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Database: UniProt
Entry: Q80M10_9HEPC
LinkDB: Q80M10_9HEPC
Original site: Q80M10_9HEPC 
ID   Q80M10_9HEPC            Unreviewed;       180 AA.
AC   Q80M10;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Polyprotein {ECO:0000313|EMBL:BAC67095.1};
DE   Flags: Fragment;
GN   Name=NS3 {ECO:0000313|EMBL:BAC67095.1};
OS   Hepacivirus hominis.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Hepacivirus.
OX   NCBI_TaxID=3052230 {ECO:0000313|EMBL:BAC67095.1};
RN   [1] {ECO:0000313|EMBL:BAC67095.1}
RP   NUCLEOTIDE SEQUENCE.
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; AB089546; BAC67095.1; -; Genomic_RNA.
DR   MEROPS; S29.001; -.
DR   euHCVdb; AB089546; -.
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; NS3_Peptidase_S29.
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:BAC67095.1"
FT   NON_TER         180
FT                   /evidence="ECO:0000313|EMBL:BAC67095.1"
SQ   SEQUENCE   180 AA;  18938 MW;  27D59A972343B29D CRC64;
     APITAYSQQT RGLLGCIITS LTGRDKNQVE GEVQVVSTAT QSFLATCVNG VCWTVYHGAG
     SKTLAGPKGP ITQMYTNVDQ DLVGWQAPPG ARSLTPCTCG SSDLYLVTRH ADVIPVRRRG
     DGRGSLLSPR PVSYLKGSSG GPLLCPSGHV VGIFRAAVCT RGVAKAVDFV PVESMETTMR
//
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