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Database: UniProt
Entry: B6SBC7_9HEPC
LinkDB: B6SBC7_9HEPC
Original site: B6SBC7_9HEPC 
ID   B6SBC7_9HEPC            Unreviewed;       174 AA.
AC   B6SBC7;
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:ACH97494.1};
DE   Flags: Fragment;
GN   Name=NS3 {ECO:0000313|EMBL:ACH97494.1};
OS   Hepacivirus hominis.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Hepacivirus.
OX   NCBI_TaxID=3052230 {ECO:0000313|EMBL:ACH97494.1};
RN   [1] {ECO:0000313|EMBL:ACH97494.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=7G74R317S3 {ECO:0000313|EMBL:ACH97494.1};
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; EU710490; ACH97494.1; -; Genomic_RNA.
DR   MEROPS; S29.001; -.
DR   euHCVdb; EU710490; -.
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:ACH97494.1};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Helicase {ECO:0000313|EMBL:ACH97494.1};
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:ACH97494.1};
KW   Protease {ECO:0000313|EMBL:ACH97494.1};
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..174
FT                   /note="Peptidase S29"
FT                   /evidence="ECO:0000259|PROSITE:PS51822"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACH97494.1"
FT   NON_TER         174
FT                   /evidence="ECO:0000313|EMBL:ACH97494.1"
SQ   SEQUENCE   174 AA;  18486 MW;  9095D590F42F80B4 CRC64;
     QQTRGLLGCI ITSLTGRDKN QVEGEVQIVS TATQTFLATC INGVCWTVYH GAGTRTIASP
     KGPVIQMYTN VDQDLVGWPA PQGARSLTPC TCGSSDLYLV TRHADVIPVR RRGDSRGSLL
     SPRPISYLKG SSGGPLLCPA GHVTGIFRAA VCTRGVAKAV DFIPVENLET TMRS
//
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