ID A0A7T3R0P4_9FLAV Unreviewed; 3392 AA. AC A0A7T3R0P4; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. DE RecName: Full=Core protein {ECO:0000256|ARBA:ARBA00019458}; DE EC=3.4.21.91 {ECO:0000256|ARBA:ARBA00013228}; DE EC=3.6.1.15 {ECO:0000256|ARBA:ARBA00012445}; DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552}; DE AltName: Full=Envelope protein E {ECO:0000256|ARBA:ARBA00017531}; DE AltName: Full=Flavivirin protease NS2B regulatory subunit {ECO:0000256|ARBA:ARBA00013313}; DE AltName: Full=Flavivirin protease NS3 catalytic subunit {ECO:0000256|ARBA:ARBA00018941}; DE AltName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; DE AltName: Full=Matrix protein {ECO:0000256|ARBA:ARBA00017678}; DE AltName: Full=Non-structural protein 1 {ECO:0000256|ARBA:ARBA00016002}; DE AltName: Full=Non-structural protein 2A {ECO:0000256|ARBA:ARBA00019777, ECO:0000256|ARBA:ARBA00019791}; DE AltName: Full=Non-structural protein 2B {ECO:0000256|ARBA:ARBA00019779}; DE AltName: Full=Non-structural protein 3 {ECO:0000256|ARBA:ARBA00016254}; DE AltName: Full=Non-structural protein 4A {ECO:0000256|ARBA:ARBA00019785}; DE AltName: Full=Non-structural protein 4B {ECO:0000256|ARBA:ARBA00019812}; DE AltName: Full=Non-structural protein 5 {ECO:0000256|ARBA:ARBA00016251}; DE AltName: Full=Peptide 2k {ECO:0000256|ARBA:ARBA00018340}; DE AltName: Full=Peptide pr {ECO:0000256|ARBA:ARBA00017165}; DE AltName: Full=Protein prM {ECO:0000256|ARBA:ARBA00013848}; DE AltName: Full=RNA-directed RNA polymerase NS5 {ECO:0000256|ARBA:ARBA00016595}; DE AltName: Full=Serine protease NS3 {ECO:0000256|ARBA:ARBA00016200}; DE AltName: Full=Serine protease subunit NS2B {ECO:0000256|ARBA:ARBA00015417}; DE AltName: Full=Small envelope protein M {ECO:0000256|ARBA:ARBA00018173}; GN Name=POLY {ECO:0000313|EMBL:QPZ88406.1}; OS Dengue virus 1. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Flavivirus. OX NCBI_TaxID=11053 {ECO:0000313|EMBL:QPZ88406.1}; RN [1] {ECO:0000313|EMBL:QPZ88406.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DENV-1/AP/BR/460 {ECO:0000313|EMBL:QPZ88406.1}; RA Ribeiro G., Gill D., Da Costa A.C., Sabino E., Leal E.; RT "Molecular Epidemiological Context of 15 Dengue Virus Serotype 1 Genotype V RT Genomes from the Brazilian State of Amapa, 2014-2015."; RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the viral RNA replication complex that functions CC in virion assembly and antagonizes the host immune response. CC {ECO:0000256|ARBA:ARBA00024317}. CC -!- FUNCTION: Functions as a signal peptide for NS4B and is required for CC the interferon antagonism activity of the latter. CC {ECO:0000256|ARBA:ARBA00003504}. 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|ARBA:ARBA00001556}; 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|ARBA:ARBA00001491}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004477}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004397}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004367}; Lumenal side CC {ECO:0000256|ARBA:ARBA00004367}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004461}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004461}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004461}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00023443}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00023443}; Lumenal side CC {ECO:0000256|ARBA:ARBA00023443}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Membrane CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004287}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. Secreted CC {ECO:0000256|ARBA:ARBA00004613}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004385}. 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; MW377902; QPZ88406.1; -; Genomic_RNA. DR CDD; cd20761; capping_2-OMTase_Flaviviridae; 1. 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; 2.40.10.10; -; 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 Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR043502; DNA/RNA_pol_sf. 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; IPR043504; Peptidase_S1_PA_chymotrypsin. 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; SSF56672; SSF56672; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Capsid protein {ECO:0000256|ARBA:ARBA00022561}; KW Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|ARBA:ARBA00022570}; KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|ARBA:ARBA00022510}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|ARBA:ARBA00022506}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184, KW ECO:0000256|PROSITE-ProRule:PRU00859}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|PROSITE- KW ProRule:PRU00859}; Host nucleus {ECO:0000256|ARBA:ARBA00022562}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|ARBA:ARBA00022632}; KW Inhibition of host interferon signaling pathway by virus KW {ECO:0000256|ARBA:ARBA00022830}; KW Inhibition of host MAVS by virus {ECO:0000256|ARBA:ARBA00022986}; KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022986}; KW Inhibition of host STAT2 by virus {ECO:0000256|ARBA:ARBA00022883}; KW Inhibition of host TYK2 by virus {ECO:0000256|ARBA:ARBA00022923}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE- KW ProRule:PRU00859}; Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603}; KW mRNA capping {ECO:0000256|ARBA:ARBA00023042}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE- KW ProRule:PRU00859}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE- KW ProRule:PRU00859}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280}; KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}; KW Virion {ECO:0000256|ARBA:ARBA00022844}; KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022570}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}. FT TRANSMEM 101..117 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 724..748 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 755..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 1822..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" SQ SEQUENCE 3392 AA; 378877 MW; 6D3ED84726CC87D5 CRC64; MNNQRKKTGR PSFNMLKRAR NRVSTGSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP PTAGILARWS SFKKNGAIKV LRGFKKEISS MLNIMNRRKR SVTMLLMLLP TALAFHLTTR GGEPHMIVSK QERGKSLLFK TSVGVNMCTL IAMDLGELCE DTMTYKCPRI TEAEPDDVDC WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQRVETW ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW VDVVLEHGSC VTTMAKNKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSLLTCAKFK CVTKLEGKIV QYENLKYSVI VTVHTGDQHQ VGNETTEHGT IATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT MKEKSWLVHK QWFLDLPLPW TSGASTSQEA WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV LVQVKYEGTD APCKIPFSTQ DEKGVTQNGR LITANPIVTD KEKPVNIETE PPFGESYIVV GAGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW DFGSIGGVFT SVGKLVHQVF GTAYGVLFSG VSWTMKIGIG ILLTWLGLNS RSTSLSMTCI AVGMVTLYLG VMVQADSGCV INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGKAWEEGVC GIRSATRLEN IMWKQISNEL NHILLENDMK FTVVVGDANG ILAQGKKMIR PQPMEHKYSW KRWGKAKIIG ADIQNTTFII DGPDTPECPD GQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQMCDHRLMS AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCTW PKSHTLWSNG VLESEMVIPK IYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGNRG PSLRTTTVTG KIIHEWCCRS CTLPPLRFRG EDGCWYGMEI RPVKEKEENL VRSMVSAGSG EVDSFSLGIL CVSIMIEEVM RSRWSRKMLM TGTLAVFLLL IMGQLTWNDL IRLCIMVGAN ASDRMGMGTT HLALMATFKM RPMFAVGLLF RRLTSREVLL LTIGLSLMAS MELPNSLEEL GDGLAMGIMM LKLLTEFQPH QLWTTLLSLT FVKTTLSLDY AWKTTAMTLS IVSLFPLCLS TTSQKTTWLP VLLGSFGCKP LTMFLITENK IWGRKSWPLN EGIMAIGIVS ILLSSLLKND VPLAGPLIAG GMLIACYVIS GSSADLSLEK AAEVSWEQEA EHSGASHNIL VEVQDDGTMK IKDEERDDTL TILLKATLLA VSGVYPMSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI LQRGLVGRSQ VGVGVFQDGV FHTMWHVTWG GGRMEPWKRL EPNWASVKKD LISYGGGWRF QGSWNTGEEV QVIAVGPGKN PKNVQTTPGT FKTPEGEVGA IALDFKPGTS GSPIVNREGK IVGLYGNGVV TTSGTYVSAI AQAKASQEGP LPEIEDEVFK KRNLTIMDLH PGSGKTRRYL PAIVREAIKR KLRTLILAPT RVVASEMAEA LKGMPIRYQT TAVKSETTGR EIVDLMCHAT FTMRLLSPVR VPNYNMIIMD EAHFTDPASI AARGYISTRV GMGEAAAIFM TATPPGSVEA FPRSNAVIQD EERDIPERSW 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 LTLRAQNALD NLVMLHNSEQ GGKAYRHAME ELPDTIETLM LLALIAVLTG GVTLFFLSGK GLGKTSIGLL CVTASSALLW MASVEPHWIA ASIILEFFLM VLLIPEPDRQ RTPQDNQLAY VVIGLLFMIL TVAANEMGLL ETTKKDLGIG YVAAENHQHA TMLDVDLRPA SAWTLYAVAT TVITPMMRHT IENTTANISL TAIANQAAIL MGLDKGWPIS KMDIGVPLLA LGCYSQVNPL TLTAAVLMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW EGSPGKFWNT TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE TLGEKWKRQL NQLSKSEFNT YKRSGIMEVD RSEAKEGLKR GETTKHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW SYYCAGLKRV TEVKGYTKGG PGHEEPIPMA TYGWNLVKLH SGKDVFFMPP EKCDTLLCDI GESSPNPTIE EGRTLRVLKM VEPWLKGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVAVE PEVANLDIIG QRIENIKNEH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVRLL TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPRAKR GTTQIMEVTA KWLWGFLSRN KKPRICTREE FTRKVRSNAA IGAVFVNENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA TCVYNMMGKS LRPLEKFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLH NEAKITDIME PEHALLATSI FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEVQ LIRQMESEGI FLPSELETPN LAGRVLDWLE KHGAERLKRM AISGDDCVVK PIDDRFATAL TALNDMGRVG KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED MLSVWNRVWI EENPWMEDKT HVSSWEEVPY LGKREDQWCG SLIGLTARAT WATNIQVAIN QVRRLIGNEN YLDYMTSMKR FKNESDPEGA LW //