ID Q8QVY4_9HEPC Unreviewed; 180 AA.
AC Q8QVY4;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Polyprotein {ECO:0000313|EMBL:BAB88273.1};
DE Flags: Fragment;
OS Hepatitis C virus subtype 1b.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus; Hepacivirus hominis.
OX NCBI_TaxID=31647 {ECO:0000313|EMBL:BAB88273.1};
RN [1] {ECO:0000313|EMBL:BAB88273.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=53 {ECO:0000313|EMBL:BAB88273.1};
RX PubMed=12843009; DOI=10.1128/JCM.41.7.2835-2841.2003;
RA Ogata S., Florese R.H., Nagano-Fujii M., Hidajat R., Deng L., Ku Y.,
RA Yoon S., Saito T., Kawata S., Hotta H.;
RT "Identification of hepatitis C virus (HCV) subtype 1b strains that are
RT highly, or only weakly, associated with hepatocellular carcinoma on the
RT basis of the secondary structure of an amino-terminal portion of the HCV
RT NS3 protein.";
RL J. Clin. Microbiol. 41:2835-2841(2003).
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; AB072091; BAB88273.1; -; Genomic_RNA.
DR MEROPS; S29.001; -.
DR euHCVdb; AB072091; -.
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..180
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAB88273.1"
FT NON_TER 180
FT /evidence="ECO:0000313|EMBL:BAB88273.1"
SQ SEQUENCE 180 AA; 18991 MW; 9B8ECD8580EB5131 CRC64;
APITAYSQQT RGLLGCIITS LTGRDKNQVE GEVQVVSTAT QSFLATCVSG VCWTVYHGAG
SKTLAGPKGP ITQMYTNVDQ DLVGWPAPPG ARSLTPCTCG SSDLYLVTRH ADVIPVRRRG
DNRGSLLSPR PISYLKGSSG GPLLCPSGHL VGIFRAPVCT RGVAKAVDFV PVESMETTMR
//