ID B6SB25_9HEPC Unreviewed; 150 AA.
AC B6SB25;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Protease-helicase {ECO:0000313|EMBL:ACH97631.1};
DE Flags: Fragment;
GN Name=NS3 {ECO:0000313|EMBL:ACH97631.1};
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:ACH97631.1};
RN [1] {ECO:0000313|EMBL:ACH97631.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=79977433K3 {ECO:0000313|EMBL:ACH97631.1};
RX PubMed=19263475; DOI=10.1002/hep.22773;
RA Gaudieri S., Rauch A., Pfafferott K., Barnes E., Cheng W., McCaughan G.,
RA Shackel N., Jeffrey G.P., Mollison L., Baker R., Furrer H., Gunthard H.F.,
RA Freitas E., Humphreys I., Klenerman P., Mallal S., James I., Roberts S.,
RA Nolan D., Lucas M.;
RT "Hepatitis C virus drug resistance and immune-driven adaptations: Relevance
RT to new antiviral therapy.";
RL Hepatology 0:0-0(2008).
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};
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DR EMBL; EU710003; ACH97631.1; -; Genomic_RNA.
DR MEROPS; S29.001; -.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
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 InterPro; IPR004109; HepC_NS3_protease.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR Pfam; PF02907; Peptidase_S29; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51822; HV_PV_NS3_PRO; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:ACH97631.1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Helicase {ECO:0000313|EMBL:ACH97631.1};
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:0000313|EMBL:ACH97631.1};
KW Protease {ECO:0000313|EMBL:ACH97631.1};
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:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT DOMAIN 1..150
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACH97631.1"
FT NON_TER 150
FT /evidence="ECO:0000313|EMBL:ACH97631.1"
SQ SEQUENCE 150 AA; 15633 MW; EA6DE044BAF5AF19 CRC64;
EVQVLSTATQ TFLGTTVGGV MWTVYHGAGS RTLAGVKHPA LQMYTNVDQD LVGWPAPPGA
KSLEPCXCGS ADLYLVTREA DVIPARRRGD STASLLSPRP LACLKGSSGG PVMCPSGHVA
GIFRAAVCTR GVAKALQFIP VETLNTQARS
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