ID A0MSJ9_9FLAV Unreviewed; 3392 AA. AC A0MSJ9; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 18-APR-2012, entry version 50. DE SubName: Full=Polyprotein; OS Dengue virus 1. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae; OC Flavivirus; Dengue virus group. OX NCBI_TaxID=11053; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GZ01/95; RA Zhou J.M., Liu X.L., Liang Y., Fang D.Y., Zhou J.J., Yan H.J., RA Jiang L.F.; RT "Molecular Epidemiological Study of Dengue Virus Type 1 in RT Guangzhou."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GZ01/95; RX PubMed=18446424; DOI=10.1007/s00705-008-0090-1; RA Chen S.P., Yu M., Jiang T., Deng Y.Q., Qin C.F., Han J.F., Qin E.D.; RT "Identification of a recombinant dengue virus type 1 with 3 RT recombination regions in natural populations in Guangdong province, RT China."; RL Arch. Virol. 153:1175-1179(2008). 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; EF032590; ABK54370.1; -; Genomic_RNA. DR ProteinModelPortal; A0MSJ9; -. DR SMR; A0MSJ9; 21-100, 115-195, 281-674, 1495-2094, 2500-2760, 2766-3375. 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: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 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 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 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 3392 AA; 378601 MW; 0CEA3643F14145A6 CRC64; MNNQRKKTGR PSFNMLKRAR NRVSTVSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP PTAGILARWG SFKKNGAIKV LRGFKKEISN MLNIMNRRKR SVTMLLMLLP TAMTFHLTTR GGEPHMIVSK QERGKSLLFK TSAGVNMCTL IAMDLGELCD DTMTYKCPRI SETEPDDVDC WCNATETWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWTSSEGA WRQIQKVETW ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW VDVVLEHGSC VTTMAKDKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA TLVEEQDTNF VCRRTFVDRG WGNGCGLFGK GSLITCAKFK CVTKLEGKIV QYENLKYSVI VTVHTGDQHQ VGNETTEHGT IATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT MKEKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGISYV MCTGPFKLEK EVAETQHGTV LVQVKYEGTD APCKIPFSSQ DEKGVTQNGR LVTANPIVTD KEKPVSIEAE PPFGESYIVV GAGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW DFGSIGGVFT SVGKLVHQIF GTAYGVLFSG VSWTMKIGIG ILLTWLGLNS RSTSLSMTCI AVGMVTLYLG VMVQADSGCV INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGKAWEEGVC GIRSATRLEN IMWKQISNEL NHILLENDMK FTVVVGDVSG ILAQGKKTIR PQPMEHKYSW KSWGKAKIIG ADVQNTTFII DGPNTPECPD DQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQVCDHRLMS AAIKDSKAVH ADMGYWMESE KNETWKLARA SFIEVKTCIW PKSHTLWSNG VLESEMIIPK IYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGNRG PSLRTTTVTG KIIHEWCCRS CTLPPLRFKG EDGCWYGMEI RPVKEKEENL VKSMVSAGSG EVDSFSLGLL CISIMIEEVM RSRWSRKMLM TGTLAVFLLL TMGQLTWNDL IRLCIMVGAN ASDNMGMGTT YLALMATFRM RPMFAVGLLF RRLTSREVLL LTVGLSLVAS VELPNSLEEL GDGFAMGIMI LKLLTDFQSH QLWATLLSLT FVKTTFSLHY AWKTMAMILS IVSLFPSCLS TTSQKTTWLP VLLGSLGCKP LTMFLITENK IWGRKSWPLN EGIMAVGIVS ILLSSLLKND VPLAGPLIAG GMLIACYVIS GSSADLSLEK AAEVSWEEEA EHSGASHNIL VEVQDDGTMK IKDEERDDTI TILLKATLLA ISGVYPMSIP ATPFVWYFWQ KKKQRSGELW DTPSPPEVER AVLDDGIYRI LQRGLLGRSQ VGVGVFQEGV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD LISYGGGWRF QGSWNTGEEV QVIAVEPGKN PKNVQTAPGT FKTSEGEVGA IALDFKPGTS GSPIVNREGK IVGLYGNGVV TTSGTYVSAI AQAKASQEGP LPEIEDEVFR KRNLTIMDLH PGSGKTRRYL PAIVREAIKR KLRTLVLAPT RVVASEMAEA LKGMPIRYQT TAVKSEHTGK EIVDLMCHAT FTMRLLSPVR VPNYNMIIMD EAHFTDPASI AARGYISTRV GMGEAAAIFM TATPPGSVEA FPQSNAVIQD EEKDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC LRKNGKRVIQ LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID PRRCLKPVIL KDGPERVILA GPMPVTVASA AQRRGRIGRN QNKEGDQYVY MGQPLNNDED HAHWTEAKML LDNINTPEGI IPALFEPERE KSAAIDGEYR LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF DGERNNQVLE ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL ILEIGKLPQH LTQRAQNALD NLVMLHNSEQ GGKAYRHAME ELPDTIETLM LLALIAVLTG GVTLFFLSGR GLGKTSIGLL CVMSSSALLW MASEEPHWIA ASIILEFFLM VLLIPEPDRQ RTPQDNQLAY VVIGLLFVIL TVAANEMGLL ETTKKDLGIG HAAAENHHHA AMLDVDLHPA SAWTLYAVAT TIITPMMRHT IENTTANISL TAIANQAAIL MGLDKGWPIS KMDIGVPLLA LGCYSQVNPL TLTAAVLMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW EGSPGKFWNT TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE TLGEKWKRQL NQLSKSEFNT YKRSGIIEVD RSEAKEGLRR GETTKHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW SYYCAGLKKV TEVKGYTKGG PGHEEPIPMA AYGWNLVKLH SGKDVFFIPP EKCDTLLCDI GESSPNPTIE EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVAVE PEVANLDIIG QRIENIKNEH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVRLL TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPKAKR GTAQIMEVTA RWLWGFLSRN KKPRICTREE FTRKVRSNAA IGAVFVDENQ WNSAKEAVED ERFWDLVRRE RELHKQGKCA TCVYNMMGKR EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SGENSLSGVE GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLQ NEAKITDIME PEHALLATSI FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEAQ LIRQMESEGI FSPSELETPN LAGRVLDWLE KHGIERLRRM AISGDDCVVK PIDDRFATAL TALNDMGKVR KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED MLSVWNRVWI EENPWMEDKT HVSSWEDIPY LGKREDQWCG SLIGLTARAT WATNIQVAIS QVRRLIGNEN YLDYMTSMKR FKNESDPEGA LW //