ID E9LL77_9HEPC Unreviewed; 414 AA.
AC E9LL77;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:ADV92184.1};
RN [1] {ECO:0000313|EMBL:ADV92184.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=630C_3567_4808_2 {ECO:0000313|EMBL:ADV92184.1};
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; HQ113679; ADV92184.1; -; 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: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: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; 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; IPR014001; Helicase_ATP-bd.
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; 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; PS51192; HELICASE_ATP_BIND_1; 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 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
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..133
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 142..294
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADV92184.1"
FT NON_TER 414
FT /evidence="ECO:0000313|EMBL:ADV92184.1"
SQ SEQUENCE 414 AA; 43245 MW; FEAC89A1AB6870DC CRC64;
GVCWTVYHGA GTRTIASPKG PVIQMYTNVD QDLVGWPAPH GARSLTPCTC GSSDLYLVTR
HADVIPVRRR GDSRGSLLSP RPISYLKGSS GGPLLCPAGH AVGIFRAAVC TRGVAKAVDF
IPVESLETTM RSPVFTDNSS PPAVPQSFQV AHLHAPTGSG KSTKVPAAYA AQGYKVLVLN
PSVAATLGFG AYMSKAHGID PNIRTGVRTI TTGSSITYST YGKFLADGGC SGGAYDIIIC
DECHSTDATS ILGIGTVLDQ AETAGARLVV LATATPPGSV TVPHPNIEEV ALSTTGEIPF
YGKAIPLEVI KGGRHLIFCH SKKKCDELAT KLVALGINAV AYYRGLDVSV IPTSGDVVVV
ATDALMTGFT GDFDSVIDCN TCVTQTVDFS LDPTFTIETT TIPQDAVSRT QREG
//
