ID D6QM25_9HEPC Unreviewed; 1651 AA. AC D6QM25; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 16-JAN-2019, entry version 54. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684}; DE Flags: Fragment; OS Hepacivirus C. OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Flaviviridae; Hepacivirus. OX NCBI_TaxID=11103 {ECO:0000313|EMBL:ADG34859.1}; RN [1] {ECO:0000313|EMBL:ADG34859.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=30vSDc21_y00 {ECO:0000313|EMBL:ADG34859.1}; RX PubMed=20200239; DOI=10.1128/JVI.02265-09; RA Liu L., Fisher B.E., Dowd K.A., Astemborski J., Cox A.L., Ray S.C.; RT "Acceleration of hepatitis C virus envelope evolution in humans is RT consistent with progressive humoral immune selection during the RT transition from acute to chronic infection."; RL J. Virol. 84:5067-5077(2010). 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, CC ChEBI:CHEBI:83400; EC=2.7.7.48; CC Evidence={ECO:0000256|SAAS:SAAS01122277}; CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|SAAS:SAAS00560857}. 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; HM000525; ADG34859.1; -; Genomic_RNA. DR euHCVdb; HM000525; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019028; C:viral capsid; IEA:InterPro. DR GO; GO:0019031; C:viral envelope; IEA:InterPro. 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:UniProtKB-UniRule. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro. DR CDD; cd00079; HELICc; 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; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR004109; Peptidase_S29_NS3. 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 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; PS51822; HV_PV_NS3_PRO; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00445701}; KW Helicase {ECO:0000256|SAAS:SAAS00058020}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01030, KW ECO:0000256|SAAS:SAAS00057591}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00445889}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00445834}; KW Protease {ECO:0000256|PROSITE-ProRule:PRU01030}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00057670}; KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU01030}; KW Transferase {ECO:0000256|SAAS:SAAS00057618}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS00057947}; KW Virion {ECO:0000256|SAAS:SAAS00445868}. FT TRANSMEM 351 378 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 718 741 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 753 778 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 785 802 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 814 835 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 891 913 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 903 1026 Peptidase C18. {ECO:0000259|PROSITE: FT PS51693}. FT DOMAIN 1027 1208 Peptidase S29. {ECO:0000259|PROSITE: FT PS51822}. 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 ACT_SITE 952 952 For protease NS2-3 activity; shared with FT dimeric partner. {ECO:0000256|PROSITE- FT ProRule:PRU01030}. FT ACT_SITE 972 972 For protease NS2-3 activity; shared with FT dimeric partner. {ECO:0000256|PROSITE- FT ProRule:PRU01030}. FT ACT_SITE 993 993 For protease NS2-3 activity; shared with FT dimeric partner. {ECO:0000256|PROSITE- FT ProRule:PRU01030}. FT SITE 1026 1027 Cleavage; by protease NS2-3. FT {ECO:0000256|PROSITE-ProRule:PRU01030}. FT NON_TER 1651 1651 {ECO:0000313|EMBL:ADG34859.1}. SQ SEQUENCE 1651 AA; 179408 MW; 19F51152A33164DD CRC64; MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG RRQPIPKARR PEGRSWAQPG YPWPLYGNEG CGWAGWLLSP RGSRPSWGPT DPRRRSRNLG KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA LLSCLTVPAS AYQVRNSTGL YHVTNDCPNS SIVYEAADAI LHTPGCVPCV REGNASRCWV AVTPTVATRD GKLPTTQLRR HIDLLVGSAT LCSALYVGDL CGSVFLVGQL FTFSPRRHWT TQGCNCSIYP GHITGHRMAW DMMMNWSPTA ALVVAQLLRI PQAILDMIAG AHWGVLAGMA YFSMVGNWAK VLVVLLLFAG VDAETHVSGG TAARTTARLT NLFSPGAMQN IQLVNTNGSW HINRTALNCN DSLNTGWVAG LFYRYKFNSS GCPERLASCR RLTDFAQGWG PIRYANGSGP DQRPYCWHYP PKPCGFVPAK SVCGPVYCFT PSPVVVGTTD KSGAPTYSWG ENDTDVFVLN NTRPPLGNWF GCTWMNSTGF TKVCGAPPCA IGGVGNNTLL CPTDCFRKHP EATYSRCGSG PWITPRCLVD YPYRLWHYPC TINYTIFKVR MYVGGVEHRL DAACNWTRGE RCDLEDRDRS ELSPLLLSTT QWQVLPCSFT TLPALSTGLI HLHQNIVDVQ YLYGVGSSIA SWAIKWEYVV LLFLLLADAR VCSCLWMMLL ISQAEAALEN LVILNAASLA GTHGLASFLV FFCFAWYLKG RWVPGAVYAL YGMWPLLLLS LALPQRAYAL DTEVAASCGG VVLVGLMALT LSPYYKRYIR WCMWWLQYFL TRAEAQLHIW VPPLNVRGGR DAVILLMCVA HPTLVFDITK LLLAVFGPLW ILQASLLRVP YFVRVQGLLR VCALARKLAG GHYVQMAIIK LGALTGTYVY NHLTPLRNWA HNSLQDLAVA VEPVIFSPME TKLITWGADT AACGDIINGL PVSARRGREI LLGPADGMVS KGWRLLAPIT AYAQQTRGLL GCIITSLTGR DKNQVEGEVQ IVSTAAQTFL ATCINGACWT VYHGAGTRTI ASPKGPVIQM YTNVDKDLVG WPAPQGSRSL TPCTCGSSDL YLVTRHADVI PVRRRGDSRG SLLSPRPISY LKGSSGGPLL CPAGHAVGIF RAAVCTRGVA KAVDFIPVEN LETTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA TLGFGAYMSK AHGIDPNIRT GVRTITTGSS ITYSTYGKFL ADGGCSGGAY DIIICDECHS VDATSILGIG TVLDQAETAG ARLVVLATAT PPGSVTVPHP NIEEVALSTT GEIPFYGKAI PLEVIKGGRH LIFCHSKRKC DELASKLVAL GVNAVAYYRG IDVSVIPTSG DVVVVATDAL MTGFTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTLPQD AVSRTQRRGR TGRGKPGIYR FVAPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETTVRLR AYMNTPGLPV CQDHLEFWEG VFTGLTHIDA HFLSQTKQSG ENFPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLQG PTPLLYRLGA VQNEVILTHP ITKYIMTCMS A //