ID POLG_SVM10 Reviewed; 2278 AA. AC Q6XDK8; DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 16-APR-2014, entry version 58. DE RecName: Full=Genome polyprotein; DE Contains: DE RecName: Full=Protein p11; DE Contains: DE RecName: Full=Protein p28; DE Contains: DE RecName: Full=NTPase; DE EC=3.6.1.15; DE AltName: Full=p35; DE Contains: DE RecName: Full=Protein p32; DE Contains: DE RecName: Full=Viral genome-linked protein; DE AltName: Full=VPg; DE AltName: Full=p14; DE Contains: DE RecName: Full=Protease-polymerase p70; DE Short=Pro-Pol; DE EC=2.7.7.48; DE EC=3.4.22.66; DE Contains: DE RecName: Full=Capsid protein; DE Short=CP; DE AltName: Full=VP1; DE AltName: Full=p60; GN ORFNames=ORF1; OS Sapporo virus (isolate GII/Human/Thailand/Mc10/2000) OS (Hu/SaV/Mc10/2000/Thailand). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Caliciviridae; OC Sapovirus. OX NCBI_TaxID=234601; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEOLYTIC PROCESSING OF RP POLYPROTEIN, AND MUTAGENESIS OF CYS-1171. RX PubMed=15919882; DOI=10.1128/JVI.79.12.7283-7290.2005; RA Oka T., Katayama K., Ogawa S., Hansman G.S., Kageyama T., Ushijima H., RA Miyamura T., Takeda N.; RT "Proteolytic processing of sapovirus ORF1 polyprotein."; RL J. Virol. 79:7283-7290(2005). RN [2] RP MUTAGENESIS OF HIS-1069; HIS-1075; HIS-1086; GLU-1107; HIS-1120; RP HIS-1136; GLU-1143; GLU-1147 AND HIS-1186. RX PubMed=17459935; DOI=10.1128/JVI.02840-06; RA Oka T., Yamamoto M., Yokoyama M., Ogawa S., Hansman G.S., Katayama K., RA Miyashita K., Takagi H., Tohya Y., Sato H., Takeda N.; RT "Highly conserved configuration of catalytic amino acid residues among RT calicivirus-encoded proteases."; RL J. Virol. 81:6798-6806(2007). RN [3] RP PROTEIN SEQUENCE OF 1056-1060. RX PubMed=16052286; DOI=10.1007/s00705-005-0591-0; RA Oka T., Katayama K., Ogawa S., Hansman G.S., Kageyama T., Miyamura T., RA Takeda N.; RT "Cleavage activity of the sapovirus 3C-like protease in Escherichia RT coli."; RL Arch. Virol. 150:2539-2548(2005). CC -!- FUNCTION: NTPase presumably plays a role in replication. Despite CC having similarities with helicases, does not seem to display any CC helicase activity (By similarity). CC -!- FUNCTION: Viral genome-linked protein is covalently linked to the CC 5'-end of the positive-strand, negative-strand genomic RNAs and CC subgenomic RNA. Acts as a genome-linked replication primer. May CC recruit ribosome to viral RNA thereby promoting viral proteins CC translation (By similarity). CC -!- FUNCTION: Protease-polymerase p70 processes the polyprotein: Pro- CC Pol is first released by autocleavage, then all other proteins are CC cleaved (By similarity). It is also an RNA-directed RNA polymerase CC which replicates genomic and antigenomic viral RNA by recognizing CC specific signals. Catalyzes the covalent attachment VPg with viral CC RNAs (By similarity). CC -!- FUNCTION: Capsid protein self assembles to form an icosahedral CC capsid with a T=3 symmetry, about 38 nm in diameter, and CC consisting of 180 capsid proteins. The capsid encapsulate the CC genomic RNA and VP2 proteins. Attaches virion to target cells, CC inducing endocytosis of the viral particle. Acidification of the CC endosome induces conformational change of capsid protein thereby CC injecting virus genomic RNA into host cytoplasm (By similarity). CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- CATALYTIC ACTIVITY: Endopeptidase with a preference for cleavage CC when the P1 position is occupied by Glu-|-Xaa and the P1' position CC is occupied by Gly-|-Yaa. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBUNIT: Capsid protein homodimerizes, then multimerizes (By CC similarity). CC -!- SUBCELLULAR LOCATION: Capsid protein: Virion. Host cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage; Named isoforms=2; CC Name=Genome polyprotein; CC IsoId=Q6XDK8-1; Sequence=Displayed; CC Note=Produced from the genomic RNA; CC Name=Subgenomic capsid protein; Synonyms=VP1; CC IsoId=Q6XDK8-2; Sequence=VSP_034390; CC Note=Produced from the subgenomic RNA; CC -!- DOMAIN: Protease-polymerase is composed of two domains displaying CC two different catalytic activity. These activities may act CC independently. CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. CC Pro-Pol is first autocatalytically cleaved, then processes the CC whole polyprotein. CC -!- PTM: VPg is uridylylated by the polymerase and is covalently CC attached to the 5'-end of the polyadenylated genomic and CC subgenomic RNAs. This uridylylated form acts as a nucleotide- CC peptide primer for the polymerase (By similarity). CC -!- MISCELLANEOUS: Two differents RNAs lead the expression of the CC capsid protein. One arises from the cleavage of the polyprotein CC translated from the genomic RNA and the other from the translation CC of a subgenomic RNA derived from the (-)RNA template. Capsid CC protein expressed from the subgenomic mRNA is produced in much CC larger amounts than the cleaved one (By similarity). CC -!- SIMILARITY: Contains 1 peptidase C24 domain. 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; AY237420; AAQ17058.2; -; mRNA. DR RefSeq; YP_022762.1; NC_010624.1. DR ProteinModelPortal; Q6XDK8; -. DR SMR; Q6XDK8; 1209-1703. DR MEROPS; C24.003; -. DR GeneID; 2943313; -. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C:viral capsid; 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:0003723; F:RNA binding; IEA:InterPro. 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:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR004005; Calicivirus_coat. 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; IPR027417; P-loop_NTPase. DR InterPro; IPR000317; Peptidase_C24. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR009003; Trypsin-like_Pept_dom. DR Pfam; PF00915; Calici_coat; 1. DR Pfam; PF03510; Peptidase_C24; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00910; RNA_helicase; 1. DR PRINTS; PR00916; 2CENDOPTASE. DR PRINTS; PR00918; CALICVIRUSNS. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 1: Evidence at protein level; KW Alternative promoter usage; ATP-binding; Capsid protein; KW Covalent protein-RNA linkage; Direct protein sequencing; KW DNA replication; Host cytoplasm; Hydrolase; Nucleotide-binding; KW Nucleotidyltransferase; Phosphoprotein; Protease; KW RNA-directed RNA polymerase; Thiol protease; Transferase; KW Viral RNA replication; Virion. FT CHAIN 1 2278 Genome polyprotein. FT /FTId=PRO_0000342101. FT CHAIN 1 69 Protein p11. FT /FTId=PRO_0000342102. FT CHAIN 70 325 Protein p28. FT /FTId=PRO_0000342103. FT CHAIN 326 666 NTPase. FT /FTId=PRO_0000342104. FT CHAIN 667 940 Protein p32. FT /FTId=PRO_0000342105. FT CHAIN 941 1055 Viral genome-linked protein. FT /FTId=PRO_0000342106. FT CHAIN 1056 1722 Protease-polymerase p70. FT /FTId=PRO_0000342107. FT CHAIN 1723 2278 Capsid protein. FT /FTId=PRO_5000090469. FT DOMAIN 454 609 SF3 helicase. FT DOMAIN 1071 1177 Peptidase C24. FT DOMAIN 1443 1568 RdRp catalytic. FT NP_BIND 481 488 ATP (Potential). FT ACT_SITE 1086 1086 For protease activity (By similarity). FT ACT_SITE 1107 1107 For protease activity (By similarity). FT ACT_SITE 1171 1171 For protease activity (By similarity). FT SITE 69 70 Cleavage; by Pro-Pol. FT SITE 325 326 Cleavage; by Pro-Pol. FT SITE 666 667 Cleavage; by Pro-Pol. FT SITE 940 941 Cleavage; by Pro-Pol. FT SITE 1055 1056 Cleavage; by Pro-Pol. FT SITE 1722 1723 Cleavage; by Pro-Pol. FT MOD_RES 966 966 O-(5'-phospho-RNA)-tyrosine (By FT similarity). FT VAR_SEQ 1 1720 Missing (in isoform Subgenomic capsid FT protein). FT /FTId=VSP_034390. FT MUTAGEN 1069 1069 H->A: No effect on protease activity in FT vitro. FT MUTAGEN 1075 1075 H->A: No effect on protease activity in FT vitro. FT MUTAGEN 1086 1086 H->A: Complete loss of protease activity FT in vitro. FT MUTAGEN 1107 1107 E->A: Complete loss of protease activity FT in vitro. FT MUTAGEN 1120 1120 H->A: No effect on protease activity in FT vitro. FT MUTAGEN 1136 1136 H->A: No effect on protease activity in FT vitro. FT MUTAGEN 1143 1143 E->A: No effect on protease activity in FT vitro. FT MUTAGEN 1147 1147 E->A: No effect on protease activity in FT vitro. FT MUTAGEN 1171 1171 C->A: Complete loss of protease activity FT in vitro. FT MUTAGEN 1186 1186 H->A: No effect on protease activity in FT vitro. SQ SEQUENCE 2278 AA; 250097 MW; DE7386F8EE49AD11 CRC64; MASKPFYPIE FNPSVELQVL RSAHLRVGGR EQMFETINDL NDHVRGVVAK LWCKHLHRSL AAAPTFTEEG LLDSFLSKPP VDINPDTTFR ELFGINPHEQ FPLSIHDLAK LQGELVDAAR NPGHVLRRHY STDSLTALIN KITKFVPVHA TLQEMQARRA FERERAELFR ELPHADLDVS RQQKSYFYAM WRQVVKKSKE FFIPLVKCTS WRKKFTEPAE IVRQVLVHFC EGMRSQFSTN ANYINLSLIA KLRPTVLTMI LQQHKNTYRG WLATVTALVE VYSNLFQDMR DTAVSAVSAI TLVFETIKDF VVNVIDLVKS TFQSQGPTSC GWAAIIAGAL LILMKLSGCS NTTSYWHRLL KVCGGVTTIA AAARAVVWVR DIIAEADGKA RLKKYMARTA ALLELAASRD VTGTDELKRL LDCFTQLIEE GTELIQEFGT SPLAGLTRSY VSELESTANS IRSTILLDTP RKTPVAIILT GPPGIGKTRL AQHLAAGFGK VSNFSVTLDH HDSYTGNEVA IWDEFDVDTQ GKFVETMIGV VNTAPYPLNC DRVENKGKVF TSDYIICTSN YPTSVLPDNP RAGAFYRRVT TIDVSSPTIE DWKKKNPGKK PPPDLYKNDF THLRLSVRPF LGYNPEGDTL DGVRVKPVLT SVDGLSRLME TKFKEQGNEH RNLWITCPRD LVAPAASGLK AYMAANRALA QVFQEPSSQD IGETCTSRVY VSCNNPPPTY SGRVVKITAI NPWDASLANS MLSMFETTSH IPASIQREIM YRVWDPLVHL QTREPNTQML PYINRVVPVS SAFDFIRGLR HHLGLCSVKG MWRAYQGWNS SSSILEFLSK HMADVAFPHN PECTVFRAPD GDVIFYTFGS YACFVSPARV PFVGEPPKNV HSNITRNMTW AETLRLLAET ITESLVHFGP FLLMMHNVSY LATRSGREEE AKGKTKHGRG AKHARRGGVS LSDDEYDEWR DLVRDWRQDM TVGEFVELRE RYALGMDSED VQRYRAWLEL RAMRMGAGAY QHATIIGRGG VQDTIIRTQP MRAPRAPRNQ GYDEEAPTPI VTFTSGGDHI GYGCHMGNGV VVTVTHVASA SDQVEGQDFA IRKTEGETTW VNTNLGHLPH YQIGDGAPVY YSARLHPVTT LAEGTYETPN ITVQGYHLRI INGYPTKRGD CGTPYFDSCR RLVGLHAATS TNGETKLAQR VTKTSKVENA FAWKGLPVVR GPDCGGMPTG TRYHRSPAWP NPVEGETHAP APFGSGDERY KFSQVEMLVN GLKPYSEPTP GIPPALLQRA ATHTRTYLET IIGTHRSPNL SFSEACSLLE KSTSCGPFVA GQKGDYWDED KQCYTGVLAE HLAKAWDAAN RGVAPQNAYK LALKDELRPI EKNAQGKRRL LWGCDAGATL VATAAFKGVA TRLQAVAPMT PVSVGINMDS YQVEVLNESL KGGVLYCLDY SKWDSTQHPA VTAASLGILE RLSEATPITT SAVELLSSPA RGHLNDIVFI TKSGLPSGMP FTSVINSLNH MTYFAAAVLK AYEQHGAPYT GNVFQVETVH TYGDDCLYSV CPATASIFQT VLANLTSFGL KPTAADKSET IAPTHTPVFL KRTLTCTPRG VRGLLDITSI KRQFLWIKAN RTVDINSPPA YDRDARGIQL ENALAYASQH GHAVFEEVAE LARHTAKAEG LVLTNVNYDQ ALATYESWFI GGTGLVQGSP SEETTKLVFE MEGLGQPQPQ GGEKTSPQPV TPQDTIGPTA ALLLPTQIET PNASAQRLEL AMATGAVTSN VPNCIRECFA SVTTIPWTTR QAANTFLGAI HLGPRINPYT AHLSAMFAGW GGGFQVRVTI SGSGLFAGRA VTAILPPGVN PASVQNPGVF PHAFIDARTT EPILINLPDI RPVDFHRVDG DDATASVGLW VAQPLINPFQ TGPVSTCWLS FETRPGPDFD FCLLKAPEQQ MDNGISPASL LPRRLGRSRG NRMGGRIVGL VVVAAAEQVN HHFDARSTTL GWSTLPVEPI AGDISWYGDA GNKSIRGLVS AQGKGIIFPN IVNHWTDVAL SSKTSNTTTI PTDTSTLGNL PGASGPLVTF ADNGDVNESS AQNAILTAAN QNFTSFSPTF DAAGIWVWMP WATDRPGASD SNIYISPTWV NGNPSHPIHE KCTNMIGTNF QFGGTGTNNI MLWQEQHFTS WPGAAEVYCS QLESTAEIFQ NNIVNIPMNQ MAVFNVETAG NSFQIAILPN GYCVTNAPVG THQLLDYETS FKFVGLFPQS TSLQGPHGNS GRAVRFLE //