ID W0G9Q8_9HEPC Unreviewed; 114 AA. AC W0G9Q8; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 22-FEB-2023, entry version 32. DE RecName: Full=RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU363062}; DE EC=2.7.7.48 {ECO:0000256|RuleBase:RU363062}; DE Flags: Fragment; OS hepatitis C virus genotype 1a. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Hepacivirus. OX NCBI_TaxID=2847144 {ECO:0000313|EMBL:AHF51797.1}; RN [1] {ECO:0000313|EMBL:AHF51797.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H11 {ECO:0000313|EMBL:AHF51797.1}; RX PubMed=23714239; DOI=10.1186/1743-422X-10-167; RA da Silva N.M.O., Germano F.N., Mendoza-Sassi R.A., Seuanez H.N., RA Soares M.A., de Martinez A.M.B.; RT "Evidence of association between hepatitis C virus genotype 2b and RT nosocomial transmissions in hemodialysis centers from southern Brazil."; RL Virol. J. 10:167-167(2013). 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:0000256|RuleBase:RU363062}; 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; KC520832; AHF51797.1; -; Genomic_RNA. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. 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; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002166; RNA_pol_HCV. DR Pfam; PF00998; RdRP_3; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. PE 4: Predicted; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|ARBA:ARBA00022510}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|ARBA:ARBA00022506}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022825}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU363062}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000256|RuleBase:RU363062}; Protease {ECO:0000256|ARBA:ARBA00022825}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484, KW ECO:0000256|RuleBase:RU363062}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363062}; KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022506}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953, KW ECO:0000256|RuleBase:RU363062}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00022506}. FT DOMAIN 1..108 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AHF51797.1" FT NON_TER 114 FT /evidence="ECO:0000313|EMBL:AHF51797.1" SQ SEQUENCE 114 AA; 12213 MW; AF27A0C5EE2528D9 CRC64; DSTVTESDIR TEEAIYQCCD LDPQARVAIR SLTERLYVGG PLTNSRGENC GYRRCRASGV LTTSCGNTLT CYIKAQAACR AAGLRDCTML VCGDDLVVIC ESAGVQEDAA XLRA //