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Database: UniProt
Entry: J7JFN6_9HEPC
LinkDB: J7JFN6_9HEPC
Original site: J7JFN6_9HEPC 
ID   J7JFN6_9HEPC            Unreviewed;       867 AA.
AC   J7JFN6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
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:AFQ55074.1};
RN   [1] {ECO:0000313|EMBL:AFQ55074.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=10025.08 {ECO:0000313|EMBL:AFQ55074.1};
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: 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; JQ804347; AFQ55074.1; -; 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: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: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   Gene3D; 2.40.10.120; -; 1.
DR   Gene3D; 6.10.250.1610; -; 1.
DR   Gene3D; 6.10.250.1750; -; 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; 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; 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   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 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, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
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};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
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        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          123..250
FT                   /note="Peptidase C18"
FT                   /evidence="ECO:0000259|PROSITE:PS51693"
FT   DOMAIN          251..432
FT                   /note="Peptidase S29"
FT                   /evidence="ECO:0000259|PROSITE:PS51822"
FT   DOMAIN          441..593
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          585..762
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFQ55074.1"
FT   NON_TER         867
FT                   /evidence="ECO:0000313|EMBL:AFQ55074.1"
SQ   SEQUENCE   867 AA;  93424 MW;  90A9877D8EC25596 CRC64;
     YLKGRWVPGA AYALYGMWPL LLLLLALPQR AYALDTEVAA SCGGVVIVGL MVLTLSPHYK
     RYISWCLWWL QYFLTRVEAQ LHVWVPPLNV RGGRDAVILL MCVIHPALVF DITKLLLAVF
     GPLWILQTSL LKVPYFVRVQ GLLRLCALAR KMAGGHYVQM AIIKVGALTG TYIYNHLTPL
     RDWAHNSLRD LAVAVEPVVF SQMETKLITW GADTAACGDI INGLPVSARR GREILLGPAD
     GAVSKGWRLL APITAYAQQT RGLLGCIITS LTGRDKNQVE GEVQIVSTAA QTFLATCING
     VCWTVYHGAG TRTIASPKGP VIQMYTNVDQ DLVGWPAPYG ARSLTPCTCG SSDLYLVTRH
     ADVIPVRRRG DSRGSLLSPR PISYLKGSSG GPLLCPAGHA VGIFRAAVCT RGVAKAVDFI
     PVESLETTMR SPVFTDNSSP PAVPQSFQVA HLHAPTGSGK STKVPAAYAA QGYKVLVLNP
     SVAATLGFGA YMSKAHGIDP NIRTGVRTIT TGSPITYSTY GKFLADGGCS GGAYDIIICD
     ECHSTDATSI LGIGTVLDQA ETAGARLVVL ATATPPGSVT VPHSNIEEVA LSTTGEIPFY
     GKAIPLEAIK GGRHLIFCHS RKKCDELAAR LVALGINAVA YYRGLDVSVI PTSGDVVVVA
     TDALMTGFSG DFDSVIDCNT CVTQTVDFSL DPTFTIETTT LPQDAVSRTQ RRGRTGRGKP
     GIYRFVAPGE RPSGMFDSSV LCECYDAGCA WYELTPAETT VRLRAYMNTP GLPVCQDHLE
     FWEGVFTGLT HIDAHFLSQT KQSGENFPYL VAYQATVCAR AQAPPPSWDQ MWKCLIRLKP
     TLHGPTPLLY RLGAVQNEIT LTHPITK
//
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