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Database: UniProt
Entry: D3W8V4_9HEPC
LinkDB: D3W8V4_9HEPC
Original site: D3W8V4_9HEPC 
ID   D3W8V4_9HEPC            Unreviewed;       665 AA.
AC   D3W8V4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Polyprotein {ECO:0000313|EMBL:ADC54704.1};
DE   Flags: Fragment;
OS   hepatitis C virus genotype 1a.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Hepacivirus; Hepacivirus hominis.
OX   NCBI_TaxID=2847144 {ECO:0000313|EMBL:ADC54704.1};
RN   [1] {ECO:0000313|EMBL:ADC54704.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1/910 {ECO:0000313|EMBL:ADC54704.1};
RX   PubMed=19918975; DOI=10.1002/hep.23319;
RA   Fuller M.J., Shoukry N.H., Gushima T., Bowen D.G., Callendret B.,
RA   Campbell K.J., Hasselschwert D.L., Hughes A.L., Walker C.M.;
RT   "Selection-driven immune escape is not a significant factor in the failure
RT   of CD4 T cell responses in persistent hepatitis C virus infection.";
RL   Hepatology 51:378-387(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; GQ870511; ADC54704.1; -; Genomic_RNA.
DR   euHCVdb; GQ870511; -.
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   CDD; cd20903; HCV_p7; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   Gene3D; 6.10.250.1610; -; 1.
DR   Gene3D; 6.10.250.1750; -; 1.
DR   Gene3D; 2.30.30.710; Hepatitis C virus non-structural protein NS2, C-terminal domain; 1.
DR   Gene3D; 1.20.1280.150; Hepatitis C virus non-structural protein NS2, N-terminal domain; 1.
DR   InterPro; IPR002531; HCV_NS1.
DR   InterPro; IPR002518; HCV_NS2.
DR   InterPro; IPR042205; HCV_NS2_C.
DR   InterPro; IPR042209; HCV_NS2_N.
DR   InterPro; IPR004109; HepC_NS3_protease.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   Pfam; PF01560; HCV_NS1; 1.
DR   Pfam; PF01538; HCV_NS2; 1.
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, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
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   TRANSMEM        150..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          331..458
FT                   /note="Peptidase C18"
FT                   /evidence="ECO:0000259|PROSITE:PS51693"
FT   DOMAIN          459..640
FT                   /note="Peptidase S29"
FT                   /evidence="ECO:0000259|PROSITE:PS51822"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADC54704.1"
FT   NON_TER         665
FT                   /evidence="ECO:0000313|EMBL:ADC54704.1"
SQ   SEQUENCE   665 AA;  73189 MW;  DA3D157B6827E048 CRC64;
     CVIGGAGNNT LHCPTDCFRK HPDATYSRCG SGPWITPRCL VDYPYRLWHY PCTINYTIFK
     IRMYVGGVEH RLEAACNWTR GERCDLEDRD RSELSPLLLT TTQWQVLPCS FTTLPALSTG
     LIHLHQDIVD VQYLYGVGSS IASWAIKWEY VVLLFLLLAD ARVCSCLWMM LLISQAEAAL
     ENLVILNAAS LAGTHGLVSF LVFFCFAWYL KGKWVPGAVY TFYGMWPLLL LLLALPQRAY
     ALDTEVAASC GGVVLVGLMA LTLSPYYKRY ISWCLWWLQY FLTRVEAQLH VWIPPLNVRG
     GRDAVILLMC AVHPTLVFDI TKLLLAVFGP LWILQASLLK VPYFVRVQGL LRFCALARKM
     IGGHYVQMVI IKLGALTGTY VYNHLTPLRD WAHNGLRDLA VAVEPVVFSQ METKLITWGA
     DTAACGDIIN GLPVSARRGR EILLGPADGM VSKGWRLLAP ITAYAQQTRG LLGCIITSLT
     GRDKNQVEGE VQIVSTAAQT FLATCINGVC WTVYHGAGTR TIASPKGPVI QMYTNVDQDL
     VGWPAPQGSR SLTPCTCGSS DLYLVTRHAD VIPVRRRGDS RGSLLSPRPI SYLKGSSGGP
     LLCPAGHAVG IFRAAVCTRG VAKAVDFIPV ENLETTMRSP VFTDNSSPPV VPESFQVAHL
     HAPTG
//
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