POLG_SVSAP
ID POLG_SVSAP Reviewed; 2280 AA.
AC Q672I1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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;
OS Sapporo virus (isolate GI/Human/Germany/pJG-Sap01)
OS (Hu/Dresden/pJG-Sap01/DE).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Sapovirus.
OX NCBI_TaxID=291175;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17121797; DOI=10.1128/jvi.01462-06;
RA Fullerton S.W., Blaschke M., Coutard B., Gebhardt J., Gorbalenya A.,
RA Canard B., Tucker P.A., Rohayem J.;
RT "Structural and functional characterization of sapovirus RNA-dependent RNA
RT polymerase.";
RL J. Virol. 81:1858-1871(2007).
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, Alternative initiation; Named isoforms=3;
CC Name=Genome polyprotein;
CC IsoId=Q672I1-1; Sequence=Displayed;
CC Name=Subgenomic capsid protein; Synonyms=VP1;
CC IsoId=Q672I1-2; Sequence=VSP_034391;
CC Name=Uncharacterized protein VP3;
CC IsoId=Q672I0-1; Sequence=External;
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.
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 by alternative promoter usage. {ECO:0000305}.
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; AY694184; AAU09265.2; -; Genomic_RNA.
DR RefSeq; YP_077278.1; NC_006269.1. [Q672I1-1]
DR SMR; Q672I1; -.
DR MEROPS; C24.003; -.
DR GeneID; 5176815; -.
DR KEGG; vg:5176815; -.
DR Proteomes; UP000007049; 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; IPR001665; Norovirus_pept_C37.
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; PF05416; Peptidase_C37; 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 3: Inferred from homology;
KW Alternative initiation; Alternative promoter usage; ATP-binding;
KW Capsid protein; Covalent protein-RNA linkage; DNA replication;
KW Host cytoplasm; Hydrolase; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Protease; Reference proteome; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2280
FT /note="Genome polyprotein"
FT /id="PRO_0000342108"
FT CHAIN 1..68
FT /note="Protein p11"
FT /id="PRO_0000342109"
FT CHAIN 69..324
FT /note="Protein p28"
FT /id="PRO_0000342110"
FT CHAIN 325..665
FT /note="NTPase"
FT /id="PRO_0000342111"
FT CHAIN 666..939
FT /note="Protein p32"
FT /id="PRO_0000342112"
FT CHAIN 940..1053
FT /note="Viral genome-linked protein"
FT /id="PRO_0000342113"
FT CHAIN 1054..1721
FT /note="Protease-polymerase p70"
FT /id="PRO_0000342114"
FT CHAIN 1722..2280
FT /note="Capsid protein"
FT /id="PRO_0000342115"
FT DOMAIN 454..608
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1054..1202
FT /note="Peptidase C24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT DOMAIN 1442..1567
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1722..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1084
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1105
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1169
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT BINDING 480..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 68..69
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 324..325
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 665..666
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 939..940
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 1053..1054
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 1721..1722
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT MOD_RES 965
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1719
FT /note="Missing (in isoform Subgenomic capsid protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_034391"
SQ SEQUENCE 2280 AA; 251007 MW; 2402A87ACE40873F CRC64;
MVSKPFKPIV LNATFEWQVF KRCYLRVAPR EAFCENLSEL HHYFARRVNA WLKHATRTLP
DGYTFVEEGL LDMFGTKAPD SVQEGTLFRE LFGVDQTEQF PLSLADLAKL QGELVDATRT
PGHALRQKYT MTTIQDLINK ITKVVPVQAT LTEMHARRQF ERERADLFHE LPLVDEDAVS
QPKTYFYTMW RQVVKKGKAY FCPLVKTSAW RTKISAITEP IKDFLIAFCQ AVQQEMGVNP
QYLQLAWLQK LKPTTLTIIL QQHKYTVSGW LATMTALVEV YSNLFDDLRK SSVAIVSSIG
AFFDICKDFV SQVVELVKTT FTAQGPTDLG WAAVLAGAAM ILLKMSGCPG VIGMWTKVLK
ICGGITTITA AARGVRWLKD LYEEAEGRRL AKMYMARGAA LIELAASREV TGIDELKGLL
DCFTILIEEG TELIHKFGTS PLAGLVRTYV SELETQANNI RSTIKLDTPR RVPVVIILTG
APGIGKTRLA QYVGQRFGKT SNFSVAVDHH DGYTGNTVCI WDEFDVDSKG AFVETMIGIA
NTAPFPLNCD RVENKGRVFT SDYVICTSNY PTSVIPDNPR AAAFYRRVLT VDVSAPDLEE
WKKRNPGKRP TPDLYQDDFS HLKLMLRPYL GYNPDGDTLE GPRVAPTQIS IAGLITLMER
RFKEQAGPLQ NLWLQVPKTL VEQSTNMVKA FMYANRAVCD VIPNPATRDI AETALTKIFV
CGTAPPPEFV GKHIVITGIE VGDASIANSL LSMFTTTTRL SAAAQREYMY RVWSPLIHIQ
DRSINTQNLP YINRVIPVTS HWDFLRGLRH HLGFTSIPGM WKAFQGWRTS QGIVDFVAHH
MADVTFPSNP ECTIFRTPDA DVVFYTFGSY VCFATPARVP YVGTPPTTIH SNTPRCMTWG
ETIALLCEVV AEFVLHFGPV ILSAANIAYL MTRGSRTEEA KGKTKHGRGM RHGHRAGVSL
SDDEYDEWRD LMRDWRRDMS VNDFLMLRER SALGVDDEDE ARYRAWLEIR AMRMAGGAYT
HATIIGRGGV RDEIIRTAPR RAPTRPQQHY EEEAPTAIVE FTQGGDHIGY GVHIGNGNVI
TVTHVASTSD EVNGSAFKIT RTVGETTWVQ GPFSQLPHMQ IGSGSPVYFT TRLHPVFTIS
EGTFETPNIT VNGFHVRIMN GYPTKKGDCG LPYFNSNRQL VALHAGTDTQ GETKVAQRVV
KEVTTQDEFQ WKGLPVVKSG LDVGGMPTGT RYHRSPAWPE EQPGETHAPA PFGAGDKRYT
FSQTEMLVNG LKPYTEPTAG VPPQLLSRAV THVRSYIETI IGTHRSPVLT YHQACELLER
TTSCGPFVQG LKGDYWDEEQ QQYTGVLANH LEQAWDKANK GIAPRNAYKL ALKDELRPIE
KNKAGKRRLL WGCDAATTLI ATAAFKAVAT RLQVVTPMTP VAVGINMDSV QMQVMNDSLK
GGVLYCLDYS KWDSTQNPAV TAASLAILER FAEPHPIVSC AIEALSSPAE GYVNDIKFVT
RGGLPSGMPF TSVVNSINHM IYVAAAILQA YESHNVPYTG NVFQVETVHT YGDDCMYSVC
PATASIFHAV LANLTSYGLK PTAADKSDAI KPTNTPVFLK RTFTQTPHGV RALLDITSIT
RQFYWLKANR TSDPSSPPAF DRQARSAQLE NALAYASQHG PVVFDTVRQI AIKTAQGEGL
VLVNTNYDQA LATYNAWFIG GTVPDPVGHT EGTHKIVFEM EGNGSNPEPK QSNNPMVVDP
PGTTGPTTSH VVVANPEQPN GAAQRLELAV ATGAIQSNVP EAIRNCFAVF RTFAWNDRMP
TGTFLGSISL HPNINPYTAH LSGMWAGWGG SFEVRLSISG SGVFAGRIIA SVIPPGVDPS
SIRDPGVLPH AFVDARITEP VSFMIPDVRA VDYHRMDGAE PTCSLGFWVY QPLLNPFSTT
AVSTCWVSVE TKPGGDFDFC LLRPPGQQME NGVSPEGLLP RRLGYSRGNR VGGLVVGMVL
VAEHKQVNRH FNSNSVTFGW STAPVNPMAA EIVTNQAHST SRHAWLSIGA QNKGPLFPGI
PNHFPDSCAS TIVGAMDTSL GGRPSTGVCG PAISFQNNGD VYENDTPSVM FATYDPLTSG
TGVALTNSIN PASLALVRIS NNDFDTSGFA NDKNVVVQMS WEMYTGTNQI RGQVTPMSGT
NYTFTSTGAN TLVLWQERML SYDGHQAILY SSQLERTAEY FQNDIVNIPE NSMAVFNVET
NSASFQIGIR PDGYMVTGGS IGINVPLEPE TRFQYVGILP LSAALSGPSG NMGRARRVFQ
