ID D2E675_9CALI Unreviewed; 269 AA.
AC D2E675;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=RNA-dependent RNA polymerase {ECO:0000313|EMBL:ACX30396.1};
DE Flags: Fragment;
OS Norovirus Hu/GII/Seoul0552/2007/KR.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX NCBI_TaxID=676786 {ECO:0000313|EMBL:ACX30396.1};
RN [1] {ECO:0000313|EMBL:ACX30396.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19950237; DOI=10.1002/jmv.21650;
RA Chung J.Y., Han T.H., Park S.H., Kim S.W., Hwang E.S.;
RT "Detection of GII-4/2006b variant and recombinant noroviruses in children
RT with acute gastroenteritis, South Korea.";
RL J. Med. Virol. 82:146-152(2010).
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; FJ913997; ACX30396.1; -; 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; 1.20.960.20; -; 1.
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:ACX30396.1}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}.
FT DOMAIN 1..116
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACX30396.1"
SQ SEQUENCE 269 AA; 30239 MW; ADD399177A1FAF58 CRC64;
DYSRWDSTQQ RAVLAAALEI MVKFSSEPHL AQVVAEDLLS PSVMDVGDFT ISINEGLPSG
VPCTSQWNSI AHWLLTLCAL SEVTNLSPDI IQANSLFSFY GDDEIVSTDI KLDPEKLTAK
LKEYGLKPTR PDKTEGPLVI SEDLDGLTFL RRTVTRDPAG WFGKLEQSSI LRQMYWTRGP
NHEDPSESMI PHSQRPIQLM SLLGEAALHG PTFYSRISKL VIAELKEGGM DFYVPRQEPM
FRWMRFSDLS TWEGDRNLAP SFVNEDGVE
//
