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Database: UniProt
Entry: I0IWM1_9HEPC
LinkDB: I0IWM1_9HEPC
Original site: I0IWM1_9HEPC 
ID   I0IWM1_9HEPC            Unreviewed;       300 AA.
AC   I0IWM1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Polyprotein {ECO:0000313|EMBL:BAM09670.1};
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:BAM09670.1};
RN   [1] {ECO:0000313|EMBL:BAM09670.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ME070516 {ECO:0000313|EMBL:BAM09670.1};
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; AB709278; BAM09670.1; -; 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: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   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; NS3_Peptidase_S29.
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   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:BAM09670.1"
FT   NON_TER         300
FT                   /evidence="ECO:0000313|EMBL:BAM09670.1"
SQ   SEQUENCE   300 AA;  31257 MW;  185752BBE33773E4 CRC64;
     APITAYSQQT RGLLGCIITS LTGRDKNQVE GEVQVVSTAT QSFLATCVNG VCWTVYHGAG
     SKTLAGPKGP ITQMYTNVDQ DLVGWQAPPG ARSLTPCTCG SSDLYLVTRH ADVIPVRRRG
     DNRGSLLSPR PVSYLKGSSG GPLLCPSGHA VGIFRAAVCT RGVAKAVDFI PVESMETTMR
     SPVFTDNSSP PAVPQTFQVA HLHAPTGSGK STKVPAAYAA QGYKVLVLNP SVAATLGFGA
     YMSKAHGVDP NIRTGVRTIT TGAPITYSTY GKFLADGGCS GGAYDIIICD ECHSTDSTSI
//
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