ID G3FEY0_9FLAV Unreviewed; 3432 AA. AC G3FEY0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-MAY-2012, entry version 7. DE SubName: Full=Polyprotein; OS Japanese encephalitis virus. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae; OC Flavivirus; Japanese encephalitis virus group. OX NCBI_TaxID=11072; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZMT; RX PubMed=21697481; DOI=10.1128/JVI.00825-11; RA Pan X.L., Liu H., Wang H.Y., Fu S.H., Liu H.Z., Zhang H.L., Li M.H., RA Gao X.Y., Wang J.L., Sun X.H., Lu X.J., Zhai Y.G., Meng W.S., He Y., RA Wang H.Q., Han N., Wei B., Wu Y.G., Feng Y., Yang D.J., Wang L.H., RA Tang Q., Xia G., Kurane I., Rayner S., Liang G.D.; RT "Emergence of genotype I of Japanese encephalitis virus as the RT dominant genotype in Asia."; RL J. Virol. 85:9847-9853(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZMT; RA Liang G., Fu S., Zhang H.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Envelope protein E binding to host cell surface receptor CC is followed by virus internalization through clathrin-mediated CC endocytosis. Envelope protein E is subsequently involved in CC membrane fusion between virion and host late endosomes. CC Synthesized as an homodimer with prM which acts as a chaperone for CC envelope protein E. After cleavage of prM, envelope protein E CC dissociate from small envelope protein M and homodimerizes (By CC similarity). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane; Multi- CC pass membrane protein. Host endoplasmic reticulum membrane; Multi- CC pass membrane protein (By similarity). CC -!- SIMILARITY: Contains 1 RdRp catalytic domain. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. 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; JF706283; AEO86792.1; -; Genomic_RNA. DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to 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:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. 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:0070008; F:serine-type exopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0032774; P:RNA biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0019079; P:viral genome replication; IEA:InterPro. DR Gene3D; G3DSA:3.30.67.10; Flav_glyE_cen_2; 1. DR Gene3D; G3DSA:2.60.98.10; Flav_glyE_dim; 3. DR Gene3D; G3DSA:2.60.40.350; Flv_glyE_Ig-like; 1. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR000069; Env_glycoprot_M_flavivir. DR InterPro; IPR001122; Flavi_capsidC. DR InterPro; IPR001157; Flavi_NS1. DR InterPro; IPR000752; Flavi_NS2A. DR InterPro; IPR000487; Flavi_NS2B. DR InterPro; IPR000404; Flavi_NS4A. DR InterPro; IPR001528; Flavi_NS4B. DR InterPro; IPR002535; Flavi_propep. DR InterPro; IPR000336; Flv_glyE_Ig-like. DR InterPro; IPR014412; Gen_Poly_FLV. DR InterPro; IPR011998; GlycoprotE/E1_cen/dimer. DR InterPro; IPR013756; GlyE_cen_dom_subdom2. DR InterPro; IPR013754; GlyE_dim. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR009003; Pept_cys/ser_Trypsin-like. DR InterPro; IPR001850; Peptidase_S7. DR InterPro; IPR000208; RNA-dir_pol_flavivirus. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002877; rRNA_MeTrfase_RrmJ/FtsJ. DR Pfam; PF01003; Flavi_capsid; 1. DR Pfam; PF07652; Flavi_DEAD; 1. DR Pfam; PF02832; Flavi_glycop_C; 1. DR Pfam; PF00869; Flavi_glycoprot; 1. DR Pfam; PF01004; Flavi_M; 1. DR Pfam; PF00948; Flavi_NS1; 1. DR Pfam; PF01005; Flavi_NS2A; 1. DR Pfam; PF01002; Flavi_NS2B; 1. DR Pfam; PF01350; Flavi_NS4A; 1. DR Pfam; PF01349; Flavi_NS4B; 1. DR Pfam; PF00972; Flavi_NS5; 1. DR Pfam; PF01570; Flavi_propep; 1. DR Pfam; PF01728; FtsJ; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00949; Peptidase_S7; 1. DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF56983; Flavi_glycoprotE; 1. DR SUPFAM; SSF81296; Ig_E-set; 1. DR SUPFAM; SSF50494; Pept_Ser_Cys; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. PE 3: Inferred from homology; KW ATP-binding; Capsid protein; KW Clathrin-mediated endocytosis of virus by host; Disulfide bond; KW Fusion of virus membrane with host endosomal membrane; KW Fusion of virus membrane with host membrane; Helicase; KW Host endoplasmic reticulum; Host membrane; Host-virus interaction; KW Hydrolase; Initiation of viral infection; Membrane; KW Nucleotide-binding; Nucleotidyltransferase; Protease; RNA replication; KW RNA-directed RNA polymerase; Serine protease; Transferase; KW Transmembrane; Transmembrane helix; Viral attachment to host cell; KW Viral envelope protein; Viral penetration into host cytoplasm; Virion; KW Virus endocytosis by host. SQ SEQUENCE 3432 AA; 380151 MW; 6F537678D97E402F CRC64; MTKKPGGPGK NRAINMLKRG LPRVFPLVGV KRVVMSLLDG RGPVRFVLAL ITFFKFTALA PTKTLLGRWK AVEKSVAMKH LTSFKRELGT LIDAVNKRGR KQNKRGGNEG SIMWLASLAV VIACAGAMKL SNFQGKLLMT INNTDIADVI VIPTSKGENR CWVRAIDVGY MCEDTITYEC PKLTMGNDPE DVDCWCDNQE VYVQYGRCTR TRHSKRSRRS VSVQIHGESS LVNKKEAWLD STKATRYLMK TENWIIRNPG YAFLAAVLGW MLGSNNGQRV VFTILLLLVA PAYSFNCLGM GNRDFIEGAS GATWVDLVLE GDSCLTIMAN DKPTLDVRMI NIEASQLAEV RSYCYHASVT DISTVARCPT TGEAHNKKRA DSSYVCKQGF TDRGWGNGCG LFGKGSIDTC AKFSCTSKAI GRTIQPENIK YEVGIFVHGT TTSENHGNYS AQVGASQAAK FTVTPNAPSI TLKLGDYGEV TLDCEPRSGL NTEAFYVMTV GSKSFLVHRE WFHDLALPWT SPSSTAWRNR ELLMEFEEAH ATKQSVVALG SQEGGLHQAL AGAIVVEYSS SVKLTSGHLK CRLKMDKLAL KGTTYGMCTE KFSFAKNPAD TGHGTVVIEL SYSGSDGPCK IPIVSVASLN DMTPVGRLVT VNPFVATSSA NSKVLVEMEP PFGDSYIVVG RGDKQINHHW HKAGSTLGKA FSTTLKGAQR LAALGDTAWD FGSIGGVFNS IGKAVHQVFG GAFRTLFGGM SWITQGLMGA LLLWMGVNAR DRSIALAFLA TGGVLVFLAT NVHADTGCAI DITRKEMRCG SGIFVHNDVE AWVDRYKYLP ETPRSLAKIV HKAHKEGVCG VRSVTRLEHQ MWEAVRDELN VLLKENAVDL SVVVNKPVGR YRSAPKRLSM TQEKFEMGWK AWGKSILFAP ELANSTFVVD GPETKECPDE HRAWNSMQIE DFGFGITSTR VWLKIREEST DECDGAIIGT AVKGHVAVHS DLSYWIESRY NDTWKLERAV FGEVKSCTWP ETHTLWGDGV EESELIIPHT IAGPKSKHNR REGYKTQNQG PWDENGIVLD FDYCPGTKVT ITEDCGKRGP SVRTTTDSGK LITDWCCRSC SLPPLRFRTE NGCWYGMEIR PVRHDETTLV RSQVDAFNGE MVDPFQLGLL VMFLATQEVL RKRWTARLTI PAVLGALLVL MLGGITYTDL ARYVVLVAAA FAEANSGGDV LHLALIAVFK IQPAFLVMNM LSTRWTNQEN VVLVLGAAFF QLASVDLQIG VHGILNAAAI AWMIVRAITF PTTSSVTMPV LALLTPGMRA LYLDTYRIIL LVIGICSLLQ ERKKTMAKKK GAVLLGLALT STGWFSPTTI AAGLMVCNPN KKRGWPATEF LSAVGLMFAI VGGLAELDIE SMSIPFMLAG LMAVSYVVSG KATDMWLERA ADISWEMDAA ITGSSRRLDV KLDDDGDFHL IDDPGVPWKV WVLRMSCIGL AALTPWAIVP AAFGYWLTLK TTKRGGVFWD TPSPKPCSKG DTTTGVYRIM ARGILGTYQA GVGVMYENVF HTLWHTTRGA AIMSGEGKLT PYWGSVKEDR IAYGGPWRFD RKWNGTDDVQ VIVVEPGKAA VNIQTKPGVF RTPFGEVGAV SLDYPRGTSG SPILDSNGDI IGLYGNGVEL GDGSYVSAIV QGDRQEEPVP EAYTPNMLRK RQMTVLDLHP GSGKTRKILP QIIKDAIQQR LRTAVLAPTR VVAAEMAEAL RGLPVRYQTS AVQREHQGNE IVDVMCHATL THRLMSPNRV PNYNLFVMDE AHFTDPASIA ARGYIATKVE LGEAAAIFMT ATPPGTTDPF PDSNAPIHDL QDEIPDRAWS SGYEWITEYA GKTVWFVASV KMGNEIAMCL QRAGKKVIQL NRKSYDTEYP KCKNGDWDFV ITTDISEMGA NFGASRVIDC RKSVKPTILE EGEGRVILGN PSPITSASAA QRRGRVGRNP NQVGDEYHYG GATSEDDSNL AHWTEAKIML DNIHMPNGLV AQLYGPEREK AFTMDGEYRL RGEEKKNFLE LLRTADLPVW LAYKVASNGI QYTDRKWCFD GPRTNAILED NTEVEIVTRM GERKILKPRW LDARVYADHQ ALKWFKDFAA GKRSAVSFIE VLGRMPEHFM GKTREALDTM YLVATAEKGG KAHRMALEEL PDALETITLI VAITVMTGGF FLLMMQRKGI GKMGLGALVL TLATFFLWAA EVPGTKIAGT LLIALLLMVV LIPEPEKQRS QTDNQLAVFL ICVLTVVGVV AANEYGMLEK TKADLKSMFG GKTQASGLTG LPSMALDLRP ATAWALYGGS TVVLTPLLKH LITSEYVTTS LASINSQAGS LFVLPRGVPF TDLDLTVGLV FLGCWGQITL TTFLTAMVLA TLHYGYMLPG WQAEALRAAQ RRTAAGIMKN AVVDGMVATD VPELERTTPL MQKKVGQVLL IGVSVAAFLV NPNVTTVREA GVLVTAATLT LWDNGASAVW NSTTATGLCH VMRGSYLAGG SIAWTLIKNA DKPSLKRGRP GGRTLGEQWK EKLNAMSREE FFKYRREAII EVDRTEARRA RRENNIVGGH PVSRGSAKLR WLVEKGFVSP IGKVIDLGCG RGGWSYYAAT LKKVQEVRGY TKGGAGHEEP MLMQSYGWNL VSLKSGVDVF YKPSEPSDTL FCDIGESSPS PEVEEQRTLR VLEMTSDWLH RGPREFCIKV LCPYMPKVIE KMEVLQRRFG GGLVRLPLSR NSNHEMYWVS GAAGNVVHAV NMTSQVLLGR MDRTVWRGPK YEEDVNLGSG TRAVGKGEVH SNQEKIKKRI QKLKEEFATT WHKDPEHPYR TWTYHGSYEV KATGSASSLV NGVVKLMSKP WDAIANVTTM AMTDTTPFGQ QRVFKEKVDT KAPEPPAGAK EVLNETTNWL WAHLSREKRP RLCTKEEFIK KVNSNAALGA VFAEQNQWST AREAVNDPRF WEMVDEEREN HLRGECHTCI YNMMGKREKK PGEFGKAKGS RAIWFMWLGA RYLEFEALGF LNEDHWLSRE NSGGGVEGSG VQKLGYILRD IAGKQGGKMY ADDTAGWDTR ITRTDLENEA KVLELLDGEH RMLARAIIEL TYRHKVVKVM RPAAEGKTVM DVISREDQRG SGQVVTYALN TFTNIAVQLV RLMEAEGVIG PQHLEQLPRK NKIAVRTWLF ENGEERVTRM AISGDDCVVK PLDDRFATAL HFLNAMSKVR KDIQEWKPSH GWHDWQQVPF CSNHFQEIVM KDGRSIVVPC RGQDELIGRA RISPGAGWNV KDTACLAKAY AQMWLLLYFH RRDLRLMANA ICSAVPVDWV PTGRTSWSIH SKGEWMTTED MLRVWNRVWI EENEWMMDKT PITSWTDVPY VGKREDIWCG SLIGTRSRAT WAENIYAAIN QVRAVIGKEN YVDYMTSLRR YEDVLIQEDR VI //