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Database: UniProt
Entry: K7Y6T7_9HEPC
LinkDB: K7Y6T7_9HEPC
Original site: K7Y6T7_9HEPC 
ID   K7Y6T7_9HEPC            Unreviewed;       695 AA.
AC   K7Y6T7;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
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:AFX77044.1};
RN   [1] {ECO:0000313|EMBL:AFX77044.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=V0076 {ECO:0000313|EMBL:AFX77044.1};
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; KC125083; AFX77044.1; -; 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   CDD; cd17931; DEXHc_viral_Ns3; 1.
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; NS3_Peptidase_S29.
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   SMART; SM00490; HELICc; 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:AFX77044.1};
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:AFX77044.1"
FT   NON_TER         695
FT                   /evidence="ECO:0000313|EMBL:AFX77044.1"
SQ   SEQUENCE   695 AA;  74013 MW;  374ED3938F3B863B CRC64;
     APITAYAQQT RGLLGCIITS LTGRDKNQVE GEVQIVSTAA QTFLATCING VCWTVYHGAG
     TRTLASSKGP VIQMYTNVDK DLVGWSAPQG ARSLTPCTCG SSDLYLVTRH ADVIPVRRRG
     DSRGSLLSPR PISYLKGSSG GPLLCPAGHA VGIFRAAVCT RGVAKAVDFI PVESLETTMR
     SPVFTDNSSP PAVPQSFQVA HLHAPTGSGK STKVPAAYAA QGYKVLVLNP SVAATLGFGA
     YMSKAHGIDP NIRTGVRTIT TGSPITYSTY GKFLADGGCS GGAYDIIICD ECHSTDATSI
     LGIGTVLDQA ETAGARLVVL ATATPPGSVT VPHPNIEEVA LSTTGEIPFY GKAIPLEVIK
     GGRHLIFCHS KKKCDELAAK LVALGVNAVA YYRGLDVSVI PTSGDVVVVA TDALMTGFTG
     DFDSVVDCNT CVTQTVDFSL DPTFTIETTT LPQDAVSRTQ RRGRTGRGKP GIYRFVAPGE
     RPSGMFDSSV LCECYDAGCA WYELTPAETT VRLRAYMNTP GLPVSQDHLE FWEGVFTGLT
     HIDAHFLSQT KQSGENLPYL VAYQATVCAR AQAPPPSWDQ MWKCLIRLKP TLHGPTPLLY
     RLGAVQNDVT LTHPVTKYIM TCMSADLEVV TSTWVLVGGV LAALAAYCLS TGCVVIVGRI
     VLSGKPAIIP DREVLYREFD EMEECSQHLP YIEQG
//
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