ID J4B0H1_9HEPC Unreviewed; 1635 AA.
AC J4B0H1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:AFQ54129.1};
RN [1] {ECO:0000313|EMBL:AFQ54129.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=6213.10 {ECO:0000313|EMBL:AFQ54129.1};
RX PubMed=22927816; DOI=10.1371/journal.ppat.1002880;
RA Li H., Stoddard M.B., Wang S., Blair L.M., Giorgi E.E., Parrish E.H.,
RA Learn G.H., Hraber P., Goepfert P.A., Saag M.S., Denny T.N., Haynes B.F.,
RA Hahn B.H., Ribeiro R.M., Perelson A.S., Korber B.T., Bhattacharya T.,
RA Shaw G.M.;
RT "Elucidation of hepatitis C virus transmission and early diversification by
RT single genome sequencing.";
RL PLoS Pathog. 8:e1002880-e1002880(2012).
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Endoplasmic
CC reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I
CC membrane protein {ECO:0000256|ARBA:ARBA00004115}. Host cytoplasm
CC {ECO:0000256|ARBA:ARBA00004192}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004482}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004482}. Host lipid droplet
CC {ECO:0000256|ARBA:ARBA00004338}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Lipid droplet
CC {ECO:0000256|ARBA:ARBA00004502}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004563}.
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DR EMBL; JQ803350; AFQ54129.1; -; Genomic_RNA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044186; C:host cell lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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:0005198; F:structural molecule activity; IEA:InterPro.
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 CDD; cd17931; DEXHc_viral_Ns3; 1.
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; 3.30.160.890; Hepatitis C virus envelope glycoprotein E1, chain C; 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; IPR002521; HCV_Core_C.
DR InterPro; IPR044896; HCV_core_chain_A.
DR InterPro; IPR002522; HCV_core_N.
DR InterPro; IPR002519; HCV_Env.
DR InterPro; IPR002531; HCV_NS1.
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; PF01543; HCV_capsid; 1.
DR Pfam; PF01542; HCV_core; 1.
DR Pfam; PF01539; HCV_env; 1.
DR Pfam; PF01560; HCV_NS1; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
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 cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
KW Host lipid droplet {ECO:0000256|ARBA:ARBA00023190};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host mitochondrion {ECO:0000256|ARBA:ARBA00023147};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879};
KW Viral nucleoprotein {ECO:0000256|ARBA:ARBA00023086};
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 702..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 736..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 799..816
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 857..885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 883..1010
FT /note="Peptidase C18"
FT /evidence="ECO:0000259|PROSITE:PS51693"
FT DOMAIN 1011..1192
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 1201..1353
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1345..1522
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 25..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFQ54129.1"
FT NON_TER 1635
FT /evidence="ECO:0000313|EMBL:AFQ54129.1"
SQ SEQUENCE 1635 AA; 177394 MW; 60E6C9A58117D7F7 CRC64;
RRPQDVKFPG GGQIVGGVYL LPRRGPRLGV RATRKTSERS QPRGRRQPIP KARRPEGRTW
AQPGYPWPLY GNEGCGWAGW LLSPRGSRPS WGPTDPRRRS RNLGKVIDTL TCGFADLMGY
IPLVGAPLGG AARALAHGVR VLEDGVNYAT GNLPGCSFSI FLLALLSCLT VPASAYQVRN
SSGLYHVTND CPNSSIVYET ADTILHSPGC VPCVREGNAS KCWVAVAPTV ATRDGRLPTT
QLRRHIDLLV GSATLCSALY VGDLCGSVFL VGQLFTFSPR RHWTTQDCNC SIYPGHITGH
RMAWDMMMNW SPTAALVVAQ LLRVPQAILD MIAGAHWGVL AGIAYFSMVG NWAKVLVVLL
LFAGVDAGTH ITGGSVAHST ARLTGLFSRG SQQHIQLINT NGSWHINRTA LNCNESLNTG
WLAGLFYSNK FNSSGCPERL ASCRPLADFD QGWGPISYAN GSGPDHRPYC WHYPPKPCGI
VPAQSVCGPV YCFTPSPVVV GTTNKLGAPT YNWGCNDTDV FVLNNTRPPL GNWFGCTWMN
SSGFTKVCGA PPCVIGGGGN NTLHCPTDCF RKHPEATYSR CGSGPWITPR CLVHYPYRLW
HYPCTVNYTM FKVRMYVGGV EHRLDVACNW TRGERCDLDD RDRSELSPLL LSTTQWQVLP
CSFTTLPALT TGLIHLHQNI VDVQYLYGVG SSIVSWAIKW EYVILLFLLL ADARICSCLW
MMLLISQAEA ALENLVLLNA ASLAGTHGLA SFLVFFCFAW YLKGKWAPGA AYAFYGMWPL
LLLLLALPQR AYALDTEMAA SCGGVVIVGL MALTLSPHYK RYISWCLWWL QYFLTRVEAQ
LHVWVPPLNV RGGRDAVILL MCAVHPALVF DITKLLLAVF GPLWILQTSL LKVPYFVRVQ
GLLRICALAR KMAGGHYVQM AIIKMGALTG TYVYNHLTPL RDWAHNGLRD LAVAVEPVVF
SQMETKLITW GADTAACGDI INGLPVSARR GREILLGPAD GMVSKGWRLL APITAYAQQT
RGLLGCIITS LTGRDKNQVE GEVQIVSTAA QTFLATCING VCWTVYHGAG TRTIASPKGP
VIQMYTNVDQ DLVGWPAPQG ARSLTPCTCG SSDLYLVTRH ADVIPVRRRG DSRGSLLSPR
PISYLKGSSG GPLLCPAGHA VGIFRAAVCT RGVAKAVDFI PVESLETTMR SPVFTDNSSP
PAVPQSFQVA HLHAPTGSGK STKVPAAYAA QGYKVLVLNP SVAATLGFGA YMSKAHGVDP
NIRTGVRTIT TGSSITYSTY GKFLADGGCS GGAYDIIICD ECHSTDATSI LGIGTVLDQA
ETAGARLVVL ATATPPGSVT VPHPNIEEVA LSTTGEIPFY GKAIPLEAIK GGRHLIFCHS
KKKCDELAAK LVAMGINAVA YYRGLDVSVI PTSGDVVVVA TDALMTGYTG DFDSVIDCNT
CVTQTVDFSL DPTFTIETTT LPQDAVSRTQ RRGRTGRGKP GIYRFVAPVE RPSGMFDSSV
LCECYDAGCA WYELTPAETT VRLRAYMNTP GLPVCQDHLE FWEGVFTGLT HIDAHFLSQT
KQSGENFPYL VAYQATVCAR AQAPPPSWDQ MWKCLIRLKP TLHGPTPLLY RLGAVQNEVT
LTHPITKYIM TCMSA
//
