PRO_0000039704. FT CHAIN 331 568 Coat protein VP3. FT /FTId=PRO_0000039705. FT CHAIN 569 860 Coat protein VP1. FT /FTId=PRO_0000039706. FT CHAIN 861 1010 Picornain 2A. FT /FTId=PRO_0000039707. FT CHAIN 1011 1109 Core protein P2B. FT /FTId=PRO_0000039708. FT CHAIN 1110 1438 Core protein P2C. FT /FTId=PRO_0000039709. FT CHAIN 1439 1527 Core protein P3A. FT /FTId=PRO_0000039710. FT CHAIN 1528 1549 Genome-linked protein VPg. FT /FTId=PRO_0000039711. FT CHAIN 1550 1732 Picornain 3C. FT /FTId=PRO_0000039712. FT CHAIN 1733 2194 RNA-directed RNA polymerase. FT /FTId=PRO_0000039713. FT DOMAIN 1959 2075 RdRp catalytic. FT ACT_SITE 881 881 Picornain 2A (By similarity). FT ACT_SITE 899 899 Picornain 2A (By similarity). FT ACT_SITE 970 970 Picornain 2A (By similarity). FT ACT_SITE 1589 1589 Picornain 3C (Potential). FT ACT_SITE 1620 1620 Picornain 3C (Potential). FT ACT_SITE 1696 1696 Picornain 3C (By similarity). FT BINDING 1530 1530 5'-phospho-RNA (covalent) (By FT similarity). FT LIPID 1 1 N-myristoyl glycine (by host) (By FT similarity). FT CONFLICT 822 826 RLCQY -> SYANT (in Ref. 2). FT STRAND 3 6 FT STRAND 25 28 FT HELIX 35 37 FT TURN 42 43 FT HELIX 49 51 FT TURN 52 52 FT STRAND 56 57 FT STRAND 82 86 FT TURN 87 88 FT STRAND 89 93 FT STRAND 99 101 FT TURN 102 103 FT TURN 112 114 FT STRAND 122 122 FT HELIX 125 127 FT TURN 128 128 FT STRAND 132 133 FT STRAND 137 139 FT TURN 141 142 FT STRAND 146 149 FT TURN 152 153 FT TURN 155 156 FT HELIX 158 166 FT STRAND 167 179 FT TURN 184 185 FT STRAND 187 196 FT TURN 197 197 FT STRAND 202 202 FT TURN 205 206 FT STRAND 209 209 FT HELIX 211 214 FT STRAND 221 222 FT STRAND 224 224 FT STRAND 232 232 FT STRAND 234 234 FT STRAND 237 237 FT HELIX 238 240 FT TURN 241 244 FT HELIX 247 252 FT STRAND 255 259 FT TURN 260 262 FT STRAND 265 270 FT STRAND 279 279 FT TURN 281 283 FT STRAND 284 284 FT STRAND 287 298 FT STRAND 307 323 FT TURN 338 341 FT TURN 345 346 FT STRAND 353 353 FT TURN 356 357 FT STRAND 369 370 FT STRAND 372 372 FT HELIX 373 377 FT TURN 378 378 FT STRAND 381 382 FT TURN 385 386 FT STRAND 388 388 FT TURN 389 390 FT TURN 392 393 FT HELIX 395 398 FT STRAND 400 404 FT TURN 408 409 FT STRAND 411 416 FT TURN 419 421 FT HELIX 423 426 FT TURN 427 427 FT HELIX 429 434 FT TURN 435 436 FT STRAND 437 441 FT STRAND 444 450 FT TURN 454 455 FT STRAND 457 465 FT HELIX 475 478 FT TURN 479 480 FT STRAND 482 487 FT STRAND 493 498 FT STRAND 507 508 FT TURN 514 515 FT STRAND 519 529 FT TURN 532 533 FT STRAND 537 546 FT TURN 548 549 FT STRAND 551 555 FT TURN 559 560 FT TURN 571 572 FT STRAND 581 581 FT STRAND 585 585 FT TURN 597 598 FT STRAND 599 600 FT HELIX 602 604 FT HELIX 612 615 FT STRAND 621 621 FT STRAND 626 626 FT HELIX 628 630 FT STRAND 631 631 FT HELIX 632 636 FT STRAND 640 648 FT HELIX 655 657 FT STRAND 658 662 FT HELIX 669 675 FT TURN 676 677 FT STRAND 678 695 FT STRAND 709 715 FT TURN 717 718 FT TURN 725 726 FT HELIX 728 731 FT STRAND 737 741 FT TURN 742 743 FT STRAND 748 751 FT STRAND 760 761 FT STRAND 766 767 FT TURN 770 771 FT STRAND 776 776 FT HELIX 778 781 FT STRAND 786 791 FT STRAND 800 818 FT STRAND 843 843 FT TURN 846 847 SQ SEQUENCE 2194 AA; 245276 MW; 7195C2367239C681 CRC64; GAQVSTQKTG AHETGLNASG SSIIHYTNIN YYKDAASNSA NRQEFSQDPG KFTEPVKDIM VKSLPALNSP SAEECGYSDR VRSITLGNST ITTQESANVV VGYGRWPEYL KDNEATAEDQ PTQPDVATCR FYTLESVTWE RDSPGWWWKF PDALKDMGLF GQNMYYHYLG RAGYTLHVQC NASKFHQGCL LVVCVPEAEM GCSQVDGTVN EHGLSEGETA KKFSSTSTNG TNTVQTIVTN AGMGVGVGNL TIYPHQWINL RTNNCATIVM PYINNVPMDN MFRHHNFTLM IIPFVPLDYS SDSSTYVPIT VTVAPMCAEY NGLRLSTSLQ GLPVMNTPGS NQFLTSDDFQ SPSAMPQFDV TPELNIPGEV QNLMEIAEVD SVVPVNNVEG KLDTMEVYRI PVQSGNHQSD QVFGFQVQPG LDSVFKHTLL GEILNYFAHW SGSIKLTFVF CGSAMATGKF LLAYAPPGAN APKNRKDAML GTHIIWDVGL QSSCVLCVPW ISQTHYRLVQ QDEYTSAGNV TCWYQTGIVV PAGTPTSCSI MCFVSACNDF SVRLLKDTPF IEQTALLQGD VVEAVENAVA RVADTIGSGP SNSQAVPALT AVETGHTSQV TPSDTMQTRH VKNYHSRSES SIENFLSRSA CVYMGGYHTT NTDQTKLFAS WTISARRMVQ MRRKLEIFTY VRFDVEVTFV ITSKQDQGSR LGQDMPPLTH QIMYIPPGGP IPKSVTDYAW QTSTNPSIFW TEGNAPPRMS IPFISIGNAY SNFYDGWSHF SQNGVYGYNT LNHMGQIYVR HVNGSSPLPM TSTVRMYFKP KHVKAWVPRP PRLCQYKNAS TVNFTPTNVT DKRTSINYIP ETVKPDLSNY GAFGYQSGAV YVVNYRVVNR HLATHTDWQN CVWEDYNRDL LISTTTAHGC DVIARCRCST GVYYCQSKGK HYPVNFEGPG LVEVQESEYY PKRYQSHVLL AAGFSEPGDC GGILRCEHGV IGIVTMGGEG VVGFADVRDL LWLEDDAMEQ GVKDYVEQLG NAFGSGFTNQ ICEQVNLLKE SLVGQDSILE KSLKALVKII SALVIVVRNH DDLITVTATL ALIGCTSSPW RWLKQKVSQY YGIPMAERQN NGWLKKFTEM TNSCKGMEWI SIKIQKFIEW LKVKILPEVR EKHEFLNRLK QLPLLESQIA TIEQSAPSQS DQEQLFSNVQ YFAHYCRKYA PLYASEAKRV FSLEKKMSNY IQFKSKCRIE PVCLLLHGSP GAGKSVATNL IGRSLAEKLN SSVYTLPPDP DHFDGYKQQA VVIVDDLCQN PDGKDVSLFC QMVSSVDFVP PMAALEEKGI LFTSLFVLAS TNAGSINAPT VSDSRALARR FHFDMNIEVI SMYSQNGKIN MPMSEKTCDE ECCPVNFKRC CPLVCGKAIQ FIDRRTQVRY SLDMLVTEMF REYNHRHSVG ATLEALFQGP PIYREIKISV APETPPPPAI ADLLKSVDSE AVREYCKEKG WLVPEVNSTL QIEKHVSRAF ICLQALTTFV SVAGIIYIIY KLFAGFQGAY TGMPNQKPKV PTLRQAKVQG PAFEFAVAMM KRNSSTVKTE YREFTMLGIY DRWAVLPRHA KPGPTILMNN QEVGVLDAKE LVDKDGTNLE LTLLKLNRNE KFRDIRGFLA KEEVEANQAV LAINTSKFPN MYIPVGQVTD YGFLNLGGTP TKRMLMSNFP TRAGQCGGVL MSTGKVLGIH VGGNGHQGFS AALLKHYFND EQGEIEFIES SKDAGFPIIN TPSKTKLEPS VFHQVFEGDK EPAVLRNGDP RLKANFEEAI FSKYIGNVNT HVDEYMLEAV DHYAGQLATL DISTEPMRLE DAVYGTEGLE ALDLTTSAGY PYVALGIKKR DILSRRTRDL TKLKECMDKY GLNLPMVTYV KDELRSADKV AKGKSRLIEA SSLNDSVAMR QTFGNLYRTF HLNPGIVTGS AVGCDPDLFW SKIPVMLDGH LIAFDYSGYD ASLSPVWFAC LKLLLEKLGY THKETNYIDY LCNSHHLYRD KHYFERGGMP SGYSGTSMFN SMINNIIIRT LMLKVYKGID LDQFRMIAYG DDVIASYPWP IDASLLAETG KGYGLIMTPA DKGECFNEVT WTNVTFLKRY FRADEQYPFL VHPVMPMKDI HESIRWTKDP KNTQDHVRSL CLLAWHNGEH EYEEFIRKIR SVPVGRCLTL PAFSTLRRKW LDSF //