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Database: UniProt
Entry: B5A282_9CALI
LinkDB: B5A282_9CALI
Original site: B5A282_9CALI 
ID   B5A282_9CALI            Unreviewed;       437 AA.
AC   B5A282;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Polymerase {ECO:0000313|EMBL:ACF34344.1};
DE   Flags: Fragment;
OS   Norovirus Hu/GII.4/Shenzhen179-06/2006/CHN.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX   NCBI_TaxID=545143 {ECO:0000313|EMBL:ACF34344.1};
RN   [1] {ECO:0000313|EMBL:ACF34344.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hu/GII.4/Shenzhen179-06/2006/CHN {ECO:0000313|EMBL:ACF34344.1};
RA   He Y.Q., Wu W.L., Cheng J.Q., Yin X.Y., Yang H., Sun H.H., Zhang H.L.,
RA   Yao X.J., Chen W.J.;
RT   "Epidemiologic and Virologic Investigation of Acute Gastroenteritis in
RT   Southern China, 2006.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00025359}.
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         Evidence={ECO:0000256|ARBA:ARBA00001491};
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DR   EMBL; EU794713; ACF34344.1; -; Genomic_RNA.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd23192; Caliciviridae_RdRp; 1.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 6.10.250.3230; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00680; RdRP_1; 1.
DR   PRINTS; PR00918; CALICVIRUSNS.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   4: Predicted;
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}.
FT   DOMAIN          197..318
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACF34344.1"
FT   NON_TER         437
FT                   /evidence="ECO:0000313|EMBL:ACF34344.1"
SQ   SEQUENCE   437 AA;  48907 MW;  0D3C167F9076FD8B CRC64;
     TYEPAYLGGK DPRVKDGPSL QQVMRDQLKP FTEPRGKPPK PSVLEAAKKT IINVLEQTID
     PPEKWSFAQA CASLDKTTSS GHPHHMRKND CWNGESFTGK LADQASKANL MFEEGKNMTP
     VYTGALKDEL VKTDKIYGKI KKRLLWGSDL ATMIRCARAF GGLMDELKAH CVTLPIRVGM
     NMNEDGPIIF EKHSRYRYHY DADYSRWDST QQRAVLAAAL EIMVKFSSEP HLAQVVAEDL
     LSPSVVDVGD FTISINEGLP SGVPCTSQWN SIAHWLLTLC ALSEVTNLSP DIIQANSLFS
     FYGDDEIVST DIKLDPEKLT TKLKEYGLKP TRPDKTEGPL VISEDLDGLT FLRRTVTRDP
     AGWFGKLEQS SILRQMYWTR GPNHEDPFES MIPHSQRPIQ LMSLLGEAAL HGPTFYSKIS
     KLVIAELKEG GMDFYVP
//
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