ID L7VMI0_9CALI Unreviewed; 108 AA.
AC L7VMI0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=RNA-dependent RNA polymerase {ECO:0000313|EMBL:AGC66773.1};
DE Flags: Fragment;
OS Norovirus Hu/GII.6/GZ2010-L1/Guangzhou/CHN/2010.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX NCBI_TaxID=1282428 {ECO:0000313|EMBL:AGC66773.1};
RN [1] {ECO:0000313|EMBL:AGC66773.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hu/GII.6/GZ2010-L1/Guangzhou/CHN/2010
RC {ECO:0000313|EMBL:AGC66773.1};
RX PubMed=23947818; DOI=10.1089/fpd.2013.1521;
RA Xue L., Wu Q., Dong R., Kou X., Li Y., Zhang J., Guo W.;
RT "Genetic analysis of noroviruses associated with sporadic gastroenteritis
RT during winter in Guangzhou, China.";
RL Foodborne Pathog. Dis. 10:888-895(2013).
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};
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; JX984936; AGC66773.1; -; 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 Gene3D; 3.30.70.270; -; 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 ECO:0000313|EMBL:AGC66773.1}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}.
FT DOMAIN 1..108
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGC66773.1"
FT NON_TER 108
FT /evidence="ECO:0000313|EMBL:AGC66773.1"
SQ SEQUENCE 108 AA; 11880 MW; 15EC3456145AB3DB CRC64;
YHYDADYSRW DSTQQRNILS AAMEVMVRFS AEPELAQVVA EDLLAPSQLD VGDFVISVQE
GLPPGVPCTS QWNSIAHWIL TLSAMAEVSG LSPDVVQAHS CFSFYGDD
//
