ID A0MSJ9_9FLAV Unreviewed; 3392 AA. AC A0MSJ9; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 20-DEC-2017, entry version 95. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684}; OS Dengue virus 1. OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Flaviviridae; Flavivirus; Dengue virus group. 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 RT recombination regions in natural populations in Guangdong province, RT China."; RL Arch. Virol. 153:1175-1179(2008). CC -!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and CC is required for the interferon antagonism activity of the latter. CC {ECO:0000256|SAAS:SAAS00892720}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|SAAS:SAAS00368577}. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC {ECO:0000256|SAAS:SAAS00368620}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|SAAS:SAAS00383097}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S- CC adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. CC {ECO:0000256|SAAS:SAAS00232292}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl CC 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S- CC adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'- CC triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA]. CC {ECO:0000256|SAAS:SAAS00445805}. CC -!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds CC in which each of the Xaa can be either Arg or Lys and Yaa can be CC either Ser or Ala. {ECO:0000256|SAAS:SAAS00232385}. CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane CC {ECO:0000256|SAAS:SAAS00944756}; Peripheral membrane protein CC {ECO:0000256|SAAS:SAAS00944756}; Lumenal side CC {ECO:0000256|SAAS:SAAS00944756}. Host nucleus CC {ECO:0000256|SAAS:SAAS00892522}. Secreted CC {ECO:0000256|SAAS:SAAS00944768}. Virion membrane CC {ECO:0000256|SAAS:SAAS00944678}; Multi-pass membrane protein CC {ECO:0000256|SAAS:SAAS00944678}. 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 Proteomes; UP000155771; Genome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. 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:0008026; F:ATP-dependent helicase activity; IEA:InterPro. 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:InterPro. 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:0070008; F:serine-type exopeptidase 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:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW. DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; 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 CDD; cd00079; HELICc; 1. DR CDD; cd06174; MFS; 1. DR Gene3D; 2.60.40.350; -; 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; 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; 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; 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; IPR013756; GlyE_cen_dom_subdom2. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR020846; MFS_dom. 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:SAAS00445756}; KW ATP-binding {ECO:0000256|SAAS:SAAS00969169}; KW Capsid protein {ECO:0000256|SAAS:SAAS00969288}; KW Complete proteome {ECO:0000313|Proteomes:UP000155771}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR003817-3, KW ECO:0000256|SAAS:SAAS00139753}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|SAAS:SAAS00489633}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|SAAS:SAAS00489579}; KW Helicase {ECO:0000256|SAAS:SAAS00058020}; KW Host endoplasmic reticulum {ECO:0000256|SAAS:SAAS00944771}; KW Host membrane {ECO:0000256|SAAS:SAAS00445977}; KW Host nucleus {ECO:0000256|SAAS:SAAS00892445}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00445875}; KW Hydrolase {ECO:0000256|SAAS:SAAS00969059}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|SAAS:SAAS00941647}; KW Inhibition of host interferon signaling pathway by virus KW {ECO:0000256|SAAS:SAAS00892563}; KW Inhibition of host STAT2 by virus {ECO:0000256|SAAS:SAAS00892696}; KW Membrane {ECO:0000256|SAAS:SAAS00445865, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4, KW ECO:0000256|SAAS:SAAS00940329}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00817755}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00969385}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510590}; KW Protease {ECO:0000256|SAAS:SAAS00911134}; KW RNA-binding {ECO:0000256|SAAS:SAAS00076745}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600}; KW Secreted {ECO:0000256|SAAS:SAAS00944674}; KW Serine protease {ECO:0000256|SAAS:SAAS00462397}; KW Transferase {ECO:0000256|SAAS:SAAS00510371}; KW Transmembrane {ECO:0000256|SAAS:SAAS00445861, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00445939, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|SAAS:SAAS00445995}; KW Viral immunoevasion {ECO:0000256|SAAS:SAAS00941647}; KW Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00489650}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS00664279}; KW Virion {ECO:0000256|SAAS:SAAS00445868}; KW Virus entry into host cell {ECO:0000256|SAAS:SAAS00445755}; KW Zinc {ECO:0000256|PIRSR:PIRSR003817-4}. FT TRANSMEM 101 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 724 748 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 754 773 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2149 2168 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2175 2192 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2198 2215 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2227 2244 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1346 1475 FLAVIVIRUS_NS2B. {ECO:0000259|PROSITE: FT PS51527}. FT DOMAIN 1476 1653 Peptidase S7. {ECO:0000259|PROSITE: FT PS51528}. FT DOMAIN 1656 1812 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 1807 1988 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT DOMAIN 2495 2756 MRNA cap 0-1 NS5-type MT. FT {ECO:0000259|PROSITE:PS51591}. FT DOMAIN 3020 3169 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50507}. FT ACT_SITE 1526 1526 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT ACT_SITE 1550 1550 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT ACT_SITE 1610 1610 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT METAL 2930 2930 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 2934 2934 Zinc 1; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR003817-4}. FT METAL 2939 2939 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 2942 2942 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 3204 3204 Zinc 2; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR003817-4}. FT METAL 3220 3220 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 3339 3339 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT BINDING 2549 2549 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT BINDING 2579 2579 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2580 2580 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2597 2597 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT BINDING 2598 2598 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2624 2624 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT BINDING 2625 2625 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2711 2711 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT DISULFID 283 310 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 340 396 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 354 385 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 372 401 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 465 565 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 582 613 {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 //