ID D6QM25_9HEPC Unreviewed; 1651 AA. AC D6QM25; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 12-AUG-2020, entry version 60. DE RecName: Full=Capsid protein C {ECO:0000256|ARBA:ARBA00014462}; DE EC=3.6.1.15 {ECO:0000256|ARBA:ARBA00012445}; DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552}; DE AltName: Full=Core protein p19 {ECO:0000256|ARBA:ARBA00017544}; DE AltName: Full=Core protein p21 {ECO:0000256|ARBA:ARBA00017537}; DE AltName: Full=Envelope glycoprotein E1 {ECO:0000256|ARBA:ARBA00021997}; DE AltName: Full=Envelope glycoprotein E2 {ECO:0000256|ARBA:ARBA00021988}; DE AltName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; DE AltName: Full=Gp32 {ECO:0000256|ARBA:ARBA00020582, ECO:0000256|ARBA:ARBA00022393}; DE AltName: Full=NS1 {ECO:0000256|ARBA:ARBA00014816}; DE AltName: Full=Serine protease NS3 {ECO:0000256|ARBA:ARBA00016200}; DE AltName: Full=gp35 {ECO:0000256|ARBA:ARBA00020579}; DE AltName: Full=gp68 {ECO:0000256|ARBA:ARBA00020638}; DE AltName: Full=gp70 {ECO:0000256|ARBA:ARBA00020520}; DE AltName: Full=p21 {ECO:0000256|ARBA:ARBA00016716}; DE Flags: Fragment; OS Hepacivirus C. OC Viruses; Riboviria; 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 transition RT from acute to chronic infection."; RL J. Virol. 84:5067-5077(2010). 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:ARBA00004389}; Single-pass CC membrane protein {ECO:0000256|ARBA:ARBA00004389}. Endoplasmic reticulum CC membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane CC 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:ARBA00004517}; Single-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004517}. 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 mitochondrion membrane CC {ECO:0000256|ARBA:ARBA00004458}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004458}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. Lipid droplet CC {ECO:0000256|ARBA:ARBA00004502}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Membrane CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004167}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. Mitochondrion membrane CC {ECO:0000256|ARBA:ARBA00004583}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004583}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. Secreted CC {ECO:0000256|ARBA:ARBA00004613}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004563}. CC -!- SIMILARITY: Belongs to the hepacivirus polyprotein family. CC {ECO:0000256|ARBA:ARBA00008286}. 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:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. 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 Gene3D; 1.20.1280.150; -; 1. DR Gene3D; 2.30.30.710; -; 1. DR Gene3D; 2.40.10.10; -; 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; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. 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 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 3: Inferred from homology; 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 Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|ARBA:ARBA00022570}; 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 Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; 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 nucleus {ECO:0000256|ARBA:ARBA00022562}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01030}; KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023258}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protease {ECO:0000256|PROSITE-ProRule:PRU01030}; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU01030}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}; 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 Virion {ECO:0000256|ARBA:ARBA00022844}; KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}. FT TRANSMEM 351..378 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 814..835 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 891..913 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 REGION 1..77 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 47..69 FT /note="Polyampholyte" 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" FT NON_TER 1651 FT /evidence="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 //