GenomeNet

Database: UniProt
Entry: D3W7V6_9HEPC
LinkDB: D3W7V6_9HEPC
Original site: D3W7V6_9HEPC 
ID   D3W7V6_9HEPC            Unreviewed;       664 AA.
AC   D3W7V6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Polyprotein {ECO:0000313|EMBL:ADC54603.1};
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:ADC54603.1};
RN   [1] {ECO:0000313|EMBL:ADC54603.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1238 {ECO:0000313|EMBL:ADC54603.1};
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GQ848815; ADC54603.1; -; Genomic_RNA.
DR   MEROPS; C18.001; -.
DR   euHCVdb; GQ848815; -.
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..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        270..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..333
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:ADC54603.1"
FT   NON_TER         664
FT                   /evidence="ECO:0000313|EMBL:ADC54603.1"
SQ   SEQUENCE   664 AA;  72905 MW;  38E61DF670FB3D48 CRC64;
     CVIGGAGNNT LHCPTDCFRK HPDATYSRCG SGPWLTPRCL VNYPYRLWHY PCTINYTIFK
     IRMYVGGVEH RLEAACNWTR GERCDLEDRD RSELSPLLLT TTQWQVLPCS FTTLPALPTG
     LIHLHQNIVD VQYLYGVGSS IASWAIKWDY VVLLFLLLAD ARVCSCLWMM LLISQAEAAL
     ENLVVLNAAS LAGTHSLASF LVFFCLAWYL KGKWVPGAVY TFYGMWPLLL LLLALPQRAY
     ALDTEAAASC GGVVLVGLMA LTLSPYYKHY ISWCLWWLQY FLTRVEALLH VWIPPLNVRG
     GRDAVILLMC AVHPTLVFDI TKLLLAVFGP LWILQANLLK VPYFVRVQGL LRFCALARKM
     IGGHYVQMVI IKLGALTGTY VYNHLTPLRD WAHNGLRDLA VAVEPVVFSQ METKLITGGA
     DTAACGDIID GLPVSARRGR EILLGPADGM VSKGWRLLAP ITAYAQQTRG LLGCIITSLT
     GRDKNQVEGE VQIVSTAAQT FLATCINGVC WTVYHGAGTR TIASPKGPVI QMYTNVDQDL
     VGWPASQGSR SLTPCTCGSS DLYLVTRHAD VIPVRRRGDS RGSLLSPRPI SYLKGSSGGP
     LLCPAGHAVG IFRAAVCTRG VAKAVDFIPV ENLETTMRSP VFTDNSSPPV VPQSFQVAHL
     HAPT
//
DBGET integrated database retrieval system