ID B6SB01_9HEPC Unreviewed; 181 AA.
AC B6SB01;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Protease-helicase {ECO:0000313|EMBL:ACH97607.1};
DE Flags: Fragment;
GN Name=NS3 {ECO:0000313|EMBL:ACH97607.1};
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:ACH97607.1};
RN [1] {ECO:0000313|EMBL:ACH97607.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=79697834D7 {ECO:0000313|EMBL:ACH97607.1};
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; EU709979; ACH97607.1; -; Genomic_RNA.
DR euHCVdb; EU709979; -.
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:ACH97607.1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Helicase {ECO:0000313|EMBL:ACH97607.1};
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:ACH97607.1};
KW Protease {ECO:0000313|EMBL:ACH97607.1};
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..181
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACH97607.1"
FT NON_TER 181
FT /evidence="ECO:0000313|EMBL:ACH97607.1"
SQ SEQUENCE 181 AA; 18837 MW; 6574C1735871BB08 CRC64;
APITAYAQXT RGLFGTIVTS LTGRDRNVVT GEIQVLSTAT QTFLGTTVGG VIWTVYHGAG
SRTLAGVKHP ALQMYTNVDQ DLVGWPAPQG AKSLEPCTCG SADLYLVTRE ADVLPARRRG
DSTASLLSPR PLASLKGSSG GPVMCPSGHV AGIFRAAVCT RGVAKALQFI PVETLSTQAR
S
//
