ID   O39930_9HEPC            Unreviewed;       591 AA.
AC   O39930;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU363062};
DE            EC=2.7.7.48 {ECO:0000256|RuleBase:RU363062};
DE   Flags: Fragment;
GN   Name=NS5b {ECO:0000313|EMBL:CAB10747.1};
OS   Hepacivirus hominis.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Hepacivirus.
OX   NCBI_TaxID=3052230 {ECO:0000313|EMBL:CAB10747.1};
RN   [1] {ECO:0000313|EMBL:CAB10747.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9343198;
RA   Lohmann V., Korner F., Herian U., Bartenschlager R.;
RT   "Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA
RT   polymerase and identification of amino acid sequence motifs essential for
RT   enzymatic activity.";
RL   J. Virol. 71:8416-8428(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
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; Z97730; CAB10747.1; -; Genomic_RNA.
DR   SMR; O39930; -.
DR   BindingDB; O39930; -.
DR   DrugBank; DB07199; (2S,4S,5R)-1-(4-TERT-BUTYLBENZOYL)-2-ISOBUTYL-5-(1,3-THIAZOL-2-YL)PYRROLIDINE-2,4-DICARBOXYLIC ACID.
DR   DrugBank; DB07200; (2S,4S,5R)-2-ISOBUTYL-5-(2-THIENYL)-1-[4-(TRIFLUOROMETHYL)BENZOYL]PYRROLIDINE-2,4-DICARBOXYLIC ACID.
DR   DrugBank; DB05060; R1626.
DR   DrugBank; DB08934; Sofosbuvir.
DR   euHCVdb; Z97730; -.
DR   EvolutionaryTrace; O39930; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0000166; F:nucleotide 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:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd23202; Hepacivirus_RdRp; 1.
DR   Gene3D; 3.30.70.270; -; 2.
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}; Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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:ARBA00022670};
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
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   TRANSMEM        571..588
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          214..332
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAB10747.1"
SQ   SEQUENCE   591 AA;  65754 MW;  6FA9C2F970260349 CRC64;
     SMSYTWTGAL ITPCAAEESK LPINALSNSL LRHHNMVYAT TSRSASLRQK KVTFDRLQVL
     DDHYRDVLKE MKAKASTVKA KLLSVEEACK LTPPHSAKSK FGYGAKDVRN LSSKAVNHIR
     SVWKDLLEDT ETPIDTTIMA KNEVFCVQPE KGGRKPARLI VFPDLGVRVC EKMALYDVVS
     TLPQAVMGSS YGFQYSPGQR VEFLVNTWKS KKCPMGFSYD TRCFDSTVTE NDIRVEESIY
     QCCDLAPEAR QAIRSLTERL YIGGPLTNSK GQNCGYRRCR ASGVLTTSCG NTLTCYLKAS
     AACRAAKLQD CTMLVCGDDL VVICESAGTQ EDAASLRAFT EAMTRYSAPP GDPPQPEYDL
     ELITSCSSNV SVAHDASGKR VYYLTRDPTT PLARAAWETA RHTPVNSWLG NIIMYAPTLW
     ARMILMTHFF SILLAQEQLE KALDCQIYGA CYSIEPLDLP QIIQRLHGLS AFSLHSYSPG
     EINRVASCLR KLGVPPLRVW RHRARSVRAR LLSQGGRAAT CGKYLFNWAV RTKLKLTPIP
     AASQLDLSSW FVAGYSGGDI YHSLSRARPR WFMWCLLLLS VGVGIYLLPN R
//