ID E9LKN9_9HEPC Unreviewed; 583 AA.
AC E9LKN9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:ADV91996.1};
RN [1] {ECO:0000313|EMBL:ADV91996.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=015C_3090_4839_4 {ECO:0000313|EMBL:ADV91996.1};
RX PubMed=21573177; DOI=10.1371/journal.pone.0019562;
RA Li H., Hughes A.L., Bano N., McArdle S., Livingston S., Deubner H.,
RA McMahon B.J., Townshend-Bulson L., McMahan R., Rosen H.R., Gretch D.R.;
RT "Genetic Diversity of Near Genome-Wide Hepatitis C Virus Sequences during
RT Chronic Infection: Evidence for Protein Structural Conservation Over
RT Time.";
RL PLoS ONE 6:E19562-E19562(2011).
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: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004153}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; HQ113479; ADV91996.1; -; Genomic_RNA.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; 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 Gene3D; 2.40.10.120; -; 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; 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; 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; PF02907; Peptidase_S29; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
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};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
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 DOMAIN 1..110
FT /note="Peptidase C18"
FT /evidence="ECO:0000259|PROSITE:PS51693"
FT DOMAIN 111..292
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 301..453
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 445..583
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADV91996.1"
FT NON_TER 583
FT /evidence="ECO:0000313|EMBL:ADV91996.1"
SQ SEQUENCE 583 AA; 61415 MW; E93D1312C43465D9 CRC64;
GLLRLCALVR KMAGGHYVQM AIIKLGTLTG TYVYNHLTPL RDWAHNGLQD LAVAVEPVVF
SQMETKLITW GADTAACGDI INGLPVSARR GREILLGPAD GMVSKGWRLL APITAYAQQT
RGLLGCIITS LTGRDKNQVE GEVQIVSTAA QTFLATCING VCWTVYHGAG TRTIASPKGP
VIQMYTNVDQ DLVGWPAPQG ARSLTPCTCG SSDLYLVTRH ADVIPVRRRG DSRGSLLSPR
PISYLKGSSG GPLLCPAGHA VGIFRAAVCT RGVAKAVDFI PVENLETTMR SPVFTDNSSP
PAVPQSFQVA HLHAPTGSGK STKVPAAYAA QGYKVLVLNP SVAATLGFGA YMSKAHGVDP
NIRTGVRTIT TGSPITYSTY GKFLADGGCS GGAYDIIICD ECHSTDATSI LGIGTVLDQA
ETAGARLVVL ATATPPGSVT VPHPNIEEVA LSTTGEIPFY GKAIPLEVIK GGRHLIFCHS
RKKCDELAAK LVALGINAVA YYRGLDVSVI PTSGDVVVVA TDALMTGFTG DFDSVIDCNT
CVTQTVDFSL DPTFTIETTT LPQDAVSRTQ RRGRTGRGKP GIY
//
