ID Q9DTF0_9HEPC Unreviewed; 3010 AA. AC Q9DTF0; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 17-JUN-2020, entry version 140. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS01197934}; OS Hepacivirus C. OC Viruses; Riboviria; Flaviviridae; Hepacivirus. OX NCBI_TaxID=11103 {ECO:0000313|EMBL:BAB18800.1, ECO:0000313|Proteomes:UP000117176}; RN [1] {ECO:0000313|EMBL:BAB18800.1, ECO:0000313|Proteomes:UP000117176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HCVT050 {ECO:0000313|EMBL:BAB18800.1}; RX PubMed=11348851; DOI=10.1016/S1386-6346(00)00141-8; RA Takahashi K., Iwata K., Matsumoto M., Matsumoto H., Nakao K., Hatahara T., RA Ohta Y., Kanai K., Maruo H., Baba K., Hijikata M., Mishiro S.; RT "Hepatitis C virus (HCV) genotype 1b sequences from fifteen patients with RT hepatocellular carcinoma: the 'progression score' revisited."; RL Hepatol. Res. 20:161-171(2001). 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|SAAS:SAAS01122357}; 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|SAAS:SAAS01122355}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; CC EC=2.7.7.48; Evidence={ECO:0000256|SAAS:SAAS01198479}; CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|SAAS:SAAS01046204}. 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; AB049087; BAB18800.1; -; Genomic_RNA. DR PIR; A61196; A61196. DR PIR; PQ0246; PQ0246. DR PIR; PQ0251; PQ0251. DR PIR; PQ0252; PQ0252. DR PIR; PQ0254; PQ0254. DR PIR; PS0329; PS0329. DR euHCVdb; AB049087; -. DR Proteomes; UP000117176; Genome. 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:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:InterPro. 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:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0003968; F:RNA-directed 5'-3' 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:0039503; P:suppression by virus of host innate immune response; 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; 1.20.1280.150; -; 1. DR Gene3D; 2.20.25.210; -; 1. DR Gene3D; 2.20.25.220; -; 1. DR Gene3D; 2.30.30.710; -; 1. DR Gene3D; 3.30.70.270; -; 1. 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; IPR042205; HCV_NS2_C. DR InterPro; IPR042209; HCV_NS2_N. DR InterPro; IPR000745; HCV_NS4a. DR InterPro; IPR001490; HCV_NS4b. DR InterPro; IPR002868; HCV_NS5a. DR InterPro; IPR013193; HCV_NS5a_1B_dom. DR InterPro; IPR038568; HCV_NS5A_1B_sf. DR InterPro; IPR024350; HCV_NS5a_C. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR013192; NS5A_1a. DR InterPro; IPR038170; NS5A_1a_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR004109; Peptidase_S29_NS3. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. 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 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; 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|SAAS:SAAS00291633}; KW ATP-binding {ECO:0000256|SAAS:SAAS01198603}; KW Capsid protein {ECO:0000256|SAAS:SAAS01197962}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Helicase {ECO:0000256|SAAS:SAAS01209034}; KW Host membrane {ECO:0000256|SAAS:SAAS00291629}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00291630}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01030, KW ECO:0000256|SAAS:SAAS01198589}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|SAAS:SAAS00910833}; KW Membrane {ECO:0000256|SAAS:SAAS00291489, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS01198580}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01198562}; KW Protease {ECO:0000256|PROSITE-ProRule:PRU01030}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS01198530}; KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU01030}; KW Transferase {ECO:0000256|SAAS:SAAS01198537}; KW Transmembrane {ECO:0000256|SAAS:SAAS00291514, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00291474, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|SAAS:SAAS00291492}; KW Viral immunoevasion {ECO:0000256|SAAS:SAAS00910833}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS01198628}; KW Virion {ECO:0000256|SAAS:SAAS01197947}; KW Virus entry into host cell {ECO:0000256|SAAS:SAAS00291600}. FT TRANSMEM 264..287 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 368..388 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 718..741 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 753..778 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 785..802 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 891..913 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1660..1688 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1825..1845 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1851..1870 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1882..1902 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2990..3007 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 903..1026 FT /note="Peptidase C18" FT /evidence="ECO:0000259|PROSITE:PS51693" FT DOMAIN 1027..1208 FT /note="Peptidase S29" FT /evidence="ECO:0000259|PROSITE:PS51822" FT DOMAIN 1217..1369 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1361..1538 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2633..2751 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1..76 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2351..2407 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 2487..2507 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 47..68 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2351..2385 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 952 FT /note="For protease NS2-3 activity; shared with dimeric FT partner" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01030" FT ACT_SITE 972 FT /note="For protease NS2-3 activity; shared with dimeric FT partner" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01030" FT ACT_SITE 993 FT /note="For protease NS2-3 activity; shared with dimeric FT partner" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01030" FT SITE 1026..1027 FT /note="Cleavage; by protease NS2-3" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01030" SQ SEQUENCE 3010 AA; 327156 MW; 7A9C7B1273266FF3 CRC64; MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG RRQPIPKARQ PEGRAWAQPG YPWPLYGNEG LGWAGWLLSP RGSRPSWGPT DPRRRSRNLG KVIDTLTCGF ADLMGYIPLV GGPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA LLSCLTIPAS AYEVRNVSGV YHVTNDCSNS SIVYEAADMI MHTPGCVPCV RENDCSRCWV ALTPTLAARN SSIPTTTIRR HVDLLVGAAA FCSAMYVGDL CGSIFLVSQL FTFSPRRYWT VQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQSVVDMVAG AHWGVLAGLA YYSMVGNWAK VLIVMLLFAG VDGVTHMTGG QVSHNTRSFM SLFTCGPSQK IQLINTNGSW HINRTALNCN DSLQTGFLAA LFYAHNLNSS GCPERMASCR SIDKFAQGWG PITHVVPDTW DQRPYCWHYA PKPCGIVPAS QVCGPVYCFT PSPVVVGTTD RFGVPTYTWG ENETDVLFLN NTRPPQGNWF GCTWMNSTGF TKTCGGPPCN IGGVGNNTLI CPTDCFRKHP EATYTKCGSG PWLTPRCMVD YPYRLWHYPC TVNFTIFKVR MYVGGVEHRL NAACNWTRGE RCDLEDRDRS ELSPLLLSTT EWQVLPCSFT PLPALSTGLI HLHQNIVDVQ YLYGIGSAVV SVVIKWEYVL LLFLLLADAR VCSCLWMMLL IAQAEAALEN LVVLNAASVA GAHGTLSFLV FFCAAWYIKG KLVPGAAYAL YGVWPLLLLL LALPHRAYAM DPEMAASCGG AVFVGLALLT LSPHYKAFLA RLIWWLQYFI TRAEAHLQVW IPPLNVRGGR DAIILLACAV HPELIFDITK ILLAILGPLM VLQAGLTRVP YFVRAQGLIR VCMLVRKVAG GHYFQMALMK LAALTGTYVY DHLTPLRDWA HVGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIISGL PVSARRGREI LLGPADSFRE QGWRLLAPIT AYSQQTRGLL GCIITSLTGR DKNQVEGEVQ VVSTATQSFL ATCVNGVCWT VYHGAGSKTL AGPKGPITQM YTNVDQDLVG WQAPPGARSL TPCTCGSSDL YLVTRHADVI PVRRRGDSRG SLLSPRPVSY LKGSSGGPLL CPSGHAVGIF RAAVCTRGVA KAVDFIPVES METTMRSPVF TDNSSPPAVP QTFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA TLSFGAYMSK AHGVDPNIRT GVRTITTGAP ITYSTYGKFL ADGGCSGGAY DIIICDECHS TDSTSILGIG TVLDQAETAG ARLVLLATAT PPGSVTVPHP NIEEVALSNT GEIPFYGKAI PIETIKGGRH LIFCHSKKKC DELAAKLSAL GVNAVAYYRG LDVSVIPTSG NVVVVATDAL MTGYTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRAGIYR FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV CQDHLEFWES VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG PTPLLYRLGA VQNEVTLTHP ITKFIMACMS ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV VIVGRIILSG KPAVIPDREV LYREFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT KQAEAAAPVV ESKWRALETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP LTTQHTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD ILAGYGAGVA GALVAFKVMS GEMPSAEDMV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA AARVTQILSS LTITQLLKRL HQWINEDCST PCSGSWLRDV WDWICTVLTD FKTWLQSKLL PRLPGVPFFS CQRGYKGVWL GDGVMQTTCP CGAQISGHVK NGSMKIVGPK TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGEFH YVTGMTTDNV KCPCQVPSPE FFTEVDGVRL HRYAPACKPL LRDEVTFQVG LNQYPVGSQL PCEPEPDVAV LTSMLTDPSH ITAETARRRL ARGSPPSLAS SSASQLSAPS LKATCTTCHD SPDADLIEAN LLWRQEMGGN ITRVESENKV VILDSFDPLR AEEDEREVSV AAEILRKTRK FPPAIPIWAR PDYNPPLLES WKDPDYVPPV VHGCPLPPTK APPIPPPRRK RTVILTESTV SSALAELATK TFGSSGSSAV DSGTATAPPD QPSDDGDTGS DVGSYSSMPP LEGEPGDPDL SDGSWSTVSE EAGEDVVCCS MSYTWTGALI TPCGAEETKL PINALSNSLL RHHNMVYATT SRSASQRQRK VTFDRLQVLD DHYRDVLKEM KAKASTVKAK LLSVEEACKL TPPHSARSKF GYGAKDVRNL SSKAVNHIRS VWKDLLEDTE TPINTTIMAK SEVFCVQPEK GGRKPARLIV FPDLGVRVCE KMALYDVVST LPQAVMGSSY GFQYSPGQRV EFLVNAWKSK KSPMGFAYDT RCFDSTVTES DIRVEESIYQ CCDLAPEARQ VIRSLTERLY IGGPLTNSKG QNCGYRRCRA SGVLTTSCGN TLTCYLKASA ACRAAKLQDC TMLVCGDDLV VICESAGTQE DAANLRVFTE AMTRYSAPPG DPPRPEYDLE LITSCSSNVS VAHDAAGKRV YYLTRDPITP LARAAWETAR HTPVNSWLGN IIMYAPTLWA RMILMTHFFS ILLAQEQLEK ALDCQIYGAV YSIEPLDLPQ IIQRLHGLSA FSLHSYSPGE INRVASCLRK LGVPPLRVWR HRARSVRAKL LSQGGRAATC GKYLFNWAVR TKLKLTPIPA ASQLDLSGWF VAGYSGGDIY HSLSRARPRW FMWCLLLLSV GVGIYLLPNR //