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Genome polyprotein [Cleaved into: Protein p11; Protein p28; NTPase (EC 3.6.1.15) (p35); Protein p32; Viral genome-linked protein (VPg) (p14); Protease-polymerase p70 (Pro-Pol) (EC 2.7.7.48) (EC 3.4.22.66); Capsid protein (CP) (VP1) (p60)]

 POLG_SVM10              Reviewed;        2278 AA.
Q6XDK8;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
10-MAY-2017, entry version 75.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein p11;
Contains:
RecName: Full=Protein p28;
Contains:
RecName: Full=NTPase;
EC=3.6.1.15;
AltName: Full=p35;
Contains:
RecName: Full=Protein p32;
Contains:
RecName: Full=Viral genome-linked protein;
AltName: Full=VPg;
AltName: Full=p14;
Contains:
RecName: Full=Protease-polymerase p70;
Short=Pro-Pol;
EC=2.7.7.48;
EC=3.4.22.66;
Contains:
RecName: Full=Capsid protein;
Short=CP;
AltName: Full=VP1;
AltName: Full=p60;
ORFNames=ORF1;
Sapporo virus (isolate GII/Human/Thailand/Mc10/2000)
(Hu/SaV/Mc10/2000/Thailand).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Caliciviridae; Sapovirus.
NCBI_TaxID=234601;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEOLYTIC PROCESSING OF
POLYPROTEIN, AND MUTAGENESIS OF CYS-1171.
PubMed=15919882; DOI=10.1128/JVI.79.12.7283-7290.2005;
Oka T., Katayama K., Ogawa S., Hansman G.S., Kageyama T., Ushijima H.,
Miyamura T., Takeda N.;
"Proteolytic processing of sapovirus ORF1 polyprotein.";
J. Virol. 79:7283-7290(2005).
[2]
MUTAGENESIS OF HIS-1069; HIS-1075; HIS-1086; GLU-1107; HIS-1120;
HIS-1136; GLU-1143; GLU-1147 AND HIS-1186.
PubMed=17459935; DOI=10.1128/JVI.02840-06;
Oka T., Yamamoto M., Yokoyama M., Ogawa S., Hansman G.S., Katayama K.,
Miyashita K., Takagi H., Tohya Y., Sato H., Takeda N.;
"Highly conserved configuration of catalytic amino acid residues among
calicivirus-encoded proteases.";
J. Virol. 81:6798-6806(2007).
[3]
PROTEIN SEQUENCE OF 1056-1060.
PubMed=16052286; DOI=10.1007/s00705-005-0591-0;
Oka T., Katayama K., Ogawa S., Hansman G.S., Kageyama T., Miyamura T.,
Takeda N.;
"Cleavage activity of the sapovirus 3C-like protease in Escherichia
coli.";
Arch. Virol. 150:2539-2548(2005).
-!- FUNCTION: NTPase presumably plays a role in replication. Despite
having similarities with helicases, does not seem to display any
helicase activity (By similarity). {ECO:0000250}.
-!- FUNCTION: Viral genome-linked protein is covalently linked to the
5'-end of the positive-strand, negative-strand genomic RNAs and
subgenomic RNA. Acts as a genome-linked replication primer. May
recruit ribosome to viral RNA thereby promoting viral proteins
translation (By similarity). {ECO:0000250}.
-!- FUNCTION: Protease-polymerase p70 processes the polyprotein: Pro-
Pol is first released by autocleavage, then all other proteins are
cleaved (By similarity). It is also an RNA-directed RNA polymerase
which replicates genomic and antigenomic viral RNA by recognizing
specific signals. Catalyzes the covalent attachment VPg with viral
RNAs (By similarity). {ECO:0000250}.
-!- FUNCTION: Capsid protein self assembles to form an icosahedral
capsid with a T=3 symmetry, about 38 nm in diameter, and
consisting of 180 capsid proteins. The capsid encapsulate the
genomic RNA and VP2 proteins. Attaches virion to target cells,
inducing endocytosis of the viral particle. Acidification of the
endosome induces conformational change of capsid protein thereby
injecting virus genomic RNA into host cytoplasm (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: Endopeptidase with a preference for cleavage
when the P1 position is occupied by Glu-|-Xaa and the P1' position
is occupied by Gly-|-Yaa.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: Capsid protein homodimerizes, then multimerizes.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion. Host cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=Genome polyprotein;
IsoId=Q6XDK8-1; Sequence=Displayed;
Note=Produced from the genomic RNA.;
Name=Subgenomic capsid protein; Synonyms=VP1;
IsoId=Q6XDK8-2; Sequence=VSP_034390;
Note=Produced from the subgenomic RNA.;
-!- DOMAIN: Protease-polymerase is composed of two domains displaying
two different catalytic activity. These activities may act
independently.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Pro-Pol is first autocatalytically cleaved, then processes the
whole polyprotein. {ECO:0000269|PubMed:15919882}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
attached to the 5'-end of the polyadenylated genomic and
subgenomic RNAs. This uridylylated form acts as a nucleotide-
peptide primer for the polymerase (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Two different RNAs lead the expression of the
capsid protein. One arises from the cleavage of the polyprotein
translated from the genomic RNA and the other from the translation
of a subgenomic RNA derived from the (-)RNA template. Capsid
protein expressed from the subgenomic mRNA is produced in much
larger amounts than the cleaved one (By similarity).
{ECO:0000250}.
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EMBL; AY237420; AAQ17058.2; -; mRNA.
RefSeq; YP_022762.1; NC_010624.1. [Q6XDK8-1]
ProteinModelPortal; Q6XDK8; -.
SMR; Q6XDK8; -.
MEROPS; C24.003; -.
PRIDE; Q6XDK8; -.
GeneID; 2943313; -.
KEGG; vg:2943313; -.
Proteomes; UP000112655; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
CDD; cd00205; rhv_like; 1.
InterPro; IPR004005; Calicivirus_coat.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000317; Peptidase_C24.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF00915; Calici_coat; 1.
Pfam; PF03510; Peptidase_C24; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00916; 2CENDOPTASE.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
Alternative promoter usage; ATP-binding; Capsid protein;
Complete proteome; Covalent protein-RNA linkage;
Direct protein sequencing; DNA replication; Host cytoplasm; Hydrolase;
Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
RNA-directed RNA polymerase; Thiol protease; Transferase;
Viral RNA replication; Virion.
CHAIN 1 2278 Genome polyprotein.
/FTId=PRO_0000342101.
CHAIN 1 69 Protein p11.
/FTId=PRO_0000342102.
CHAIN 70 325 Protein p28.
/FTId=PRO_0000342103.
CHAIN 326 666 NTPase.
/FTId=PRO_0000342104.
CHAIN 667 940 Protein p32.
/FTId=PRO_0000342105.
CHAIN 941 1055 Viral genome-linked protein.
/FTId=PRO_0000342106.
CHAIN 1056 1722 Protease-polymerase p70.
/FTId=PRO_0000342107.
CHAIN 1723 2278 Capsid protein.
/FTId=PRO_5000090469.
DOMAIN 454 609 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1071 1177 Peptidase C24.
DOMAIN 1443 1568 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 481 488 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
ACT_SITE 1086 1086 For protease activity. {ECO:0000250}.
ACT_SITE 1107 1107 For protease activity. {ECO:0000250}.
ACT_SITE 1171 1171 For protease activity. {ECO:0000250}.
SITE 69 70 Cleavage; by Pro-Pol.
SITE 325 326 Cleavage; by Pro-Pol.
SITE 666 667 Cleavage; by Pro-Pol.
SITE 940 941 Cleavage; by Pro-Pol.
SITE 1055 1056 Cleavage; by Pro-Pol.
SITE 1722 1723 Cleavage; by Pro-Pol.
MOD_RES 966 966 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
VAR_SEQ 1 1720 Missing (in isoform Subgenomic capsid
protein). {ECO:0000305}.
/FTId=VSP_034390.
MUTAGEN 1069 1069 H->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1075 1075 H->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1086 1086 H->A: Complete loss of protease activity
in vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1107 1107 E->A: Complete loss of protease activity
in vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1120 1120 H->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1136 1136 H->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1143 1143 E->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1147 1147 E->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1171 1171 C->A: Complete loss of protease activity
in vitro. {ECO:0000269|PubMed:15919882}.
MUTAGEN 1186 1186 H->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
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


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