ID D7USI2_9HEPC Unreviewed; 183 AA.
AC D7USI2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Nonstructural polyprotein 3 {ECO:0000313|EMBL:BAJ10185.1};
DE Flags: Fragment;
GN Name=NS3 {ECO:0000313|EMBL:BAJ10185.1};
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:BAJ10185.1};
RN [1] {ECO:0000313|EMBL:BAJ10185.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YP-29 {ECO:0000313|EMBL:BAJ10185.1};
RX PubMed=20572079; DOI=10.1002/jmv.21818;
RA Sanjo M., Saito T., Ishii R., Nishise Y., Haga H., Okumoto K., Ito J.,
RA Watanabe H., Saito K., Togashi H., Fukuda K., Imai Y., El-Shamy A.,
RA Deng L., Shoji I., Hotta H., Kawata S.;
RT "Secondary structure of the amino-terminal region of HCV NS3 and
RT virological response to pegylated interferon plus ribavirin therapy for
RT chronic hepatitis C.";
RL J. Med. Virol. 82:1364-1370(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};
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DR EMBL; AB548081; BAJ10185.1; -; Genomic_RNA.
DR euHCVdb; AB548081; -.
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: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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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 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..182
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAJ10185.1"
FT NON_TER 183
FT /evidence="ECO:0000313|EMBL:BAJ10185.1"
SQ SEQUENCE 183 AA; 19283 MW; DA3CF8D18788476F CRC64;
APITAYAQQT RGLLGCIITS LTGRDKNQVE GEVQVVSTAT QSFLATCVNG VCWTVFHGAG
SKTLAGPKGP ITQMYTNVDQ DLVGWQAPPG ARSMTPCTCG SSDLYLVTRH ADVIPVCRRG
DSRGSLLSPR PVSYLKGSSG GPLLCPSGHV VGIFRAAVCT RGVAKAVDFV PVESMETTMR
LRL
//