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Database: UniProt
Entry: H3K2Z9_9HEPC
LinkDB: H3K2Z9_9HEPC
Original site: H3K2Z9_9HEPC 
ID   H3K2Z9_9HEPC            Unreviewed;       300 AA.
AC   H3K2Z9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=NS3 protease {ECO:0000313|EMBL:BAL49529.1};
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:BAL49529.1};
RN   [1] {ECO:0000313|EMBL:BAL49529.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KF050607 {ECO:0000313|EMBL:BAL49529.1};
RA   Suzuki F., Sezaki H., Akuta N., Suzuki Y., Seko Y., Kawamura Y., Hosaka T.,
RA   Kobayashi M., Saito S., Arase Y., Ikeda K., Kobayashi M., Mineta R.,
RA   Watahiki S., Miyakawa Y., Kumada H.;
RT   "Prevalence of hepatitis C virus variants resistant to NS3 protease
RT   inhibitors or the NS5A inhibitor (BMS-790052) in hepatitis patients with
RT   genotype 1b.";
RL   J. Clin. Virol. 54:352-354(2012).
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   -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|ARBA:ARBA00004328}.
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DR   EMBL; AB693837; BAL49529.1; -; Genomic_RNA.
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: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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR004109; HepC_NS3_protease.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   Pfam; PF02907; Peptidase_S29; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   Protease {ECO:0000313|EMBL:BAL49529.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
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:BAL49529.1"
FT   NON_TER         300
FT                   /evidence="ECO:0000313|EMBL:BAL49529.1"
SQ   SEQUENCE   300 AA;  31275 MW;  116319A705BD611C CRC64;
     APITAYSQQT RGLLGCIITS LTGRDKNQVE GEVQVVSTAT QSFLATCVNG VCWTVYHGAG
     SKTLAGPKGP ITQMYTNVDR DLVGWQAPPG ARSMTPCTCG SSDLYLVTRH ADVIPVRRRG
     DSRGSLLSPR PVSYLKGSSG GPLLCPSGHV AGIFRAAVCT RGVAKAVDFV PVESMETTMR
     SPVFTDNSSP PAVPQTFQVA HLHAPTGSGK STKVPAAYAA QGYKVLVLNP SVAATLGFGA
     YMSKAYGVDP NVRTGVRTIT TGAPLTYSTY GKFLADGGCS GGAYDIIICD ECHSTDSTSI
//
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