ID K7XI14_9HEPC Unreviewed; 695 AA.
AC K7XI14;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:AFX79023.1};
RN [1] {ECO:0000313|EMBL:AFX79023.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=V2055 {ECO:0000313|EMBL:AFX79023.1};
RX PubMed=23152524; DOI=10.1128/JVI.02294-12;
RA Bartels D.J., Sullivan J.C., Zhang E.Z., Tigges A.M., Dorrian J.L.,
RA De Meyer S., Takemoto D., Dondero E., Kwong A.D., Picchio G., Kieffer T.L.;
RT "Hepatitis C Virus Variants with Decreased Sensitivity to Direct-Acting
RT Antivirals (DAAs) Were Rarely Observed in DAA-Naive Patients prior to
RT Treatment.";
RL J. Virol. 87:1544-1553(2013).
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 + 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004153}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; KC127062; AFX79023.1; -; Genomic_RNA.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
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; 2.40.10.120; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.820.10; RNA Helicase Chain A , domain 3; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR000745; HCV_NS4a.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004109; HepC_NS3_protease.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF01006; HCV_NS4a; 1.
DR Pfam; PF02907; Peptidase_S29; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51822; HV_PV_NS3_PRO; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AFX79023.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT DOMAIN 1..182
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 191..343
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 335..512
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFX79023.1"
FT NON_TER 695
FT /evidence="ECO:0000313|EMBL:AFX79023.1"
SQ SEQUENCE 695 AA; 74137 MW; DFB85C00B943B06A CRC64;
APITAYAQQT RGLLGCIITS LTGRDKNQVE GEVQIVSTAT QTFLATCING VCWSIYHGAG
TRTIASPKGP VIQMYTNVDQ DLVGWPAPQG TRSLTPCTCG SSDLYLVTRH ADVIPVRRRG
DSRGGLLSPR PISYLKGSSG GPLLCPAGHA VGIFRAAVCT RGVAKAVDFI PVENLETTMR
SPVFTDNSSP PAVPQSFQVA HLHAPTGSGK STKVPAAYAA QGYKVLVLNP SVAATLGFGA
YMSKSHGIDP NIRTGVRTIT TGSPITYSTY GKFLADGGCA GGAYDIIICD ECHSTDATSI
LGIGTVLDQA ETAGARLVVL ATATPPGSVT VPHSNIEEVA LSTTGEIPFY GKAIPLEVIK
GGRHLIFCHS KKKCDEVAAK LVALGLNAVA YYRGLDVSVI PTSGDVVVVA TDALMTGYTG
DFDSVIDCNT CVTQTVDFSL DPTFTIETTT LPQDAVSRTQ RRGRTGRGKP GIYRFVAPGE
RPSGVFDSSV LCECYDAGCA WYELTPAETT VRLRAYMNTP GLPVCQDHLE FWEGVFTGLT
HIDAHFLSQT KQSGENLPYL VAYQATVCAR AQAPPPSWDQ MWKCLIRLKP TLHGPTPLLY
RLGAVQHEIT LTHPITKYIM TCMSADLEVV TSTWVLVGGV LAALAAYCLS TGCVVIVGRI
VLSGKPAVIP DREVLYREFD EMEECSXHLP YIEHG
//
