ID   Q91NH1_9FLAV            Unreviewed;      3392 AA.
AC   Q91NH1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   18-APR-2012, entry version 75.
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=D1/H/IMTSSA/98/606;
RX   MEDLINE=21262211; PubMed=11369871;
RA   Tolou H.J., Couissinier-Paris P., Durand J.P., Mercier V.,
RA   de Pina J.J., de Micco P., Billoir F., Charrel R.N.,
RA   de Lamballerie X.;
RT   "Evidence for recombination in natural populations of dengue virus
RT   type 1 based on the analysis of complete genome sequences.";
RL   J. Gen. Virol. 82:1283-1290(2001).
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.
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DR   EMBL; AF298808; AAK60418.1; -; Genomic_RNA.
DR   HSSP; Q88653; 1L9K.
DR   ProteinModelPortal; Q91NH1; -.
DR   SMR; Q91NH1; 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;  379033 MW;  5BD567C366E75623 CRC64;
     MNNQRKKTGR PSFNMLKRAR NRVSTVSQLA KRFSKGLLSG QGPMKLVMAF IAFLTFLAIP
     PTAGILARWG SFKKNGAIKV LRGFKKEISN MLNIMNRRKR SVTMLLMLLP TVLAFHLTTR
     GGEPHMIVTK QERGKSLLFK TSTGVNMCTL IAMDLGELCE DTMTYKCPRI TEAEPDDVDC
     WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQRVETW
     ALRHPGFTVT ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW
     VDVVLEHGSC VTTMAKDKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA
     TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSLITCAKFK CVTKLEGKIV QYENLKYSVI
     VTVHTGDQHQ VGNESTEHGT TATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT
     MKEKSWLVHK QWFLDLPLPW TSGATTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM
     HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV
     LVQVKYEGTD APCKIPFSTQ DEKGVTQNGR VITANPIVTD KEKPVNIEAE PPFGESYIVV
     GAGEKALKLS WFKKGSTIGK MFEATARGAR RMAILGDTAW DFGSIGGVFT SVGKLVHQIF
     GTAYGVLFSG VSWTMKIGIG VLLTWLGLNS RSTSLSMTCI AVGLVTLYLG VMVQADSGCV
     INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGKAWEEGVC GIRSATRVEN
     IMWKQISNEL NHILFENDMK FTVVVGDVSG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG
     ADVQNSTFII DGPNTPECPD DQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQVCDHRLMS
     AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCVW PKSHTLWSNG VLESEMIIPK
     IYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGNRG PSLRTTTVTG
     KIIHEWCCRS CTLPPLRFKG EDGCWYGMEI RPVKEKEENL VKSMVSAGLG EVDSFSLGLL
     CISIMIEEVM RSRWSRKMLM TGTLAVFLLL IMGQLTWNDL IRLCIMIGAN ASDRMGMGTT
     YLALMATFKM RPMFAVGLLF RRLTSREVLL LTIGLSLVAS VELPNSLEEL GDGLAMGIMI
     LKLLTDFQSH QLWAELLSLT FIKTTCSLHY AWKTMAMVLS IVSLFPLCMS TTSQKTTWLP
     VLLGSLGCKP LTMFLIAENK IWGRKSWPLN EGIMAVGIVS ILLSSLLKND VPLAGPLIAG
     GMLIACYVIS GSSADLSLEK AAEVSWEEEA EHSGASHNIL VEVQDDGTMK IKDEERDDTL
     TILLKATLLA VSGVYPLSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI
     MQRGLLGRSQ VGVGVFQENV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD LISYGGGWRL
     QGSWNTGEEV QVIAVEPGKN PKNVQTAPGT FKTPEGEVGA IALDFKPGTS GSPIVNREGK
     IVGLYGNGVV TTSGTYVSAI AQAKASQEGP LPEIEDEVFR KRNLTIMDLH PGSGKTRRYL
     PAIVREAIKR KLRTLILAPT RVVASEMAEA LKGMPIRYQT TAVKSEHTGK EIVDLMCHAT
     FTMRLLSPVR VPNYNMIIMD EAHFTDPSSI AARGYISTRV GMGEAAAIFM TATPPGSVEA
     FPQSNAVIQD EERDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC LRKNGKRVIQ
     LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID PRRCLKPVIL KDGPERVILA
     GPMPVTVASA AQRRGRIGRN QNKEGDQYIY MGQPLNNDED HAHWTEAKML LDNINTPEGI
     IPALFEPERE KSAAIDGEYR LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF
     DGERNNQVLE ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL
     ILEIGKLPQH LTQRAQNALD NLVMLHNSEQ GGRAYRHAME ELPDTIETLM LLALIAVLTG
     GVTLFFLSGR GLGKTSIGLL CVMASSVLLW MASVEPHWIA ASIILEFFLM VLLIPEPDRQ
     RTPQDNQLAY VVIGLLFMIL TVAANEMGLL ETTKKDLGIG HVAVENHHHA TMLDVDLHPA
     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 RSEAKEGLKR GETTKHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW
     SYYCAGLKKV TEVKGYTKGG AGHEEPIPMA TYGWNLVKLH SGKDVFFTPP EKCDTLLCDI
     GESSPNPTIE EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN
     PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVTVE
     PEVANLDIIG QRIENIKHEH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVRLL
     TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPKAKR GTAQVMEVTA RWLWGFLSRN
     KKPRICTREE FTRKVRSNAA IGAVFVDENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA
     RCVYNMMGKR EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE
     GEGLHRLGYI LRGISKIPGG NMYADDTAGW DTRISEDDLQ NEAKITDIME PEHALLATSI
     FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEAQ LIRQMESEGI
     FSPSELETPN LAQRVLNWLE KYGVERLKRM AISGDDCVVK PIDDRFATAL TALNDMGKVR
     KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAEWSL
     RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTEN
     MLSVWNRVWI EENPWMEDKT HVSSWEDVPY LGKREDQWCG SLIGLTARAT WATNIQVAIN
     QVRRLIGNEN YLDYMTSMKR FKNDSDPEGA LW
//