ID B9P442_9HEPC Unreviewed; 206 AA.
AC B9P442;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
GN Name=NS3 {ECO:0000313|EMBL:ABQ95868.1};
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:ABQ95868.1};
RN [1] {ECO:0000313|EMBL:ABQ95868.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=78791b {ECO:0000313|EMBL:ABQ95868.1};
RA Mello I.M.V.G.C., Medeiros Filho J.E.M., Malta F.M., Gomes M.M.S.,
RA Pinho J.R.R., Carrilho F.J.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABQ95868.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=78791b {ECO:0000313|EMBL:ABQ95868.1};
RX PubMed=19889924; DOI=10.1099/vir.0.015594-0;
RA de Carvalho-Mello I.M., Filho J.E., Gomes-Gouvea M.S., de Mello Malta F.,
RA de Queiroz A.T., Pinho J.R., Carrilho F.J.;
RT "Molecular evidence of horizontal transmission of hepatitis C virus within
RT couples.";
RL J. Gen. Virol. 91:691-696(2010).
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; EF406158; ABQ95868.1; -; Genomic_RNA.
DR euHCVdb; EF406158; -.
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: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; 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; 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; 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 4: Predicted;
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..47
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 56..206
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABQ95868.1"
FT NON_TER 206
FT /evidence="ECO:0000313|EMBL:ABQ95868.1"
SQ SEQUENCE 206 AA; 21001 MW; B0484550789C2342 CRC64;
KGSSGGPLLC PSGHIVGIFR AAVCTRGVAK AVDFVPVESM ETTMRSPVFT DNSSPPAVPQ
TFQVAHLHAP TGSGKSTRVP AAYAAQGYKV LVLNPSVAAT LGFGAYMSKA HGVDPNIRTG
TRTITTGAPI TYSTYGKFLA DGGCSGGAYD IIICDECHST DSTSILGIGT VLDQAETAGA
RLVVLATATP PGSVTVPHPN IEEVAL
//
