ID D6MZB0_9HEPC Unreviewed; 238 AA.
AC D6MZB0;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Polyprotein {ECO:0000313|EMBL:ADG62212.1};
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:ADG62212.1};
RN [1] {ECO:0000313|EMBL:ADG62212.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BR771 {ECO:0000313|EMBL:ADG62212.1};
RX PubMed=20405151; DOI=10.1007/s00705-010-0642-z;
RA Peres-da-Silva A., de Almeida A.J., Lampe E.;
RT "Mutations in hepatitis C virus NS3 protease domain associated with
RT resistance to specific protease inhibitors in antiviral therapy naive
RT patients.";
RL Arch. Virol. 155:807-811(2010).
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; GU126604; ADG62212.1; -; 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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; 2.30.30.710; Hepatitis C virus non-structural protein NS2, C-terminal domain; 1.
DR InterPro; IPR002518; HCV_NS2.
DR InterPro; IPR042205; HCV_NS2_C.
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; PS51693; HCV_NS2_PRO; 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..36
FT /note="Peptidase C18"
FT /evidence="ECO:0000259|PROSITE:PS51693"
FT DOMAIN 37..218
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT REGION 217..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADG62212.1"
FT NON_TER 238
FT /evidence="ECO:0000313|EMBL:ADG62212.1"
SQ SEQUENCE 238 AA; 25086 MW; 67032C71F05B02AF CRC64;
AACGDIILGL PVSARRGREI LLGPADSLEG QGWRLLAPIT AYFQQTRGLL GCIITSLTGR
DKNQVEGEVQ VVSTATQTFL ATCVNGVCWT VYHGAGSKTL AGPKGPITQM YTNVDQDLVG
WQAPPGARSL TPCTCGSSDL YLVTRHADVI PVRRRGDNRG SLLSPRPISY LKGSSGGPLL
CPLGHVAGVF RAAVCTRGVA KAVDFVPVES METTMRSPVF TDNSSPPAVP QTSEVAHL
//
