ID D3W7R1_9HEPC Unreviewed; 1249 AA.
AC D3W7R1;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
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:ADC54558.1};
RN [1] {ECO:0000313|EMBL:ADC54558.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=603 {ECO:0000313|EMBL:ADC54558.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001491};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Host cell
CC membrane {ECO:0000256|ARBA:ARBA00004165}. Host endoplasmic reticulum
CC membrane {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004153}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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; GQ848761; ADC54558.1; -; Genomic_RNA.
DR MEROPS; S29.001; -.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0039563; P:disruption by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039527; P:disruption by virus of host TRAF-mediated signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039645; P:perturbation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; cd17931; DEXHc_viral_Ns3; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 6.10.250.1610; -; 1.
DR Gene3D; 6.10.250.1750; -; 1.
DR Gene3D; 6.10.250.2920; -; 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.820.10; RNA Helicase Chain A , domain 3; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR002518; HCV_NS2.
DR InterPro; IPR042205; HCV_NS2_C.
DR InterPro; IPR042209; HCV_NS2_N.
DR InterPro; IPR000745; HCV_NS4a.
DR InterPro; IPR001490; HCV_NS4b.
DR InterPro; IPR002868; HCV_NS5a.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004109; HepC_NS3_protease.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF01538; HCV_NS2; 1.
DR Pfam; PF01006; HCV_NS4a; 1.
DR Pfam; PF01001; HCV_NS4b; 1.
DR Pfam; PF01506; HCV_NS5a; 1.
DR Pfam; PF02907; Peptidase_S29; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51693; HCV_NS2_PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51822; HV_PV_NS3_PRO; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022506};
KW G1/S host cell cycle checkpoint dysregulation by virus
KW {ECO:0000256|ARBA:ARBA00023309};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022961};
KW Inhibition of host interferon signaling pathway by virus
KW {ECO:0000256|ARBA:ARBA00022961};
KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022647};
KW Inhibition of host STAT1 by virus {ECO:0000256|ARBA:ARBA00022961};
KW Inhibition of host TRAFs by virus {ECO:0000256|ARBA:ARBA00022647};
KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00022961};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Modulation of host cell cycle by virus {ECO:0000256|ARBA:ARBA00022504};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
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 Viral immunoevasion {ECO:0000256|ARBA:ARBA00022961};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
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 TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 886..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1073..1096
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1108..1128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..252
FT /note="Peptidase C18"
FT /evidence="ECO:0000259|PROSITE:PS51693"
FT DOMAIN 253..434
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 443..595
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 587..764
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADC54558.1"
FT NON_TER 1249
FT /evidence="ECO:0000313|EMBL:ADC54558.1"
SQ SEQUENCE 1249 AA; 134410 MW; B76AC58E554A6D13 CRC64;
AWYLKGKWVP GAVYTFYGMW PLLLLLLALP QRAYALDTEV AASCGGVVLV GLMALTLSPY
YKRYISWCLW WLQYFLTRVE AQLHVWIPPL NVRGGRDACI LLMCAVHPTL VFDITKLLLA
VFGPLWILQA SLLKVPYFVR VQGLLRFCAL ARKMIGGHYV QMVIIKLGAL TGTYVYNHLT
PLRDWAHNGL RDLAVAVEPV VFSQMETKLI TWGADTAACG DIINGLPVSA RRGREILLGP
ADGMVSKGWR LLAPITAYAQ QTRGLLGCII TSLTGRDKDQ VEGEVQIVST AAQTFLATCI
NGVCWTVYHG AGTRTIAPPK GPVIQMYTNV DQDLVGWPAP QGTRSLTPCT CGSSDLYLVT
RHADVIPVRR QGDSRGSLLS PRPISYLKGS SGGPLLCPAG HAVGIFRAAV CTRGVAKAVD
FIPVENLETT MRSPVFTDNS SPPVVPQSFQ VAHLHAPTGS GKSTKVPAAY AAQGYKVLVL
NPSVAATLGF GAYMVQAHGI DPNIRTGVRT ITTGSPITYS TYGKFLADGG CSGGAYDIII
CDECHSTDAT SILGIGTVLD QAETAGARLV VLATATPPGS VTVPHPNIEE VALSTTGEIP
FYGKAIPLEA IKGGRHLIFC HSKKKCDELA AKLVALGINA VAYYRGLDVS VIPTSGDVVV
VATDALMTGY TGDFESVIDC NTCVTQTVDF SLDPTFTIET ITLPQDAVSR TQRRGRTGRG
KPGIYRFVAP GERPSGMFDS SVLCECYDAG CAWYELTPAE TTVRLRAYMN TPGLPVCQDH
LEFWEGVFTG LTHIDAHFLS QTKQSGENLP YLVAYQATAC ARAQAPPPSW DQMWKCLIRL
KPTLHGPTPL LYRLGAVQNE ITLTHPVTKY IMTCMSADLE VVTSTWVLVG GVLAALAAYC
LSTGCVVIVG RIILSGKPAI IPDREVLYRE FDEMEECSQH LPYIEQGMVL AEQFKQKALG
LLQTASRQAE VIAPAVQTNW QKIETFWAKH MWNFISGIQY LAGLSTLPDN PAIASLMAFT
AAVTSPLTTS QTLLFNILGG WVAAQLAAPG AATAFVGAGL AGAAIGSVGL GKVLVDILAG
YGAGVAGALV AFKIMSGEVP STEDLVNLLP AILSPGALVV GVVCAAILRR HVGPGEGAVQ
WMNRLIAFAS RGNHVSPTHY VPESDAATRV TAILSSLTVT QLLRRLHQWL SSECTTPCSG
SWLRDIWDWI CEVLSDFKVW LKAKLMPQLP GIPFVSCQRG YKGVWRVEG
//
