ID D6BQ45_9HEPC Unreviewed; 155 AA.
AC D6BQ45;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=NS3 {ECO:0000313|EMBL:ADA68319.1};
DE Flags: Fragment;
GN Name=NS3 {ECO:0000313|EMBL:ADA68319.1};
OS Hepatitis C virus subtype 3a.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus; Hepacivirus hominis.
OX NCBI_TaxID=356426 {ECO:0000313|EMBL:ADA68319.1};
RN [1] {ECO:0000313|EMBL:ADA68319.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P7-B {ECO:0000313|EMBL:ADA68319.1};
RA Franco S., Comerma L., Garcia E., Perez N., Ruiz L., Clotet B.,
RA Martinez M.A., Tural C.;
RT "Impact of antiretroviral therapy interruption on HCV viral load and HCV
RT diversity in patients coinfected with HCV and HIV-1: a substudy of the
RT TIBET trial.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; FJ890483; ADA68319.1; -; Genomic_RNA.
DR euHCVdb; FJ890483; -.
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..155
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADA68319.1"
FT NON_TER 155
FT /evidence="ECO:0000313|EMBL:ADA68319.1"
SQ SEQUENCE 155 AA; 15919 MW; 91AF8130606856F1 CRC64;
LLGTIVTSLT GRDKNVVTGE VQVLSTATQT FLGTTVGGVM WTVYHGAGSR TLAGVKHPAL
QMYTNVDQDL VGWPAPPGAK SLEPCACGSA DLYLVTRDAD VIPARRRGDS TASLLSPRPL
ACLKGSSGGP VMCPSGHVAG IFRAAVCTRG VAKAL
//