ID A0MSJ9_9FLAV Unreviewed; 3392 AA. AC A0MSJ9; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 22-APR-2020, entry version 112. 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:ABK54370.1, ECO:0000313|Proteomes:UP000155771}; RN [1] {ECO:0000313|EMBL:ABK54370.1, ECO:0000313|Proteomes:UP000155771} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GZ01/95 {ECO:0000313|EMBL:ABK54370.1}; 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 recombination RT regions in natural populations in Guangdong province, China."; RL Arch. Virol. 153:1175-1179(2008). CC -!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the CC serine protease function of NS3. {ECO:0000256|PROSITE- CC ProRule:PRU00859}. 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}. Host nucleus CC {ECO:0000256|SAAS:SAAS01249369}. 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; EF032590; ABK54370.1; -; Genomic_RNA. DR Proteomes; UP000155771; Genome. DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-UniRule. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. 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:SAAS01197962}; 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 endoplasmic reticulum {ECO:0000256|PROSITE-ProRule:PRU00859}; KW Host membrane {ECO:0000256|PROSITE-ProRule:PRU00859, KW ECO:0000256|SAAS:SAAS00291629}; KW Host nucleus {ECO:0000256|SAAS:SAAS01249452}; 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|PROSITE-ProRule:PRU00859, KW 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|PROSITE-ProRule:PRU00859, KW ECO:0000256|SAAS:SAAS00291514, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00859, KW ECO:0000256|SAAS:SAAS00291474, 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 754..773 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 1807..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 REGION 1398..1437 FT /note="Interacts with and activates NS3 protease" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00859" 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; 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 //