ID Q9II02_9FLAV Unreviewed; 3392 AA. AC Q9II02; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-DEC-2019, entry version 138. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS01197934}; OS Dengue virus 1. OC Viruses; Riboviria; Flaviviridae; Flavivirus. OX NCBI_TaxID=11053 {ECO:0000313|EMBL:AAF82038.1, ECO:0000313|Proteomes:UP000174616}; RN [1] {ECO:0000313|EMBL:AAF82038.1, ECO:0000313|Proteomes:UP000174616} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGA/NA d1d {ECO:0000313|EMBL:AAF82038.1}; RX PubMed=10964773; DOI=10.1006/viro.2000.0457; RA Duarte dos Santos C.N., Frenkiel M.P., Courageot M.P., Rocha C.F., RA Vazeille-Falcoz M.C., Wien M.W., Rey F.A., Deubel V., Despres P.; RT "Determinants in the envelope E protein and viral RNA helicase NS3 that RT influence the induction of apoptosis in response to infection with dengue RT type 1 virus."; RL Virology 274:292-308(2000). 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|SAAS:SAAS01122357}; 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|SAAS:SAAS01122355}; 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, ChEBI:CHEBI:83400; CC EC=2.7.7.48; Evidence={ECO:0000256|SAAS:SAAS01198479}; CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum CC {ECO:0000256|SAAS:SAAS01209087}. Virion membrane CC {ECO:0000256|SAAS:SAAS01195842}; Multi-pass membrane protein CC {ECO:0000256|SAAS:SAAS01195842}. 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; AF226686; AAF82038.1; -; Genomic_RNA. DR Proteomes; UP000174616; Genome. DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of 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:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:UniProtKB-EC. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW. DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR CDD; cd12149; Flavi_E_C; 1. DR Gene3D; 1.10.10.930; -; 1. DR Gene3D; 1.10.8.970; -; 1. DR Gene3D; 1.20.1280.260; -; 1. DR Gene3D; 2.60.260.50; -; 1. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 2.60.98.10; -; 1. DR Gene3D; 3.30.387.10; -; 1. DR Gene3D; 3.30.67.10; -; 1. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR000069; Env_glycoprot_M_flavivir. DR InterPro; IPR038302; Env_glycoprot_M_sf_flavivir. DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1. DR InterPro; IPR001122; Flavi_capsidC. DR InterPro; IPR037172; Flavi_capsidC_sf. DR InterPro; IPR027287; Flavi_E_Ig-like. DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom. DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf. 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; IPR038688; Flavi_propep_sf. DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR014412; Gen_Poly_FLV. DR InterPro; IPR011998; Glycoprot_cen/dimer. DR InterPro; IPR036253; Glycoprot_cen/dimer_sf. DR InterPro; IPR038055; Glycoprot_E_dimer_dom. DR InterPro; IPR013756; GlyE_cen_dom_subdom2. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR000208; RNA-dir_pol_flavivirus. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR029063; SAM-dependent_MTases. 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; PF00949; Peptidase_S7; 1. DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF101257; SSF101257; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF56983; SSF56983; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR TIGRFAMs; TIGR04240; flavi_E_stem; 1. DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1. DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1. PE 4: Predicted; KW Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00291633}; KW ATP-binding {ECO:0000256|SAAS:SAAS01198603}; KW Capsid protein {ECO:0000256|SAAS:SAAS01208933}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR003817-3, KW ECO:0000256|SAAS:SAAS01200326}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|SAAS:SAAS01200298}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|SAAS:SAAS01200343}; Helicase {ECO:0000256|SAAS:SAAS01209034}; KW Host membrane {ECO:0000256|SAAS:SAAS00291629}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00291630}; KW Hydrolase {ECO:0000256|SAAS:SAAS01198589}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|SAAS:SAAS00910833}; KW Membrane {ECO:0000256|SAAS:SAAS00291489, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4, KW ECO:0000256|SAAS:SAAS01198594}; KW Methyltransferase {ECO:0000256|SAAS:SAAS01198504}; KW mRNA capping {ECO:0000256|SAAS:SAAS01198443}; KW mRNA processing {ECO:0000256|SAAS:SAAS01198505}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS01198580}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01198562}; KW Protease {ECO:0000256|SAAS:SAAS01200356}; KW RNA-binding {ECO:0000256|SAAS:SAAS01198501}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS01198530}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS01198586}; KW Serine protease {ECO:0000256|SAAS:SAAS01200312}; KW Transferase {ECO:0000256|SAAS:SAAS01198537}; KW Transmembrane {ECO:0000256|SAAS:SAAS00291514, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00291474, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|SAAS:SAAS00291492}; KW Viral immunoevasion {ECO:0000256|SAAS:SAAS00910833}; KW Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS01200338}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS01198628}; KW Virion {ECO:0000256|SAAS:SAAS01197947}; KW Virus entry into host cell {ECO:0000256|SAAS:SAAS00291600}; KW Zinc {ECO:0000256|PIRSR:PIRSR003817-4}. FT TRANSMEM 101..119 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 724..748 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 755..773 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1158..1177 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1201..1221 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2149..2168 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2175..2192 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2198..2215 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2227..2244 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1346..1475 FT /note="FLAVIVIRUS_NS2B" FT /evidence="ECO:0000259|PROSITE:PS51527" FT DOMAIN 1476..1653 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 1656..1812 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1822..1988 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2495..2756 FT /note="MRNA cap 0-1 NS5-type MT" FT /evidence="ECO:0000259|PROSITE:PS51591" FT DOMAIN 3020..3169 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT ACT_SITE 1526 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1550 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1610 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT METAL 2930 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2934 FT /note="Zinc 1; via tele nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2939 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2942 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3204 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3220 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3339 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2549 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2579 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2580 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2597 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2598 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2624 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2625 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2711 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT DISULFID 283..310 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 340..396 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 354..385 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 372..401 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 465..565 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 582..613 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" SQ SEQUENCE 3392 AA; 379069 MW; B40F0FA5D7A8E976 CRC64; MNNQRKKTGR PSFNMLKRAR NRVSTGSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP PTAGILARWS SFKKNGAIKV LRGFKKEISS MLNIMNRRKR SVTMLLMLLP TVLAFHLTTR GGEPHMIVSK QERGKSLLFK TSAGVNMCTL IAMDLGELCE DTMTYKCPRI TEAEPDDVDC WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQKVETW ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW VDVVLEHGSC VTTMAKNKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA TLVEEQDANF VCRRTVVDRG WGNGCGLFGK GSLLTCAKFK CVTKLEGKIV QYENLKYSVI VTVHTGDQHQ VGNETTEHGT IATITPQAPT SEIQLTDYGT LTLDCSPRTG LDFNEVVLLT MKEKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV LVQVKYEGTD APCKIPFSTQ DEKGVTQNGR LITANPIVTD KEKPINIETE PPFGESYIIV GAGEKALKLS WFKKGSSIGK MFEAIARGAR RMAILGDTAW DFGSIGGVFT SVGKLVHQVF GTAYGVLFSG VSWTMKIGIG ILLTWLGLNS RSASLSMTCI AVGMVTLYLG VMVQADSGCV INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGKAWEEGVC GIRSATRLEN IMWKQISNEL NHILLENDMK FTVVVGDANG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG ADTQNTTFII DGPDTPECPD DQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQMCDHRLMS AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCIW PKSHTLWSNG VLESEMIIPK IYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGNRG PSLRTTTVTG KIIHEWCCRS CTLPPLRFRG EDGCWYGMEI RPVKEKEENL VRSMVSAGSG EVDSFSLGIL CVSIMIEEVM RSRWSRKMLM TGTLAVFLLL IMGQLTWNDL IRLCIMVGAN ASDRMGMGTT YLALMATFKM RPMFAVGLLF RRLTSREVLL LTIGLSLVAS VELPNSLEEL GDGLAMGIMM LKLLTEFQPH QLWTTLLSLT FIKTTLSLDY AWKTMAMVLS IVSLFPLCLS TTSQKTTWLP VLLGSFGCKP LTMFLITENK IWGRKSWPLN EGIMAIGIVS ILLSSLLKND VPLAGPLIAG GMLIACYVIS GSSADLSLEK AAEVSWEEEA EHSGTSHNIL VEVQDDGTMK IKDEERDDTL TILLKATLLA VSGVYPMSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI LQRGLLGRSQ VGVGVFQDGV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD LISYGGGWRF QGSWNTGEEV QVIAVEPGKN PKNVQTTPGT FKTPEGEVGA IALDFKPGTS GSPIVNREGK IVGLYGNGVV TTSGTYVSAI AQAKASQEGP LPEIEDEVFK KRNLTIMDLH PGSGKTRRYL PAIVREAIKR KLRTLILAPT RVVASEMAEA LKGMPIRYQT TAVKSEHTGR EIVDLMCHAT FTMRLLSPVR VPNYNMIIMD EAHFTDPASI AARGYISTRV GMGEAAAIFM TATPPGSVEA FPQSNAVIQD EERDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC LRKNGKRVIQ LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID PRRCLKPVIS KDGPERVILA GPMPVTVASA AQRRGRIGRN QNKEGDQYVY MGQPLNNDED HAHWTEAKML LDNINTPEGI IPALFEPERE KSAAIDGEYR LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF DGERNNQVLE ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL ILEIGKLPQH LTLRAQNALD NLVMLHNSEQ GGKAYRHAME ELPDTIETLM LLALIAVLTG GVMLFFLSGK GLGKTSIGLL CVMASSALLW MASVEPHWIA ASIILEFFLM VLLIPEPDRQ RTPQDNQLAY VVIGLLFMIL TVAANEMGLL ETTKKDLGIG HVAAENHHHV TMLDVDLRPA SAWTLYAVAT TVITPMMRHT IENTTANISL TAIANQAAIL MGLDKGWPIS KMDIGVPLLA LGCYSQVNPL TLTAAVLMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW EGSPGKFWNT TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE TLGEKWKRQL NQLSKSEFNT YKRSGIMEVD RSEAKEGLKR GETTKHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW SYYCAGLKKV TEVKGYTKGG PGHEEPIPMA TYGWNLVKLH SGKDVFFIPP EKCDTLLCDI GESSPNPTIE EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVAVE PEVANLDIIG QRIENIKNEH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVRLL TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPRAKR GTAQIMEMTA KWLWGFLSRN KKPRICTREE FIRKVRSNAA IGAVFVDENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA TCVYNMMGKR EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLQ NEAKITDIME PEHALLATSI FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEVQ LIRQMESEGI FLPSELETPN LAERVLDWLE KHGAERLKRM AISGDDCVVK PIDDRFATAL IALNDMGKVR KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED MLSVWNRVWI EENPWMEDKT HVSSWEEVPY LGKREDQWCG SLIGLTARAT WATNIQVAIN QVRRLIGNEN YLDYMTSMKR FKNESDPEGA LW //