ID O89251_9FLAV Unreviewed; 2843 AA.
AC O89251;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 148.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS GB virus C.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Pegivirus; Pegivirus hominis.
OX NCBI_TaxID=54290 {ECO:0000313|EMBL:BAA69462.1, ECO:0000313|Proteomes:UP000164273};
RN [1] {ECO:0000313|EMBL:BAA69462.1, ECO:0000313|Proteomes:UP000164273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGV-GA128 {ECO:0000313|EMBL:BAA69462.1};
RA Saito T., Ishikawa K., Osei-Kwasi M., Kaneko T., Brandful J.A.M., Nuvor V.,
RA Aidoo S., Ampofo W., Apeagyei F.A., Ansah J.E., Adu-Sarkodie Y.,
RA Nkrumah F.K., Abe K.;
RT "Prevalence of hepatitis G virus and characterization of viral genome in
RT Ghana.";
RL Hepatol. Res. 13:221-231(1999).
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=Hydrolysis of four peptide bonds in the viral precursor
CC polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr
CC in P1 and Ser or Ala in P1'.; EC=3.4.21.98;
CC Evidence={ECO:0000256|ARBA:ARBA00001117};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:ARBA00004406}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00004406}. Host cytoplasm, host
CC perinuclear region {ECO:0000256|ARBA:ARBA00004407}. Host endoplasmic
CC reticulum membrane {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum
CC membrane {ECO:0000256|ARBA:ARBA00004291}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004291}. Host mitochondrion
CC {ECO:0000256|ARBA:ARBA00004181}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; AB013500; BAA69462.1; -; Genomic_RNA.
DR Proteomes; UP000164273; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; 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:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd23203; Pegivirus_RdRp; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 2.20.25.210; Hepatitis C NS5A, domain 1B; 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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR024347; GB_virus_envelope.
DR InterPro; IPR002518; HCV_NS2.
DR InterPro; IPR000745; HCV_NS4a.
DR InterPro; IPR001490; HCV_NS4b.
DR InterPro; IPR002868; HCV_NS5a.
DR InterPro; IPR013192; HCV_NS5A_1a.
DR InterPro; IPR013193; HCV_NS5a_1B_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR004109; HepC_NS3_protease.
DR InterPro; IPR038170; NS5A_1a_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002166; RNA_pol_HCV.
DR Pfam; PF12786; GBV-C_env; 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; PF08300; HCV_NS5a_1a; 1.
DR Pfam; PF08301; HCV_NS5a_1b; 1.
DR Pfam; PF02907; Peptidase_S29; 1.
DR Pfam; PF00998; RdRP_3; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 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; PS51822; HV_PV_NS3_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 4: Predicted;
KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
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 Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
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:ARBA00022632};
KW Inhibition of host interferon signaling pathway by virus
KW {ECO:0000256|ARBA:ARBA00022830};
KW Inhibition of host MAVS by virus {ECO:0000256|ARBA:ARBA00022986};
KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482};
KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023258};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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:ARBA00023065};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280};
KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022506};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 566..587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 599..622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 634..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 677..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 750..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1526..1549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1710..1737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1743..1765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1777..1800
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 769..894
FT /note="Peptidase C18"
FT /evidence="ECO:0000259|PROSITE:PS51693"
FT DOMAIN 894..1074
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 1081..1237
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 2488..2602
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2130..2178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2141..2178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2843 AA; 307912 MW; FDC781B1028675D5 CRC64;
MAVLLLLLVV EAGAILAPAT HACRANGQYF LTNCCAMEDI GFCLEGGCLV ALGCTICTDR
CWPLYQAGLA VRPGKSAAQL VGELGSLYGP LSVSAYVAGI LGLGEVYSGV LTVGVALTRR
VYPVPNLTCA VECELKWESE FWRWTEQLAS NYWILEYLWK VPFDFWRGVM SLTPLLVCVA
ALLLLEQRIV MVFLLVTMAG MSQGVPVSVL GSRPFEPGLT WQSCSCRSNG SRVPTGEHVW
DRREVSLLCD CPNGPWVWQP AFCQAIGWGD PITHWSHGQN QWPPSCPQYV YGAVSVTCVW
GSVSWFASTG GRDSKIDVWS LVPVGSASCT IAALGTSDRD VVVELFEWGV PCATCILDRR
PASCGSCVRD CWPETGSVRF PFHRCGAGPR LTRDLEAVPF VNRTTPFTIR GPLGNQGRGN
PVRSPLGFGS YTMTKIRDSL HLVECPIPAI EPPTGTFGFF PGVPPLNNCM LLGTEVSEAL
GGAGLTGGFY EPLVRRCSEL MGRRNPVCPG FAWLSSGRPD GFIHVQDHLQ EVDAGNFIPP
PRWLLLDFVF VLLYLMKLAE ARLVPLILLL LWWWVNQLVV LGLPAANAAV AGEVFAGPAL
SWCLGLPVVS MILGLANLVL YFRWMGPQRL MFLVLWKLAR GAFPLALLMG ISATRGRTSV
LGAEFCFDVT FEVDTSVLGW VVASVVAWAI ALLSSMSAGG WRHKAVIYRT WCKGYQAVRQ
RVVRSPLGEG RPTKPLTIAW CLASYIWPDA VMLVVVALVL LFGLFDALDW ALEELLVSRP
SLRRLARVVE CCVMAGEKAT TIRLVSKMCA RGAYLFDHMG SFSRAVKERL LEWDAALEPL
SFTRTDCRII RDAARTLSCG QCVMGLPVVA RRGDEVLIGV FQDVNHLPPG FVPTAPVVIR
RCGKGFLGVT KAALTGRDPD LHPGNVMVLG TATSRSMGTC LNGLLFTTFH GASSRTIATP
VGALNPRWWS ASDDVTVYPL PDGANLLTPC TCQAESCWVI RSDGALCHGL CKGDKVELDV
AMEVSDFRGS SGSPVLCDEG HAVGMLVSVL HSGGRVTAAR FTRPWTQVPT DAKTTTEPPP
VPAKGVFKEA PLFMPTGAGK STRVPLEYGN MGHKVLILNP SVATVRAMGP YMEKLAGKHP
SIFCGHDTTA FTRITDSPLT YSTYGRFLAN PRQMLRGVSV VICDECHSHD STVLLGIGRV
RELARGCGVQ LVLYATATPP GSPMTQHPSI IETKLDVGEI PFYGHGIPLE RMRTGRHLVF
CHSKAECERL AGQFFVPGGL NAIAYYRGKD SSIIKDGDLV VCATDALSTG YTGNFDSVTD
CGLVVEEVVE VTLDPTITIS LRTVPASAEL SMQRRGRTGR GRSGRYYYAG VGKAPAGVVR
SGPVWSAVEA GVTWYGMEPD LTANLLRLYD DCPYTAAVAA DIGEAAVFFS GLAPLRMHPD
VSWAKVRGVN WPLLVGVQRT MCRETLSPGP SDDPQWADLK GPNPVPLLLR WGNDLPSKVA
GHHIVDDLVR RLGVAEGYIR CDAGPILMVG LAIAGGMIYA SYTGSLVVVT DWDVKGGGNP
LYRNGDQATP QPVVQVPPVD HRPGGESAPS DAKTVTDAVA AIQVNCDWSV MTLSIGEVLT
LAQAKTAEAY AATTKWLAGC YTGTRAVPTV SIVDKLFAGG WAAVVGHCHS VIAAAVAAYG
ASRSPPLAAA ASYLMGLGVG GNAQARLASA LLLGAAGTAL GTPVVGLTMA GAFMGGASVS
PSLVTVLLGA VGGWEGVVNA ASLVFDFMAG KLSTEDLWYA IPVLTSPGAG LAGITLRLVL
YSTNNSGTTT WLNRLLTTLP RSSCIPDSYF QQADYCDKVS AMLRRLSLTR TVVALVNREP
KVDEVQVGYV WDLWEWIMPQ VRMVVSRLRA LCPVVSLPLW HCGEGWSGEW FLDGHVESRC
LCGCVITGDV LNGQLKEPVY FTKLCRHYWM GTVPVNMLGY GETSPLLASD TPKVVPFGTS
GWAEVVVTPT HVVVRRTSCY KLLRQQIFSA AVAEPYYVDG IPVSWEADAR APAMVYGPGQ
SVTIDGERYT LPHQLRMRNV APSEVSSEVS IEIGTETEDS ELTEADLPPA AAALQAIENA
ARILEPHIDV IMEDCSTPSL CGSSREMPVW GEDIPRTPSP ALISVTESSS DEKTPSVSSS
QEDTPSSDSF EVIQESDTAE SEESVFNVAL SVLKALFPQS DATRKLTVKM SCCVEKSVTR
FFSLGLTVAD VASLCEMEIQ NHTAYCDKVR TPLELQVGCL VGNELTFECD KCEARQETLA
SFSYIWSGVP LTRATPAKPP VVRPVGSLLV ADTTKVYVTN PDNVGRRVDK VTFWRSPRVH
DKFLVDSIER ARKAAQSCLS MGYTYEEAIR TVRPHAAMGW GSKVSVKDLA TPAGKMAVHD
RLQEILEGTP VPFTLTVKKE VFFKDRKEEK APRLIVFPPL DFRIAEKLIL GDPGRVAKAV
LGGAYAFQYT PNQRVKEMLK LWESKKTPCA ICVDATCFDS SITEEDVALE TELYALASDH
PEWVRALGKY YASGTMVTPE GVPVGERYCR SSGVLTTSAS NCLTCYIKVR AACERVGLKN
VSLLIAGDDC LIICERPICD PSEALGRALA SYGYACEPSY HASLDTAPFC STWLAECNAD
GKRHFFLTTD FRRPLARMSS EYSDPMASAI GYILLYPWHP ITRWVIIPHV LTCAFRGGGT
PSDPVWCQVH GNYYKFPLDK LPNIIVALHG PAALRVTADT TKTKMEAGKV LSDLKLPGLA
VHRKKAGALR TRMLRSRGWA ELARGLLWHP GLRLPPPEIA GVPGGFPLSP PYMGVVHQLD
FTAQRSRWRW LGFLALLIVA LFG
//
