ID A7XB60_9HEPC Unreviewed; 3010 AA. AC A7XB60; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 11-MAY-2016, entry version 70. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00058068}; OS Hepatitis C virus. OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Flaviviridae; Hepacivirus. OX NCBI_TaxID=11103 {ECO:0000313|EMBL:ABR27420.1}; RN [1] {ECO:0000313|EMBL:ABR27420.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4034 {ECO:0000313|EMBL:ABR27420.1}; RX PubMed=17522222; DOI=10.1128/JVI.00487-07; RG Virahep-C Study Group; RA Donlin M.J., Cannon N.A., Yao E., Li J., Wahed A., Taylor M.W., RA Belle S.H., Di Bisceglie A.M., Aurora R., Tavis J.E.; RT "Pretreatment sequence diversity differences in the full-length RT hepatitis C virus open reading frame correlate with early response to RT therapy."; RL J. Virol. 81:8211-8224(2007). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|SAAS:SAAS00291628}. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC {ECO:0000256|SAAS:SAAS00291428}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|SAAS:SAAS00510455}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|SAAS:SAAS00560857}. CC -!- SIMILARITY: Contains RdRp catalytic domain. CC {ECO:0000256|SAAS:SAAS00510369}. 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; EF407472; ABR27420.1; -; Genomic_RNA. DR ProteinModelPortal; A7XB60; -. DR euHCVdb; EF407472; -. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030529; C:intracellular 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:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0039520; P:induction by virus of host autophagy; 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 Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR002521; HCV_core_C. DR InterPro; IPR002522; HCV_core_N. DR InterPro; IPR002519; HCV_env. DR InterPro; IPR002531; HCV_NS1. DR InterPro; IPR002518; HCV_NS2. DR InterPro; IPR000745; HCV_NS4a. DR InterPro; IPR001490; HCV_NS4b. DR InterPro; IPR002868; HCV_NS5a. DR InterPro; IPR013193; HCV_NS5a_1B_dom. DR InterPro; IPR024350; HCV_NS5a_C. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR013192; NS5A_1a. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR004109; Peptidase_S29. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002166; RNA_pol_HCV. 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; 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; PF12941; HCV_NS5a_C; 1. DR Pfam; PF02907; Peptidase_S29; 1. DR Pfam; PF00998; RdRP_3; 1. DR ProDom; PD001388; HCV_env; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS51693; HCV_NS2_PRO; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. PE 4: Predicted; KW Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00445756}; KW ATP-binding {ECO:0000256|SAAS:SAAS00510945}; KW Capsid protein {ECO:0000256|SAAS:SAAS00445860}; KW Helicase {ECO:0000256|SAAS:SAAS00445774}; KW Host membrane {ECO:0000256|SAAS:SAAS00445977}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00445875}; KW Hydrolase {ECO:0000256|SAAS:SAAS00510997}; KW Membrane {ECO:0000256|SAAS:SAAS00445865, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00510884}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510590}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600}; KW Transferase {ECO:0000256|SAAS:SAAS00510371}; KW Transmembrane {ECO:0000256|SAAS:SAAS00445861, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00445939, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|SAAS:SAAS00445995}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS00511060}; KW Virion {ECO:0000256|SAAS:SAAS00445868}; KW Virus entry into host cell {ECO:0000256|SAAS:SAAS00445755}. FT TRANSMEM 718 740 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 752 778 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 784 803 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 815 836 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 873 901 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1660 1688 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1824 1844 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1851 1870 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1882 1902 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2990 3007 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 903 1026 Peptidase C18. {ECO:0000259|PROSITE: FT PS51693}. FT DOMAIN 1217 1369 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 1361 1538 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT DOMAIN 2633 2751 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50507}. SQ SEQUENCE 3010 AA; 326939 MW; 0572E0D6E7C7BDF1 CRC64; MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG RRQHIPKARR SEGRAWAQPG HPWPLYGNEG MGWAGWLLSP RGSRPSWGPN DPRRRSRNLG KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNIP GCSFSIFLLA LLSCLTTPAS AYEVRNVSGV YHVTNDCANT SIVYEVADMI MHTPGCVPCV RENNISRCWV ALTPTLAARN ASVPTTTIRR HVDLLVGTAA FCSAMYVGDL CGSVFLVSQL FTFSPRRHET VQDCNCSIYP GHLSGHRMAW DMMMNWSPTT ALVVSQLLRI PQAIVDMVAG AHWGVLAGLA YYSMAGNWAK VLIVMLLFAG VDGETRVSGG VLAHTTQRFT SIFTSGPSQK IQLINTNGSW HINRTALNCN DSLQTGFLAA LFYVNRFNAS GCPERLAHCR SIDKFVQGWG PITYARARDP DQRPYCWHYA PQPCGIVPAS QVCGPVYCFT PSPVVVGTTD RFGVPTYTWG ENETDVLLLN NTRPPQGNWF GCTWMNSTGF TKTCGGPPCN IGGVGNDTLT CPTDCFRKHP EATYTKCGSG PWLTPRCIVD YPYRLWHYPC TVNFTIFKIR MYVGGVEHRL NAACNWTRGE RCDLEDRDRS ELSPLLLSTT EWQILPCSFT TLPALSTGLI HLHRNIVDVQ YLYGIGSAVV SFAIKWEYVL LLFLLLADAR ICACLWMMLL IAQAEAALEN LVVLNAASVA GAHGILSFLV FFCAAWYIKG RLVPGAAYAL YGVWPLLLLL LALPPRAYAM DREMAASCGG AVFVGLVLLT LSPHYKALLA RFIWWLQYLL TRAEALLQVW IPPLNVRGGR DAIILLTCVI HPELIFTITK ILLAILGPLM VLQAGITKVP YFVRAHGLIR ACMLVRKVAG GHYVQMAFMK LAALTGTYVY NHLTPLQDWA HAGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIISGL PVSARRGREI LLGPADSLEG QGWRLLAPIT AYAQQTRGLL GCIITSLTGR DKNQVEGEVQ VVSTATQSFL ASCINGVCWT VFHGAGSKTL AGPKGPIAQM YTNVDQDLVG WQAPPGARSL TPCTCGSSDL YLVTRHADVI PVRRRGDGRG SLLSPRPVSY LKGSSGGPLL CPSGHAVGIF RAAVCTRGVA KAVDFIPVES METTMRSPVF TDNSSPPAVP QTFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA TLGFGAYMSK AHGVDPNIRT GVRTITTGAP ITYSTYGKFL ADGGCSGGAY DIIICDECHS TDSTTILGIG TVLDQAETAG ARLVVLATAT PPGSVTVPHS NIEEVALSNT GEIPFYGKAI PIETIKGGRH LIFCHSKKKC DELAAKLSGL GLNAVAYYRG LDVSVIPTSG DVVVVATDAL MTGFTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRAGIYR FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV CQDHLEFWES VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP PPSWDQMWKC LVRLKPTLHG PTPLLYRLGA VQNEIVLTHP ITKYIMACMS ADLEVVTSTW VLVGGVLAAL AAYCLTTGCV VIVGRIILSG RPAVIPDREV LYREFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT KQAEAAAPVV ESKWQALETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP LTTQTTLLLN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD VLAGYGAGVA GALVAFKIMS GEVPSTEDLV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA AARVTQILSS LTITQLLKRL HQWINEDCST PCSGSWLRDV WDWICTVLTD FRTWLQSKLL PQLPGIPFFS CQRGYKGVWR GDGIMQTTCP CGAQITGHVK NGSMRIVGPK TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGDFH YVTGMTTDNV KCPCQVPAPE FFTEVDGVRL HRYAPACKPL LRDEVVFQVG LNQYLVGSQL PCEPEPDVAV LTSMLTDPSH ITAETAKRRL ARGSPPSLAS SSASQLSAPS LKATCTTRHD SPDADLIEAN LLWRQEMGGN ITRVESENKV VILDSFEPLR AEEDEREVSV PAEILRKSRK FPRAMPIWAR PDYNPPLLES WKDPDYVPPV VHGCPLPPAK APPIPPPRRK RTVVLTESTV SSALAELAAK TFGSSESSAA DSGTATAPPD QSSGDGDAGS DVESYSSMPP LEGEPGDPDL SDGSWSTVSE EAGEDVVCCS MSYTWTGALI TPCAAEESKL PINALSNSLL RHHNMVYATT SRSASQRQKK VTFDRLQVLD DHYRDVLKEM KVKASTVKAK LLSVEEACKL TPPHSARSKF GYGAKDVRNL SSKAINHIRS VWKDLLEDTE TPIDTTIMAK NEVFCVQPEK GGRKPARLIV YPDLGVRVCE KMALYDVVST LPQAVMGSSY GFQYSPGQRV EFLVNAWKSK KCPMGFAYDT RCFDSTVTES DIRVEESIYQ CCDLAPEARQ AIKSLTERLY IGGPLTNSKG QNCGYRRCRA SGVLTTSCGN TLTCYLKASA ACRAAKLQDC TMLVNGDDLV VICESAGTQE DAASLRVFTE AMTRYSAPPG DPPQPEYDLE LITSCSSNVS VAHDASGKRV YYLTRDPTTP LARAAWETAR HTPVNSWLGN IIMYAPTLWA RMILMTHFFS ILLAQEQLEK ALDCQIYGAC YSIEPLDLPQ IIERLHGLSA FSLHSYSPGE INRVASCLRK LGVPPLRVWR HRARSVRARL LSQGGRAATC GKYLFNWAVK TKLKLTPIPA ASQLDLSGWF VAGYSGGDIY HSLSRARPRW FMLCLLLLSV GVGIYLLPNR //