ID J7JM44_9HEPC Unreviewed; 1634 AA.
AC J7JM44;
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:AFQ52630.1};
RN [1] {ECO:0000313|EMBL:AFQ52630.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BRRO6924 {ECO:0000313|EMBL:AFQ52630.1};
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}.
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; JQ801817; AFQ52630.1; -; 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: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 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 701..723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 735..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 767..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 798..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 856..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 886..1009
FT /note="Peptidase C18"
FT /evidence="ECO:0000259|PROSITE:PS51693"
FT DOMAIN 1010..1191
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 1200..1352
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1344..1521
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 24..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFQ52630.1"
FT NON_TER 1634
FT /evidence="ECO:0000313|EMBL:AFQ52630.1"
SQ SEQUENCE 1634 AA; 176569 MW; F3BFDECA31207989 CRC64;
RPQDVKFPGG GQIVGGVYLL PRRGPKLGVR ATRKTSERSQ PRGRRQPIPK ARRPEGRAWA
QPGYPWPLYG NEGMGWAGWL LSPRGSRPSW GPTDPRRRSR NLGKVIDTLT CGFADLMGYI
PLVGAPLGGA ARALAHGVRV LEDGVNYATG NLPGCSFSIF LLALLSCLTI PASAYEVRNA
SGVYHVTNDC SNASIVYEAA DMILHTPGCV PCVREGSSSR CWAALTPTLA ARNASVPTTA
IRRHVDLLVG AAAFCSAMYV GDLCGSVFLV SQLFTFSPRR HETVQDCNCS IYPGHVSGHR
MAWDMMMNWS PTAALVVSQL LRIPQAVMDM VAGAHWGVLA GLAYYSMVGN WAKVLIVMLL
FAGVDGNTQV TGGAQARTTY GLTSLFTPGP SQKIQLINTN GSWHINRTAL NCNDSLKTGF
LAALFYTHRF NSSGCPERMA SCRPIDTFDQ GWGPITYAGP SNLDQRPYCW HYAPRQCGIV
PASEVCGPVY CFTPSPVVVG TTDSSGVPTY SWGENETDVL LLNNTRPPQG NWFGCTWMNS
TGFTKTCGGP PCNIGGVGNN TLTCPTDCFR KHPEATYTKC GSGPWLTPRC MVDYPYRLWH
YPCTVNFSIF KVRMYVGGVE HRLDAACNWT RGERCGLEDR DRSELSPLLL STTEWQILPC
SFTTLPALST GLIHLHQNTV DVQYLYGIGS AVVSFAIKWE YVVLLFLLLA DARVCACLWM
MLLVAQAEAA LENLVVLNAA SVAGAHGLLS FLVFFCAAWY IKGRLVPGAA YAIYGVWPLF
LLLLALPPRA YAMDREMAAS CGGAVFIGLA LLTLSPHYKE FLARLIWWLQ YFITRAEACL
QVWIPPLNVR GGRDAIILLT CAVHPELIFS ITKILLAILG PLMVLQAGIT RVPYFVRAQG
LIRACMLVRK VAGGHYVQMA FMRLAALTGT YVYDHLTPLR DWAHASLRDL AVAVEPVVFS
DMETKIITWG ADTAACGDII LGLPVSARRG REIFLGPADS LEGQGWRLLA PITAYSQQTR
GLLGCIITSL TGRDKNQVEG EVQVVSTATQ SFLATCVNGV CWTVYHGAGS KTLAGAKGPI
SQMYTNVDQD LVGWQAPPGA RSLTPCTCGS SDLYLVTRHA DVIPVRRRGD SRGSLLSPRP
VSYLKGSSGG PLLCPSGHAV GIFRAAVCTR GVAKAVDFIP VESMETTMRS PVFTDNSSPP
AVPQTFQVAH LHAPTGSGKS TKVPAAYAAQ GYKVLVLNPS VAATLGFGAY MSKAHGVDPN
IRTGVRTITT GAPITYSTYG KFLADGGCSG GAYDIIICDE CHSTDSTTIL GIGTVLDQAE
TAGARLVVLA TATPPGSVTV PHPNIEEVAL SNIGEIPFYG KAIPIETIKG GRHLIFCHSK
KKCDELAAKL VGLGINAVAY YRGLDVSVIP TSGDVVVVAT DALMTGFTGD FDSVIDCNTC
VTQTVDFSLD PTFTIETTTV PQDAVSRSQR RGRTGRGRAG IYRFVAPGER PSGMFDSSVL
CECYDAGCAW YELTPAETSV RLRAYLNTPG LPVCQDHLEF WESVFTGLTH IDAHFLSQTK
QAGDNFPYLV AYQATVCARA QAPPPSWDQM WKCLIRLKPT LHGPTPLLYR LGAVQNEVIL
THPITKYIMA CMSA
//
