ID Q32ZD3_9FLAV Unreviewed; 3405 AA. AC Q32ZD3; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 23-MAY-2018, entry version 105. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684}; OS Sepik virus. OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Flaviviridae; Flavivirus; mosquito-borne viruses. OX NCBI_TaxID=44026 {ECO:0000313|EMBL:AAV34159.1, ECO:0000313|Proteomes:UP000124629}; RN [1] {ECO:0000313|EMBL:AAV34159.1, ECO:0000313|Proteomes:UP000124629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16223950; DOI=10.1128/CMR.18.4.608-637.2005; RA Kuno G., Chang G.J.; RT "Biological transmission of arboviruses: reexamination of and new RT insights into components, mechanisms, and unique traits as well as RT their evolutionary trends."; RL Clin. Microbiol. Rev. 18:608-637(2005). 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; AY632543; AAV34159.1; -; Genomic_RNA. DR MEROPS; S07.001; -. DR Proteomes; UP000124629; 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: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; 1.10.8.970; -; 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; 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 Complete proteome {ECO:0000313|Proteomes:UP000124629}; 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 39 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 719 743 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 750 770 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1154 1176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1227 1245 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1319 1343 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1350 1371 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1377 1395 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1446 1473 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2152 2175 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2182 2198 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2204 2222 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2234 2251 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2286 2307 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1350 1479 FLAVIVIRUS_NS2B. {ECO:0000259|PROSITE: FT PS51527}. FT DOMAIN 1480 1659 Peptidase S7. {ECO:0000259|PROSITE: FT PS51528}. FT DOMAIN 1664 1820 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 1815 1992 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT DOMAIN 2500 2764 MRNA cap 0-1 NS5-type MT. FT {ECO:0000259|PROSITE:PS51591}. FT DOMAIN 3028 3180 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50507}. FT ACT_SITE 1531 1531 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT ACT_SITE 1555 1555 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT ACT_SITE 1616 1616 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT METAL 2938 2938 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 2942 2942 Zinc 1; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR003817-4}. FT METAL 2947 2947 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 2950 2950 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 3215 3215 Zinc 2; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR003817-4}. FT METAL 3231 3231 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 3350 3350 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. 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 462 560 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 577 607 {ECO:0000256|PIRSR:PIRSR003817-3}. SQ SEQUENCE 3405 AA; 379445 MW; B27D0C3D46A90304 CRC64; MATRGASKSR VTTRGVNMVT AKAKSLAVKI KNKTKQNTRG LRGFLLFLVA QIFWARKLTP QVKKLWRMVD KVQGLKILKK LRNIVTNLMK GLSGRRKRRS PPASIILLLL PLMAYSASVT RQHGAGLLLN VTFADVGKTF EVQGGNCSVN TLEAGKWCDD YVEYACVTLT EGEEPDDLDC WCYGVDNVRV TYGRCKGGGS RRSRRSALIT PHVDKGLTTR QEKWLPSKIG EQQLQKVEKW IIRNPLYALG AIALAYFIGT SVVQKVVIAI LLLGIGPAYS THCLGIPKRD FIRGLDGNTW VSVVLEQGGC VTLIADNKPS VDVWLSSIVV DTPTLVRKIC YESSVTGSKA EGACPTMGDA HLTEEGNEEW ECKRSFSDRG WGNGCGLFGK GSIVACAKFS CTKEMEVYQI DSTKIEYTIS AQVHSGAKKE DWVNHTKLIK FVPTTGTSTV TFTGYGNFGL ECHVQMMVDL GNSYLVKVGT DAWLVNKQWA HDITLPWQSG TGGHWRDKHF MVDFEQPHAV TMKALVLGSQ EGALRTALSG AMVVEVSSNR YTLKGGHVTC KAYMNDLTLK GSTYPMCKKG MSFVKQPVET DHGTAVMQVK VTNGAPCRIP VIASDSMAGT ENRGSVITTN PIAALNNDEV LVEISPPFGE SYIIVGSGDD KLTYHWQRSG STIGNLFTET MKGAQRMIIT GEHSWDFGST GGFFASVGKA IHTVFGTAFH AMFGGLSWMT KILIGGLMVW LGLNSRSSSL SMAFICLGAL LLVLATGVGA EVGCSLNWKQ REVKCGDGMF VFKDTDDWFT KYQYIPEDPK TMAGLIAQAH EEGLCGLNSV GDLEHRMWVS RVDEINAILE ENDIDLTVVV QDSASIYQRG SHAFPRPKGE LKYGWKTWGK NIIFSPSRKN GTFIIDGKSK SECPFNKRVW NSIKVEEFGT GIYQTRVFMR PDYDYSKLCD TGMLGAAAKG DASVHGDPLF WMESQNVNDT WTITSLEALN YRECEWPSSH TLDGSRVIES DMFMPRSLAG PVSRHNHIPG YKVQSSGPWH NTPLEVKREE CPGTHVTVEE TCDDRGKSVR STTDSGKIIP EWCCRSCTMP PVSFWGPDGC WYSMEVRPKH TNEGHLVKSW VVASKGDVDP FSLGLLMLFL CSDMFLMKRF SMRALIAGSI IMLGAMTLGS LTYLDLLRYV VTVGMYMAEA NSGGDVTHLA LIAVFRVRAG FVSVLALKQM WSPRERFVAA CGIVMVQIAL GDIMNTNLME WLNAAGMSIL VIKSIVDPRK CNVVLPLLCL LTPLTTTEIQ RAVMLFCSVV ISVTVLQTDS VSTRKSIPLI ALTICSFFKW TSPFLGLVCY LAFTRIPQRS WPLGETMAAV GLVGVLAGMG LKDMNGMLGP VAVGGVLLIV MSLSGKVDGL VIKKISDIGW DEDAEISGAS HRYDVEQTET GEFKIRNEEP APWTQVMILT IAIVSAAVHP ACLAVVTLGW FFWQKTATRS GVLWDIPTVV PPEEVGYLED GVYTINQKNV LGMAQKGVGV VKDGVFHTMW HVTRGAFLLF EGKRLTPAWA NVKEDLISYG GGWKLEAKWD GTEEVQLIAV APGKNPMNIQ TTPSIFQLTN GKEIGAVNLD FPSGTSGSPI VNKNGEVIGL YGNGILIGNN TYVSAITQSE SSLEQDNDQL QDIPNMLRKG MLTVLDFHPG AGKTRVYLPQ ILKECERLRL KTLVLAPTRV VLSEMKEAMP KMSIKFHTQA FSNTATGKEI IDAMCHATLT HRMLEPTRVT NWEVVIMDEA HFMDPASIAA RGWAAHRSRA RECATIFMSA TPPGTSNEFP ESNGTIEDIR KDIPSEPWTK GHEWILEDRR PTAWFLPSIR VANSIANCLR KAERTVVVLN RKTFEKEYPT IKSKRPDFIL ATDIAEMGAN LRVERVIDCR TAYKPFLVDD GTKVMVKGPL KISASSAAQR RGRVGRDPNR DTDTYVYGDS TTEDNGHYVC WTEGSMLLDN MEIKNGMIAP LYGIEGTKTT TVPGETRLRD EQRKVFRELV KRLDMPVWLS WHVAKAGLKV QDRSWCFDGE DDNTLLNDNG EPIFARSPGG GKKPLKPRWV DTRVCSDNSA LIDFIKFAEG RRSINGLLIG LQGFPKYLSG RMKEAVDTLT VLYNSEAGSR AYKHALAMMP EAVTIFLLIM LTIICTSGIV MFFLAPKGLS RMSMAMMTML VSAYLMSLGG MNPVQVSCVM LVFFIFMVVL IPEPGTQRST YDNQLIYLLV GVMSVILMVT ANEMGMLEKT KRDIFGTTVV EEGKKWTFPE LDLHPGAAWT VYVGLVTLVT PMLHHWIKVD YGNISLSGIT QNAQVLGLMD KGIPFIKMNM SVVILLLSAW NGITLLPLFA GMGAAALHWG FILPGLRAQA AKAAQKRVYH GVAKNPVVDG NPTADIDDAP GMPAMYEKKL ALIILFILAT VNLILTRTPF SIAELVVLGS AALGPLLEGN TNAYWNGPIA VAFTGLMRGN YYATIGLMYN GWLAKQTRRG RAAGVTLGEV WKRQLNMMGK QEFEKYKISD IMEVDRSVAQ RYLKEGRNDV GISVSRGTAK MRWLHERGYV KLSGRVIDLG CGRGGWSYYS AAQKEVMSVK GYTLGINGHE KPVHMQTLGW NIIKFKDKSD VFTMPAEPCE TLLCDIGESS SNFLIEKDRT LKVLENFERW KHVNTENFCV KVLCPYHPDV IEKLERMQLR FGGGLVRIPF SRNSTHEMYY ISGARNNITH MVNTTSRSLL RRMFRPTGKA LVESDVFLPT GTRSVASEAG PVDHDALQLR VDQIKHEYSK TWTIDLNHPY RTWHYLGSYL CKATGSSSSM LNGIVKMLSM PWDKFESVTL LAMTDTTPFG QQRVFKEKVD TRAPSPPPGT RAIMRVVNSW LFKHLAREMR PRICTKEEFI SKVRSHAAIG AYLEEHENWR SASEAVQDPR FWKLVDEERK LHLQGKCRTC VYNMMGKREK KPAEFGKAKG SRAIWYMWLG ARFLEFEALG FLNEDHWVSR GNSGGGVEGT GLQYLGYILK RLGEKPGGRM YADDTAGWDT RITEEDLEDE QEILKYMTKD HKKLAWAVTE LAYKNKVVKV MRPGPGGLTF MDIISRRDQR GSGQVVTYAL NTVTNLKVQL IRMAESEHVI TRHDVESVSP STLRGLEDWL ERFGTDRLSR MAVSGDDCVV KPIDDQFADA LYHLNAMSKI RKDIDDWKPS TGWDSWEAVP FCSHHFHEII LKDGRTIIAP CRDQDELIGR ARVSPGNGWM IRETACLSKA YAQMWLLMYF HRRDLRVMGN AICSAVPVDW VPTGRTTWSI HGKGEWMTTE NMLDVWNRVW IMENPYQADK TPVTEWRDVP YLPKSIDKTC NSLVGTTQRA TWARDVKHTV HRIRKLVGNE KFYDYMSTMD RYRELDEEGP GEILW //