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Database: UniProt
Entry: D8KY46_9HEPC
LinkDB: D8KY46_9HEPC
Original site: D8KY46_9HEPC 
ID   D8KY46_9HEPC            Unreviewed;       331 AA.
AC   D8KY46;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   Flags: Fragment;
GN   Name=NS3 {ECO:0000313|EMBL:ACJ26709.1};
OS   Hepacivirus hominis.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Hepacivirus.
OX   NCBI_TaxID=3052230 {ECO:0000313|EMBL:ACJ26709.1};
RN   [1] {ECO:0000313|EMBL:ACJ26709.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P08PG {ECO:0000313|EMBL:ACJ26709.1};
RX   PubMed=19486468; DOI=10.1111/j.1365-2893.2009.01125.x;
RA   Mello I.M., Thumann C., Schvoerer E., Soulier E., Pinho J.R.,
RA   Silvestre D.A., Queiroz A.T., Wolf P., Baumert T.F., Keller F.S.,
RA   Pereira C.A.;
RT   "Conservation of hepatitis C virus nonstructural protein 3 amino acid
RT   sequence in viral isolates during liver transplantation.";
RL   J. Viral Hepat. 16:732-737(2009).
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; EU847462; ACJ26709.1; -; mRNA.
DR   euHCVdb; EU847462; -.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; 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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR011492; Flavi_DEAD.
DR   InterPro; IPR014001; Helicase_ATP-bd.
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; PF02907; Peptidase_S29; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51822; HV_PV_NS3_PRO; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022561};
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   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
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..180
FT                   /note="Peptidase S29"
FT                   /evidence="ECO:0000259|PROSITE:PS51822"
FT   DOMAIN          189..331
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACJ26709.1"
FT   NON_TER         331
FT                   /evidence="ECO:0000313|EMBL:ACJ26709.1"
SQ   SEQUENCE   331 AA;  34151 MW;  66499634C8E8AC3C CRC64;
     ITAYAQQTRG LLGTIVTSLT GRDKNVVTGE VQVLSTATQT FLGTTVGGVM WTVYHGAGSR
     TLASAKHPAL QMYTNVDQDL VGWPAPPGAK SLEPCTCGAA DLYLVTRDAD VIPARRRGDS
     TASLLSPRPL ASLKGSSGGP VMCPSGHVAG IFRAAVCTRG VAKALQFIPV ETLNTQTRSP
     SFSDNSTPPA VPQSYQVGYL HAPTGSGKST KVPAAYVAQG YNVLVLNPSV AATLGFGSFM
     SRAYGIDPNI RTGNRTVTTG AKLTYSTYGK FLADGGCSGG AYDVIICDEC HAQDATSILG
     IGTVLDQAET AGVRLTVLAT ATPPGSITVP H
//
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