ID G3FEY0_9FLAV Unreviewed; 3432 AA. AC G3FEY0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 53. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684}; OS Japanese encephalitis virus. OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Flaviviridae; Flavivirus; Japanese encephalitis virus group. OX NCBI_TaxID=11072 {ECO:0000313|EMBL:AEO86792.1, ECO:0000313|Proteomes:UP000129773}; RN [1] {ECO:0000313|EMBL:AEO86792.1, ECO:0000313|Proteomes:UP000129773} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZMT {ECO:0000313|EMBL:AEO86792.1}; RX PubMed=21697481; DOI=10.1128/JVI.00825-11; RA Pan X.L., Liu H., Wang H.Y., Fu S.H., Liu H.Z., Zhang H.L., Li M.H., RA Gao X.Y., Wang J.L., Sun X.H., Lu X.J., Zhai Y.G., Meng W.S., He Y., RA Wang H.Q., Han N., Wei B., Wu Y.G., Feng Y., Yang D.J., Wang L.H., RA Tang Q., Xia G., Kurane I., Rayner S., Liang G.D.; RT "Emergence of genotype I of Japanese encephalitis virus as the RT dominant genotype in Asia."; RL J. Virol. 85:9847-9853(2011). 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:SAAS00251038}. 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:SAAS00461695}. 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:SAAS00252694}. CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane CC {ECO:0000256|SAAS:SAAS00949449}; Peripheral membrane protein CC {ECO:0000256|SAAS:SAAS00949449}; Lumenal side CC {ECO:0000256|SAAS:SAAS00949449}. Host nucleus CC {ECO:0000256|SAAS:SAAS00892522}. Secreted CC {ECO:0000256|SAAS:SAAS00949493}. Virion membrane CC {ECO:0000256|SAAS:SAAS00980400}; Multi-pass membrane protein CC {ECO:0000256|SAAS:SAAS00980400}. 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; JF706283; AEO86792.1; -; Genomic_RNA. DR Proteomes; UP000129773; 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 Gene3D; 1.10.10.930; -; 1. DR Gene3D; 1.10.8.970; -; 1. DR Gene3D; 1.20.1280.260; -; 1. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 2.60.98.10; -; 3. DR Gene3D; 3.30.387.10; -; 2. DR Gene3D; 3.30.67.10; -; 4. 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; 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:SAAS00445756}; KW ATP-binding {ECO:0000256|SAAS:SAAS00969169}; KW Capsid protein {ECO:0000256|SAAS:SAAS00969288}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000129773}; 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:SAAS00949494}; 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:SAAS00255078}; KW RNA-binding {ECO:0000256|SAAS:SAAS00076745}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600}; KW Secreted {ECO:0000256|SAAS:SAAS00949393}; KW Serine protease {ECO:0000256|SAAS:SAAS00255094}; 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 112 130 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 254 273 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 279 298 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 746 767 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 773 794 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1178 1197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1250 1274 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1280 1304 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1342 1365 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1377 1395 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1477 1497 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2173 2193 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2200 2220 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2226 2244 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2256 2278 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2369 2392 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1374 1504 FLAVIVIRUS_NS2B. {ECO:0000259|PROSITE: FT PS51527}. FT DOMAIN 1505 1682 Peptidase S7. {ECO:0000259|PROSITE: FT PS51528}. FT DOMAIN 1685 1841 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 1852 2017 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT DOMAIN 2528 2793 MRNA cap 0-1 NS5-type MT. FT {ECO:0000259|PROSITE:PS51591}. FT DOMAIN 3057 3209 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50507}. FT COILED 2796 2816 {ECO:0000256|SAM:Coils}. FT ACT_SITE 1555 1555 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT ACT_SITE 1579 1579 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT ACT_SITE 1639 1639 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT METAL 2967 2967 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 2971 2971 Zinc 1; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR003817-4}. FT METAL 2976 2976 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 2979 2979 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 3244 3244 Zinc 2; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR003817-4}. FT METAL 3260 3260 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 3379 3379 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT BINDING 2583 2583 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT BINDING 2613 2613 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2614 2614 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2631 2631 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT BINDING 2632 2632 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2658 2658 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT BINDING 2659 2659 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2747 2747 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT DISULFID 297 324 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 354 410 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 368 399 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 386 415 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 484 581 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 598 629 {ECO:0000256|PIRSR:PIRSR003817-3}. SQ SEQUENCE 3432 AA; 380151 MW; 6F537678D97E402F CRC64; MTKKPGGPGK NRAINMLKRG LPRVFPLVGV KRVVMSLLDG RGPVRFVLAL ITFFKFTALA PTKTLLGRWK AVEKSVAMKH LTSFKRELGT LIDAVNKRGR KQNKRGGNEG SIMWLASLAV VIACAGAMKL SNFQGKLLMT INNTDIADVI VIPTSKGENR CWVRAIDVGY MCEDTITYEC PKLTMGNDPE DVDCWCDNQE VYVQYGRCTR TRHSKRSRRS VSVQIHGESS LVNKKEAWLD STKATRYLMK TENWIIRNPG YAFLAAVLGW MLGSNNGQRV VFTILLLLVA PAYSFNCLGM GNRDFIEGAS GATWVDLVLE GDSCLTIMAN DKPTLDVRMI NIEASQLAEV RSYCYHASVT DISTVARCPT TGEAHNKKRA DSSYVCKQGF TDRGWGNGCG LFGKGSIDTC AKFSCTSKAI GRTIQPENIK YEVGIFVHGT TTSENHGNYS AQVGASQAAK FTVTPNAPSI TLKLGDYGEV TLDCEPRSGL NTEAFYVMTV GSKSFLVHRE WFHDLALPWT SPSSTAWRNR ELLMEFEEAH ATKQSVVALG SQEGGLHQAL AGAIVVEYSS SVKLTSGHLK CRLKMDKLAL KGTTYGMCTE KFSFAKNPAD TGHGTVVIEL SYSGSDGPCK IPIVSVASLN DMTPVGRLVT VNPFVATSSA NSKVLVEMEP PFGDSYIVVG RGDKQINHHW HKAGSTLGKA FSTTLKGAQR LAALGDTAWD FGSIGGVFNS IGKAVHQVFG GAFRTLFGGM SWITQGLMGA LLLWMGVNAR DRSIALAFLA TGGVLVFLAT NVHADTGCAI DITRKEMRCG SGIFVHNDVE AWVDRYKYLP ETPRSLAKIV HKAHKEGVCG VRSVTRLEHQ MWEAVRDELN VLLKENAVDL SVVVNKPVGR YRSAPKRLSM TQEKFEMGWK AWGKSILFAP ELANSTFVVD GPETKECPDE HRAWNSMQIE DFGFGITSTR VWLKIREEST DECDGAIIGT AVKGHVAVHS DLSYWIESRY NDTWKLERAV FGEVKSCTWP ETHTLWGDGV EESELIIPHT IAGPKSKHNR REGYKTQNQG PWDENGIVLD FDYCPGTKVT ITEDCGKRGP SVRTTTDSGK LITDWCCRSC SLPPLRFRTE NGCWYGMEIR PVRHDETTLV RSQVDAFNGE MVDPFQLGLL VMFLATQEVL RKRWTARLTI PAVLGALLVL MLGGITYTDL ARYVVLVAAA FAEANSGGDV LHLALIAVFK IQPAFLVMNM LSTRWTNQEN VVLVLGAAFF QLASVDLQIG VHGILNAAAI AWMIVRAITF PTTSSVTMPV LALLTPGMRA LYLDTYRIIL LVIGICSLLQ ERKKTMAKKK GAVLLGLALT STGWFSPTTI AAGLMVCNPN KKRGWPATEF LSAVGLMFAI VGGLAELDIE SMSIPFMLAG LMAVSYVVSG KATDMWLERA ADISWEMDAA ITGSSRRLDV KLDDDGDFHL IDDPGVPWKV WVLRMSCIGL AALTPWAIVP AAFGYWLTLK TTKRGGVFWD TPSPKPCSKG DTTTGVYRIM ARGILGTYQA GVGVMYENVF HTLWHTTRGA AIMSGEGKLT PYWGSVKEDR IAYGGPWRFD RKWNGTDDVQ VIVVEPGKAA VNIQTKPGVF RTPFGEVGAV SLDYPRGTSG SPILDSNGDI IGLYGNGVEL GDGSYVSAIV QGDRQEEPVP EAYTPNMLRK RQMTVLDLHP GSGKTRKILP QIIKDAIQQR LRTAVLAPTR VVAAEMAEAL RGLPVRYQTS AVQREHQGNE IVDVMCHATL THRLMSPNRV PNYNLFVMDE AHFTDPASIA ARGYIATKVE LGEAAAIFMT ATPPGTTDPF PDSNAPIHDL QDEIPDRAWS SGYEWITEYA GKTVWFVASV KMGNEIAMCL QRAGKKVIQL NRKSYDTEYP KCKNGDWDFV ITTDISEMGA NFGASRVIDC RKSVKPTILE EGEGRVILGN PSPITSASAA QRRGRVGRNP NQVGDEYHYG GATSEDDSNL AHWTEAKIML DNIHMPNGLV AQLYGPEREK AFTMDGEYRL RGEEKKNFLE LLRTADLPVW LAYKVASNGI QYTDRKWCFD GPRTNAILED NTEVEIVTRM GERKILKPRW LDARVYADHQ ALKWFKDFAA GKRSAVSFIE VLGRMPEHFM GKTREALDTM YLVATAEKGG KAHRMALEEL PDALETITLI VAITVMTGGF FLLMMQRKGI GKMGLGALVL TLATFFLWAA EVPGTKIAGT LLIALLLMVV LIPEPEKQRS QTDNQLAVFL ICVLTVVGVV AANEYGMLEK TKADLKSMFG GKTQASGLTG LPSMALDLRP ATAWALYGGS TVVLTPLLKH LITSEYVTTS LASINSQAGS LFVLPRGVPF TDLDLTVGLV FLGCWGQITL TTFLTAMVLA TLHYGYMLPG WQAEALRAAQ RRTAAGIMKN AVVDGMVATD VPELERTTPL MQKKVGQVLL IGVSVAAFLV NPNVTTVREA GVLVTAATLT LWDNGASAVW NSTTATGLCH VMRGSYLAGG SIAWTLIKNA DKPSLKRGRP GGRTLGEQWK EKLNAMSREE FFKYRREAII EVDRTEARRA RRENNIVGGH PVSRGSAKLR WLVEKGFVSP IGKVIDLGCG RGGWSYYAAT LKKVQEVRGY TKGGAGHEEP MLMQSYGWNL VSLKSGVDVF YKPSEPSDTL FCDIGESSPS PEVEEQRTLR VLEMTSDWLH RGPREFCIKV LCPYMPKVIE KMEVLQRRFG GGLVRLPLSR NSNHEMYWVS GAAGNVVHAV NMTSQVLLGR MDRTVWRGPK YEEDVNLGSG TRAVGKGEVH SNQEKIKKRI QKLKEEFATT WHKDPEHPYR TWTYHGSYEV KATGSASSLV NGVVKLMSKP WDAIANVTTM AMTDTTPFGQ QRVFKEKVDT KAPEPPAGAK EVLNETTNWL WAHLSREKRP RLCTKEEFIK KVNSNAALGA VFAEQNQWST AREAVNDPRF WEMVDEEREN HLRGECHTCI YNMMGKREKK PGEFGKAKGS RAIWFMWLGA RYLEFEALGF LNEDHWLSRE NSGGGVEGSG VQKLGYILRD IAGKQGGKMY ADDTAGWDTR ITRTDLENEA KVLELLDGEH RMLARAIIEL TYRHKVVKVM RPAAEGKTVM DVISREDQRG SGQVVTYALN TFTNIAVQLV RLMEAEGVIG PQHLEQLPRK NKIAVRTWLF ENGEERVTRM AISGDDCVVK PLDDRFATAL HFLNAMSKVR KDIQEWKPSH GWHDWQQVPF CSNHFQEIVM KDGRSIVVPC RGQDELIGRA RISPGAGWNV KDTACLAKAY AQMWLLLYFH RRDLRLMANA ICSAVPVDWV PTGRTSWSIH SKGEWMTTED MLRVWNRVWI EENEWMMDKT PITSWTDVPY VGKREDIWCG SLIGTRSRAT WAENIYAAIN QVRAVIGKEN YVDYMTSLRR YEDVLIQEDR VI //