ID C3U5A5_9PICO Unreviewed; 2318 AA. AC C3U5A5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 06-MAR-2013, entry version 28. DE SubName: Full=Polyprotein; DE Flags: Fragment; GN Name=gp1; OS Saffold virus. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; OC Picornaviridae; Cardiovirus. OX NCBI_TaxID=434309; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pak5152; RX PubMed=19193786; DOI=10.1128/JVI.02085-08; RA Blinkova O., Kapoor A., Victoria J., Jones M., Wolfe N., Naeem A., RA Shaukat S., Sharif S., Alam M.M., Angez M., Zaidi S., Delwart E.L.; RT "Cardioviruses are genetically diverse and cause common enteric RT infections in South Asian children."; RL J. Virol. 83:4631-4641(2009). CC -!- FUNCTION: Protein 2C associates with and induces structural CC rearrangements of intracellular membranes. It displays RNA- CC binding, nucleotide binding and NTPase activities (By similarity). CC -!- FUNCTION: Protein 3C is a cysteine protease that generates mature CC viral proteins from the precursor polyprotein. In addition to its CC proteolytic activity, it binds to viral RNA, and thus influences CC viral genome replication. RNA and substrate bind co-operatively to CC the protease (By similarity). CC -!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic CC and antigenomic RNA by recognizing replications specific signals CC (By similarity). CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). 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 -!- SUBCELLULAR LOCATION: Picornain 3C: Host cytoplasm (By CC similarity). CC -!- SUBCELLULAR LOCATION: Protein 3B: Virion (By similarity). 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; FJ463616; ACO92355.1; -; Genomic_RNA. DR ProteinModelPortal; C3U5A5; -. DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW. DR GO; GO:0019030; C:icosahedral viral capsid; IEA:InterPro. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:InterPro. DR GO; GO:0019062; P:viral attachment to host cell; IEA:UniProtKB-KW. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0019079; P:viral genome replication; IEA:InterPro. DR Gene3D; 4.10.90.10; -; 1. DR InterPro; IPR015031; Capsid_VP4_Picornavir. DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ. DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir. DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir. DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir. DR InterPro; IPR002527; Pico_P2B. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR001205; RNA-dir_pol_picornavirus. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR009003; Trypsin-like_Pept_dom. DR Pfam; PF00548; Peptidase_C3; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00073; Rhv; 2. DR Pfam; PF00910; RNA_helicase; 1. DR Pfam; PF08935; VP4_2; 1. DR PRINTS; PR00918; CALICVIRUSNS. DR ProDom; PD649346; Pico_P2B; 1. DR SUPFAM; SSF50494; Pept_Ser_Cys; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Capsid protein; Helicase; Host cytoplasm; KW Host cytoplasmic vesicle; Host membrane; Host-virus interaction; KW Hydrolase; Ion channel; Ion transport; Membrane; Nucleotide-binding; KW Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding; KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transport; KW Viral attachment to host cell; Viral ion channel; KW Viral RNA replication; Virion; Virus entry into host cell. FT CHAIN 1 101 leader peptide. FT /FTId=PRO_5000461276. FT CHAIN 102 173 capsid protein VP4. FT /FTId=PRO_5000461277. FT CHAIN 174 444 capsid protein VP2. FT /FTId=PRO_5000461278. FT CHAIN 445 676 capsid protein VP3. FT /FTId=PRO_5000461279. FT CHAIN 677 949 capsid protein VP1. FT /FTId=PRO_5000461280. FT CHAIN 950 1091 protein 2A. FT /FTId=PRO_5000461281. FT CHAIN 1092 1218 protein 2B. FT /FTId=PRO_5000461282. FT CHAIN 1219 1543 protein 2B. FT /FTId=PRO_5000461283. FT CHAIN 1544 1629 protein 3A. FT /FTId=PRO_5000461284. FT CHAIN 1630 1649 protein 3B. FT /FTId=PRO_5000461285. FT CHAIN 1650 1866 protein 3C. FT /FTId=PRO_5000461286. FT NON_TER 2318 2318 SQ SEQUENCE 2318 AA; 259535 MW; 639293B2F85610EC CRC64; MCFTPSLWFK NCHSFSKPSG LGFLILLTGN MACKHGYPFL CPLCTAIDVS SDGSFALLFD NEWYPTDLLT VDLDDDVFYP LDCLMDWTDL PLIQDVLMEP QGNSNSSDKN NSQSSGNEGV IINNYYSNQY QNSIDLSANA NGVGKENSKP QGQLMNILGS AADAFKNIAP LLMDQDTEEM TNLSDRVASD TAGNTATNTQ STVGRLFGYA SRHRGKHPTS CADRATDKVL AAERYYTIKL ATWDTTLKAF DHIRVPFPHI LSGKEGGVFG ATLRRHYLCK CGWRIQVQCN ASQFHAGSLL IFMAPEFDTS PYESETEPDK NKVFTMDTTW QSGTKCLRGH SFESKTNQSL RPLSLNHQNT WQWTIYPHQI LNLRTNTTCD IEVPYVNICP TSSWTQHANW TLVVAVLTPL QCPTGSAPDV EITASIQPVK PVFNGLRHSV LEPDSPFPGT IREHAGTFYS TTPDTTVPVY GKTISTPANY MCGEFTDLLS LCKIPTFIGN NLDSKWNPYF SSTNSVNENV SLVTYQVTLS SINLANTMLS SVARNFNQYR GSLNFLFVFT GSAMVKGKFL ISYTPPGADK PKNRNQAMQA TYAIWDLGLN SSYNFTVPFI SPTHFRQTSY TTSTITSVDG WISVWQLTPL TYPANTPTHS DILTLVSGGD DFTLRMPVTP TKYVPHGVDN AEKGKVADDN ASTDFVAEPV KLPENQTEVG FFYDRAVQAC VLKSSQNFSD TFQLQSSDTL LNQTILTPLP NYKVDQSKEE LVEQYRWLES AGTSTQPPYK TKQDWNFVMF SPFTYYKCDL EVTLTALNNN GQGALVRYSP CGAPADITTQ TMSSTPSLAD TRDPHMWFVG PGTTNQVSFV LPFTSPLSVL PAVWFNGYAN FDNSSRYGVA PNADFGRLFV QGSGTFSVHF RYKKMRVFCP RPTVYFPWPS NPQRTKIHAE NPVPILELQN PISIYRVDLF INFSDEIIQF TYKVHGRTVC QYEIPGFGLS RSGRLLVCMG EKPCQLPIST PKCFYHIVFT GSRNSFGVSI YKARYRPWKQ PLHDELFDYG FSTFTDFFKA VRDYHASYYK QRLQHDIETN PGPVQSVFQL QGGVLTKSQA PMSGLQSMLL RAIGIEADCT EFTRAVNLIT DLCNTWESAK TTLSSPEFWT KMVMRIVKMV AASVLYLHNP DLTTTVCLSL MAGIDILTND SVFNWLSSKL SKFFHTPAPP IVPLLQQQSP IREANDNFNL AKNIEWAIKT IKRIVEWITS WFKQEETSPQ AKLDKMLADF PEHCASILAM RNGRKAYTDC AGAFKYFEQL YNLAVQCKRI PLATLCEKFK NKHDHAVARP EPVVVVLRGN AGQGKSVTSQ IIAQAVSKLS FGRQSVYSLP PDSDYLDGYE NQYSVIMDDL GQNPDGEDFK VFCQMVSSTN FLPNMAHLEK KGTPFTSNFI IATTNLPKFR PVTVAHYPAV DRRITFDLTV EAGDECVTHN GMLDVEKAFE EIPGKPQLDC FNTDCRLLHK RGVRFVCNRT KNVYNLQQVV KMVKNTIDNK VENLKKMNTL VAQSPGNDMD YVLTCLRQTN AALQDQIDEL QEAFNQAQER QNFLSDWLKV SAIVFASIAS LSAVCKLVSR FKNLVCPAPV QIQLSEGEQA AYSGGKKGEK QTLQVLDVQG GGKIVAQAGN PVMDYEVNIA KNMVTPITFF YADKAQVTQS CLLIKGHLFV VNRHVAETDW CAFELKGTRH ERDSVQMRSV NKSGMEVDLT FVKVVKGPLF KDNSKKFCSK DDDFPARNET VIGIMNTGVP FVFTGKFLIG NQPVNTTTGA CFNHCIHYRA TTHRGWGGSA LICHVNGKKA VYAMHSAGGG GIAAATIITQ EMIEAAEKAL DCLTPQGAIV EIGIDTVVHV PRKTKLRRTV AHPCFQPKFE PAVLSRYDPR TTKDVDQVAF SKHTTNLEEL PPVFTVVAKE YANRVFTTLG KENQILTPEQ AILGLSGMDP MEKDTSPGLP YTQQGLKRAQ LVNFEQGTMA QNLKEAHTKL TKGNYEDILY QSFLKDEIRP IEKIHEAKTR IVDVPPFHHC IWGRQLLGRF ASKFQTNPGL DLGSAIGTDP DTDWTAFAFQ LLQYKYVYDV DYSNFDASHS TAMFEILIEN FFTVENGFDE RIGDYLRSLA VSRHAFEERR VLVRGGLPSG CAATSMLNTI INNIVIRAAL DLTYSNFEFD DIKVLSYGDD LLIATNYQIN FNLVKQRLAP FNYKITPANK TVEFPETSNL YEVTFLKRKF VRHNSCLFKP QMDTENLKAM VSYCRPGTLK EKLNSIALLA VHSGKSVYDE IFDPFRRIGI IVPEHSTM //