ID B6SB15_9HEPC Unreviewed; 181 AA.
AC B6SB15;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Protease-helicase {ECO:0000313|EMBL:ACH97621.1};
DE Flags: Fragment;
GN Name=NS3 {ECO:0000313|EMBL:ACH97621.1};
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:ACH97621.1};
RN [1] {ECO:0000313|EMBL:ACH97621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=78387783K6 {ECO:0000313|EMBL:ACH97621.1};
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU709993; ACH97621.1; -; Genomic_RNA.
DR MEROPS; S29.001; -.
DR euHCVdb; EU709993; -.
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:ACH97621.1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Helicase {ECO:0000313|EMBL:ACH97621.1};
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:ACH97621.1};
KW Protease {ECO:0000313|EMBL:ACH97621.1};
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:ACH97621.1"
FT NON_TER 181
FT /evidence="ECO:0000313|EMBL:ACH97621.1"
SQ SEQUENCE 181 AA; 18825 MW; 0E1A15A52F8E7D69 CRC64;
APITAYAQQX XXLLGTIVTS LTGRDKNVVT GEVQVLSTAT QTFLGTTVGG VMWTVYHGAG
SRTLAGAKHP ALQMYTNVDQ DLVGWPAPPG AKSLEPCTCG SADLYLVTRD ADVIPARRRG
DSTASLLSPR PLACLKGSSG GPVMCPSGHV AGIFRAAVCT RGVAKALQFI PVETLNTQXR
S
//
