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Database: UniProt
Entry: J7JM62_9HEPC
LinkDB: J7JM62_9HEPC
Original site: J7JM62_9HEPC 
ID   J7JM62_9HEPC            Unreviewed;      1614 AA.
AC   J7JM62;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
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:AFQ52650.1};
RN   [1] {ECO:0000313|EMBL:AFQ52650.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GOTO90002 {ECO:0000313|EMBL:AFQ52650.1};
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; JQ801837; AFQ52650.1; -; 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:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019049; P:mitigation of host antiviral defense response; 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: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; NS3_Peptidase_S29.
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 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   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..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        737..762
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        769..786
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        798..815
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        875..897
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          887..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          1360..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:AFQ52650.1"
FT   NON_TER         1614
FT                   /evidence="ECO:0000313|EMBL:AFQ52650.1"
SQ   SEQUENCE   1614 AA;  174375 MW;  6300418DE116B8C4 CRC64;
     RRPQDVKFPG GGQIVGGVYL LPRRGPRLGV RATRKTSERS QPRGRRQPIP KARRPEGRSW
     AQPGYPWPLY GNEGMGWAGW LLSPRGSRPS WGPTDPRRRS RNLGKVIDTL TCGFADLMGY
     IPLVGAPLGG AARALAHGVR VLEDGVNYAT GNLPGCSFSI FLLALLSCLT IPASAYEVRN
     VSGVYHVTND CSNSSIVYEA ADMIMHTPGC VPCVRENNSS RCWVALTPTL AARNASIPTT
     TIRRHVDLLV GAAALCSAMY VGDLCGSVFL VSQLFTFSPR RHETVQDCNC SIYPGHVSGH
     RMAWDMMMNW SPTTALVVSQ LLRIPQAVVD MVAGAHWGVL AGLAYYSMAA NWAKVLVVLL
     LFAGVDGSTY TTGGAAGRKT HGFTSIFSSG ASQNIQLINT NGSWHINRTA LNCNDSLSTG
     FLAALFYTHK FNASGCPERM ASCRPIDKFD QGWGPITYAE PGDSDQRPYC WHYAPRPCGI
     VPAAQVCGPV YCFTPSPVVV GTTDRSGVPT YTWGENETDV LLLNNTRPPQ GNWFGCTWMN
     NTGFTKTCGG PPCNIGGSGN NTLTCPTDCF RKHPEATYTK CGSGPWLTPR CLVDYPYRLW
     HYPCTVNYTI FKVRMYVGGV EHRLNAACNW TRGERCNLED RDRSELSPLL LSTTEWQVLP
     CSFTTLPALS TGLIHLHQNI VDVQYLYGIG SAVVSFAIKW EYVLLLFLFL ADARVCACLW
     MMLLIAQAEA ALENLVVLNA ASVAGAHGTL SFLVFFCAAW YIKGRLVPGA AYAFYGVWPL
     LLLLLALPPR AYAMDRETAA SCGGAVFLGL VLLTLSPRYK EFLAKLIWWL QYFITRAEAA
     LQVWIPPLNV RGGRDAIILL TCAVHPELVF DITKLLLAIL GPLMVLQAGI TKVPYFVRAH
     GLIRACALVR KAAGGHYVQM ALMKLAALTG TYVYDHLTPL QDWAHASLRD LAVAVEPVVF
     SDMETKVITW GADTAACGDI ILGLPVSARR GREILLGPAD SFEGQGWRLL APITAYAQQT
     RGLLGCIVTS LTGRDRNQVE GEVQVVSTAT QSFLATCING VCWTVYHGAG SKPLAGPKGP
     ITQMYTNVDQ DLVGWQAPPG ARSLTPCTCG SSDLYLVTRH ADVIPVRRRG DSRGSLLSPR
     PVSYLKGSSG GPLLCPSGHA VGIFRAAVCT RGVAKAVDFV PVESMETTMR SPVFTDNSTP
     PAVPQTFQVA HLHAPTGSGK STKVPAAYAA QGYKVLVLNP SVAATLGFGA YMSKAHGVDP
     NIRTGVRTIT TGAPITYSTY GKFLADGGCS GGAYDIIICD ECHSTDSTSI LGIGTVLDQA
     ETAGARLVVL ATATPPGSVT VPHPNIEEVA LSNIGEIPFY GKAIPIELIK GGRHLIFCHS
     KKKCDELAAK LSGLGINAVA YYRGLDVSVI PTSGDVVVVA TDALMTGFTG DFDSVIDCNT
     CVTQTVDFSL DPTFTIETTT VPQDAVSRSQ RRGRTGRGRG GVYRFVTPGE RPSGMFDSSV
     LCECYDAGCA WYELTPAETT VRLRAYLNTP GLPVCQDHLE FWEGVFTGLT HIDAHFLSQT
     KQAGDNFPYL VAYQATVCAR AQAPPPSWDQ MWKCLIRLKP TLHGPTPLLY RLGA
//
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