POLG_SVM10
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 03-AUG-2022, entry version 91.
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; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Sapovirus.
OX NCBI_TaxID=234601;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEOLYTIC PROCESSING OF POLYPROTEIN,
RP 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; HIS-1136;
RP 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 coli.";
RL Arch. Virol. 150:2539-2548(2005).
CC -!- FUNCTION: NTPase presumably plays a role in replication. Despite having
CC similarities with helicases, does not seem to display any helicase
CC activity (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Viral genome-linked protein is covalently linked to the 5'-
CC end of the positive-strand, negative-strand genomic RNAs and subgenomic
CC RNA. Acts as a genome-linked replication primer. May recruit ribosome
CC to viral RNA thereby promoting viral proteins translation (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Protease-polymerase p70 processes the polyprotein: Pro-Pol is
CC first released by autocleavage, then all other proteins are cleaved (By
CC similarity). It is also an RNA-directed RNA polymerase which replicates
CC genomic and antigenomic viral RNA by recognizing specific signals.
CC Catalyzes the covalent attachment VPg with viral RNAs (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Capsid protein self assembles to form an icosahedral capsid
CC with a T=3 symmetry, about 38 nm in diameter, and consisting of 180
CC capsid proteins. The capsid encapsulate the genomic RNA and VP2
CC proteins. Attaches virion to target cells, inducing endocytosis of the
CC viral particle. Acidification of the endosome induces conformational
CC change of capsid protein thereby injecting virus genomic RNA into host
CC cytoplasm (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase with a preference for cleavage when the P1
CC position is occupied by Glu-|-Xaa and the P1' position is occupied by
CC Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01242};
CC -!- SUBUNIT: [Capsid protein]: Homodimer. Homomultimer. {ECO:0000250}.
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 Name=Subgenomic capsid protein; Synonyms=VP1;
CC IsoId=Q6XDK8-2; Sequence=VSP_034390;
CC -!- DOMAIN: Protease-polymerase is composed of two domains displaying two
CC different catalytic activity. These activities may act independently.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. Pro-
CC Pol is first autocatalytically cleaved, then processes the whole
CC polyprotein. {ECO:0000269|PubMed:15919882}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This
CC uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Two different RNAs lead the expression of the capsid
CC protein. One arises from the cleavage of the polyprotein translated
CC from the genomic RNA and the other from the translation of a subgenomic
CC RNA derived from the (-)RNA template. Capsid protein expressed from the
CC subgenomic mRNA is produced in much larger amounts than the cleaved one
CC (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced from the genomic
CC RNA.
CC -!- MISCELLANEOUS: [Isoform Subgenomic capsid protein]: Produced from the
CC subgenomic RNA. {ECO:0000305}.
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DR EMBL; AY237420; AAQ17058.2; -; mRNA.
DR RefSeq; YP_022762.1; NC_010624.1. [Q6XDK8-1]
DR SMR; Q6XDK8; -.
DR MEROPS; C24.003; -.
DR GeneID; 2943313; -.
DR KEGG; vg:2943313; -.
DR Proteomes; UP000112655; Genome.
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:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
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 5'-3' 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 CDD; cd00205; rhv_like; 1.
DR Gene3D; 2.60.120.20; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004005; Calicivirus_coat.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
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 SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51894; CV_3CL_PRO; 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; DNA replication;
KW Host cytoplasm; Hydrolase; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Protease; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2278
FT /note="Genome polyprotein"
FT /id="PRO_0000342101"
FT CHAIN 1..69
FT /note="Protein p11"
FT /id="PRO_0000342102"
FT CHAIN 70..325
FT /note="Protein p28"
FT /id="PRO_0000342103"
FT CHAIN 326..666
FT /note="NTPase"
FT /id="PRO_0000342104"
FT CHAIN 667..940
FT /note="Protein p32"
FT /id="PRO_0000342105"
FT CHAIN 941..1055
FT /note="Viral genome-linked protein"
FT /id="PRO_0000342106"
FT CHAIN 1056..1722
FT /note="Protease-polymerase p70"
FT /id="PRO_0000342107"
FT CHAIN 1723..2278
FT /note="Capsid protein"
FT /id="PRO_5000090469"
FT DOMAIN 454..609
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1056..1204
FT /note="Peptidase C24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT DOMAIN 1443..1568
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 939..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1086
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1107
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1171
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT BINDING 481..488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 69..70
FT /note="Cleavage; by Pro-Pol"
FT SITE 325..326
FT /note="Cleavage; by Pro-Pol"
FT SITE 666..667
FT /note="Cleavage; by Pro-Pol"
FT SITE 940..941
FT /note="Cleavage; by Pro-Pol"
FT SITE 1055..1056
FT /note="Cleavage; by Pro-Pol"
FT SITE 1722..1723
FT /note="Cleavage; by Pro-Pol"
FT MOD_RES 966
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1720
FT /note="Missing (in isoform Subgenomic capsid protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_034390"
FT MUTAGEN 1069
FT /note="H->A: No effect on protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:17459935"
FT MUTAGEN 1075
FT /note="H->A: No effect on protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:17459935"
FT MUTAGEN 1086
FT /note="H->A: Complete loss of protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:17459935"
FT MUTAGEN 1107
FT /note="E->A: Complete loss of protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:17459935"
FT MUTAGEN 1120
FT /note="H->A: No effect on protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:17459935"
FT MUTAGEN 1136
FT /note="H->A: No effect on protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:17459935"
FT MUTAGEN 1143
FT /note="E->A: No effect on protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:17459935"
FT MUTAGEN 1147
FT /note="E->A: No effect on protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:17459935"
FT MUTAGEN 1171
FT /note="C->A: Complete loss of protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:15919882"
FT MUTAGEN 1186
FT /note="H->A: No effect on protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:17459935"
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
