ID A0A1U8ZS77_9FLAV Unreviewed; 3411 AA. AC A0A1U8ZS77; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 25-APR-2018, entry version 9. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684}; GN ORFNames=AVI39_00001 {ECO:0000313|EMBL:AMZ00439.1}; OS Yellow fever virus. OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Flaviviridae; Flavivirus; Yellow fever virus group. OX NCBI_TaxID=11089 {ECO:0000313|EMBL:AMZ00439.1}; RN [1] {ECO:0000313|EMBL:AMZ00439.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ogbomosho {ECO:0000313|EMBL:AMZ00439.1}; RG Consortium for Microbial Forensics and Genomics (microFORGE); RA Rossi S.L., Guerbois M., Forrester N.L., Ksiazek T., Lin D., Hari K., RA Weaver S.C.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. 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 cytoplasm CC {ECO:0000256|SAAS:SAAS00937464}. Host endoplasmic reticulum CC membrane {ECO:0000256|SAAS:SAAS00949449}; Peripheral membrane CC protein {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; KU978763; AMZ00439.1; -; Genomic_RNA. 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; 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; -; 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; 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; 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; 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:SAAS00510945}; KW Capsid protein {ECO:0000256|SAAS:SAAS00969288}; 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 cytoplasm {ECO:0000256|SAAS:SAAS00936979}; 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:SAAS00510997}; 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:SAAS00510884}; 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 44 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 125 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 245 264 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 271 287 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 730 751 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 758 778 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1133 1151 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1160 1181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1201 1220 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1232 1249 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1293 1310 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1322 1346 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1358 1376 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1382 1400 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1451 1477 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2157 2180 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2187 2204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2210 2227 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2239 2256 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2293 2314 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1355 1484 FLAVIVIRUS_NS2B. {ECO:0000259|PROSITE: FT PS51527}. FT DOMAIN 1485 1665 Peptidase S7. {ECO:0000259|PROSITE: FT PS51528}. FT DOMAIN 1669 1825 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 1820 1997 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT DOMAIN 2507 2771 MRNA cap 0-1 NS5-type MT. FT {ECO:0000259|PROSITE:PS51591}. FT DOMAIN 3035 3187 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50507}. FT ACT_SITE 1537 1537 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT ACT_SITE 1561 1561 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT ACT_SITE 1622 1622 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT METAL 2945 2945 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 2949 2949 Zinc 1; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR003817-4}. FT METAL 2954 2954 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 2957 2957 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 3222 3222 Zinc 2; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR003817-4}. FT METAL 3238 3238 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 3357 3357 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT DISULFID 288 315 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 345 401 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 359 390 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 377 406 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 467 568 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 585 615 {ECO:0000256|PIRSR:PIRSR003817-3}. SQ SEQUENCE 3411 AA; 379326 MW; BE7F4059402A7DA3 CRC64; MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK ITAHLKRLWK MLDPRQGLAV LRKVKRVVAG LMRGLSSRKR RSHDVLTVQF LILGMLLMAG GVTLVRKNRW LLLNVTSEDL GKTFSVGTGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD DIDCWCYGVE NVRVAYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ KIERWLVRNP FFAVTALAIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDGPAE ARKVCYNAVL THVKINDKCP STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI QYVIRAQLHV GAKQENWNTD IKTLKFDALS GSQEAEFTGY GKATLECQVQ TAVDFGNSYI AEMEKESWIV DRQWAQDLTL PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGNQEGSLK TALTGATRVT KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH GTVVMQVKVP KGAPCKIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD AAWDFSSAGG FFTSIGKGIH TVFGSAFQGL FGGLSWITKV IMGAVLIWVG INTRNMTMSM SMILVGVIMM FLSLGVGADQ GCAINFGKRE LKCGDGIFIF RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS LEHEMWRSRA DEINAILEEN EVDISVVVQD PKNVYQRGTH PFSRIRDGLQ YGWKTWGKNL VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGTGV FTTRVYMDAV FEYTIDCDGS ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLETLDYK ECEWPLTHTI GTSVEESDMF MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP LEVKREACPG TSVIIDGNCD GRGKSTRSTT DSGKIIPEWC CRSCTMPPVS FHGNDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL VSMMIAMEVV LRKRQGPKQM LVGGMVLLGA MLVGQVTLLD LLKLTMAVGL HFHEMNNGGD AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGMMG GLWKYLNAVS LCILTINAVA SRRASNIILP LMALLTPVTM AEVRLATMLF CTVVIIGVLH QNSKDTSMQK TIPLVALTLT SYLGLTQPFL GLCAFLATRI FGRRSIPVNE ALAAAGLVGV LAGLAFQEME NFLGPIAVGG ILMMLVSVAG RVDGLELKKL GEVSWEEEAE ISGSSARYDV TLSEQGEFKL LSEEKVPWDQ VVMTSLALVG AAIHPFALLL VLAGWLFHVK GARRSGDVLW DIPTPKIIEE CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVRNGKK LIPSWASVKE DLVAYGGSWK LEGRWDGEEE VQLIAAVPGK NVVNVQTKPS LFKVRNGGEI GAVALDYPSG TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS AISQTEVKEE GKEELQEIPT MLKKGMTTIL DFHPGAGKTR RFLPQILAEC ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG SGREVIDAMC HATLTYRMLE PTRIVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWNTGHDWI LADKRPTAWF LPSIRAANVM AASLRKAGKS VVVLNRKTFE KEYPTIKQKK PDFILATDIA EMGANLCVER VLDCRTAFKP VLVDEGRKVA IKGPLRISAS SAAQRRGRIG RNPNRDGDSY YYSEPTSEDN AHHVCWLEAS MLLDNMEVRG GMVAPLYGIE GTKTPVSPGE MRLRDDQRRV FRELVRNCDL PVWLSWQVAK AGLKTNDRKW CFEGPEEHEI LNDSGETVKC RAPGGAKRPL RPRWCDERVS SDQSALADFI KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI VMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYIMLIFFV LMVVVIPEPG QQRSIQDNQV AYLIIGILTL VSVVAANELG MLERTKEDLF GKKNLISSSA SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI PFMKMNISVI ILLVSGWNSI TVMPLLCGIG CAMLHWTLIL PGIKAQQSKL AQRRVFHGVA KNPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLVSAAL GPLIEGNTSL LWNGPMAVSM TGVMRGNYYA FVGVMYNLWK MKTGRRGSAN GKTLGEVWKR ELNLLDKQQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE GRVTDLGCGR GGWCYYAAAQ KEVSGVKGFT LGREGHEKPM NVQSLGWNII TFKDKTDIHR LEPVKCDTLL CDIGESSSSS VTEGERTMRV LDTVERWLAC GVDNFCVKVL APYMPDVLEK LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE ADVILPIGTR SVETDKGPLN REAIEERVER IKSEYMTTWF YDNDNPYRTW HYCGSYVTKT SGSAASMVNG VIKILTYPWD RIEEVTRMAM TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI MKVVNRWLFR HLAREKNPRL CTKEEFIAKV RSHAAIGAYL EEQEQWKTAN EAVQDPKFWE LVDEERKLHQ QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGFYAD DTAGWDTRIT EADLDDEQEI LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV ISRRDQRGSG QVVTYALNTI TNLKVQLIRM AEAEMVIHHH HVQDCDDSTL ARLEAWLIEH GCDRLNRMAV SGDDCVVRPI DDRFGMALSH LNAMSKVRKD ISEWQPSKGW NDWENVPFCS HHFHELQLKD GRRIVVPCRE QDELIGRGRV SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ GRTTWSIHGK GEWMTTEDML EVWNRVWITN NPHMQDKTVV KEWRDVPYLT KRQDKLCGSL IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS VDADLQPGEL I //