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Database: UniProt
Entry: O70783_9FLAV
LinkDB: O70783_9FLAV
Original site: O70783_9FLAV 
ID   O70783_9FLAV            Unreviewed;       143 AA.
AC   O70783;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   Flags: Fragment;
OS   GB virus C.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Pegivirus; Pegivirus hominis.
OX   NCBI_TaxID=54290 {ECO:0000313|EMBL:BAA25980.1};
RN   [1] {ECO:0000313|EMBL:BAA25980.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JA-TT {ECO:0000313|EMBL:BAA25980.1};
RX   PubMed=9512347; DOI=10.1016/S0014-5793(98)00083-0;
RA   Tanaka Y., Mizokami M., Orito E., Ohba K., Kato T., Kondo Y., Mboudjeka I.,
RA   Zekeng L., Kaptue L., Bikandou B., M'Pele P., Takehisa J., Hayami M.,
RA   Suzuki Y., Gojobori T.;
RT   "African origin of GB virus C/hepatitis G virus.";
RL   FEBS Lett. 423:143-148(1998).
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; AB010202; BAA25980.1; -; Genomic_RNA.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   4: Predicted;
KW   Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Virion {ECO:0000256|ARBA:ARBA00022804};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   DOMAIN          1..143
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAA25980.1"
FT   NON_TER         143
FT                   /evidence="ECO:0000313|EMBL:BAA25980.1"
SQ   SEQUENCE   143 AA;  15501 MW;  95A0535236B78652 CRC64;
     FKEAPLFMPT GAGKSTRVPL EYGNMGHKVL ILNPSVATVR AMGPYMERLA GKHPSIYCGH
     DTTAFTRITD SPLTYSTYGR FLANPRQMLR GVSVVICDEC HSHDSTVLLG IGRVRELARG
     CGVQLVLYAT ATPPGSPMVQ HPS
//
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