ID V9IS50_9FLAV Unreviewed; 3390 AA. AC V9IS50; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 05-JUN-2019, entry version 40. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00058068}; OS Dengue virus 3. OC Viruses; Riboviria; Flaviviridae; Flavivirus. OX NCBI_TaxID=11069 {ECO:0000313|EMBL:AFK83764.1, ECO:0000313|Proteomes:UP000128110}; RN [1] {ECO:0000313|EMBL:AFK83764.1, ECO:0000313|Proteomes:UP000128110} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D3PY/AS10/03 {ECO:0000313|EMBL:AFK83764.1}; RA Alfonso H.L., Amarilla A.A., Goncaves P.F., Barros M.T., RA Silva E.V.D.A., Nunes M., Vasconcelos P.F.C., Vieira D.S., RA Batista W.C., Bobadilla M.L., Vazquez C., Moran M., Figueiredo L.T.M., RA Aquino V.H.; RT "Molecular characterization of dengue virus type 3 isolated in Brazil RT and Paraguay."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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|SAAS:SAAS01122357}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside CC 5'-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|SAAS:SAAS01122355}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, CC ChEBI:CHEBI:83400; EC=2.7.7.48; CC Evidence={ECO:0000256|SAAS:SAAS01133029}; CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum CC {ECO:0000256|SAAS:SAAS01192355}. 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; JF808129; AFK83764.1; -; Genomic_RNA. DR Proteomes; UP000128110; Genome. DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW. 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:0039503; P:suppression by virus of host innate immune response; 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; 2.60.260.50; -; 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 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; 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; 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:SAAS00291633}; KW ATP-binding {ECO:0000256|SAAS:SAAS00180352}; KW Capsid protein {ECO:0000256|SAAS:SAAS01192515}; KW Complete proteome {ECO:0000313|Proteomes:UP000128110}; 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:SAAS00139783}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|SAAS:SAAS00139991}; KW Helicase {ECO:0000256|SAAS:SAAS00077013}; KW Host membrane {ECO:0000256|SAAS:SAAS00291629}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00291630}; KW Hydrolase {ECO:0000256|SAAS:SAAS00180363}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|SAAS:SAAS00910833}; KW Membrane {ECO:0000256|SAAS:SAAS00291489, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4, KW ECO:0000256|SAAS:SAAS01176813}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00817755}; KW mRNA capping {ECO:0000256|SAAS:SAAS00460999}; KW mRNA processing {ECO:0000256|SAAS:SAAS00460960}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00462767}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00077080}; KW RNA-binding {ECO:0000256|SAAS:SAAS00076745}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00076304}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00463088}; KW Transferase {ECO:0000256|SAAS:SAAS00076372}; KW Transmembrane {ECO:0000256|SAAS:SAAS00291514, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00291474, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|SAAS:SAAS00291492}; KW Viral immunoevasion {ECO:0000256|SAAS:SAAS00910833}; KW Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00139802}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS01123964}; KW Virion {ECO:0000256|SAAS:SAAS00186443}; KW Virus entry into host cell {ECO:0000256|SAAS:SAAS00291600}; KW Zinc {ECO:0000256|PIRSR:PIRSR003817-4}. FT TRANSMEM 46 69 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 722 746 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 752 771 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1157 1175 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1195 1218 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2147 2166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2173 2190 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2196 2213 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 2225 2242 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1344 1473 FLAVIVIRUS_NS2B. {ECO:0000259|PROSITE: FT PS51527}. FT DOMAIN 1474 1651 Peptidase S7. {ECO:0000259|PROSITE: FT PS51528}. FT DOMAIN 1654 1810 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 1820 1986 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT DOMAIN 2492 2753 MRNA cap 0-1 NS5-type MT. FT {ECO:0000259|PROSITE:PS51591}. FT DOMAIN 3017 3167 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50507}. FT ACT_SITE 1524 1524 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT ACT_SITE 1548 1548 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT ACT_SITE 1608 1608 Charge relay system; for serine protease FT NS3 activity. {ECO:0000256|PIRSR: FT PIRSR003817-1}. FT METAL 2927 2927 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 2931 2931 Zinc 1; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR003817-4}. FT METAL 2936 2936 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 2939 2939 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 3202 3202 Zinc 2; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR003817-4}. FT METAL 3218 3218 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT METAL 3337 3337 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817- FT 4}. FT BINDING 2546 2546 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT BINDING 2576 2576 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2577 2577 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2594 2594 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT BINDING 2595 2595 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2621 2621 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR003817-2}. FT BINDING 2622 2622 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR003817- FT 2}. FT BINDING 2708 2708 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 463 563 {ECO:0000256|PIRSR:PIRSR003817-3}. FT DISULFID 580 611 {ECO:0000256|PIRSR:PIRSR003817-3}. SQ SEQUENCE 3390 AA; 377814 MW; 594D3241159AD3DB CRC64; MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSKGLLNG QGPMKLVMAF IAFLRFLAIP PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK TSLCLMMILP AALAFHLTSR DGEPRMIVGK NERGKSLLFK TASGINMCTL IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC WCNLTSTWVT YGTCNQAGEH RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW ALRHPGFTIL ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT DSRCPTQGEA VLPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ CLEPIEGKVV QYENLKYTVI ITVHTGDQHQ VGNETQGVTA EITPQASTTE AILPEYGTLG LECSPRTGLD FNEMILLTMK NKAWMVHRQW FFDLPLPWTS GATTETPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT ALTGATEIQN SGGTSIFAGH LKCRLKMDKL ELKGMSYAMC TNTFVLKKEV SETQHGTILI KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP FGESNIVIGI GDNALKINWY KKGSSIGKMF EATARGARRM AILGDTAWDF GSVGGVLNSL GKMVHQIFGS AYTALFSGVS WVMKIGIGVL LTWIGLNSKN TSMSFSCIAI GIITLYLGAV VQADMGCVIN WKGKELKCGS GIFVTNEVHT WTEQYKFQAD SPKRLATAIA GAWENGVCGI RSTTRMENLL WKQIANELNY ILWENNIKLT VVVGDITGVL EQGKRTLTPQ PMELKYSWKT WGKAKIVTAE TQNSSFIIDG PNTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ LCDHRLMSAA VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK SHTLWSNGVL ESDMIIPKSL AGPISQHNHR PGYHTQTAGP WHLGKLELDF NYCEGTTVVI TENCGTRGPS LRTTTVSGKL IHEWCCRSCT LPPLRYMGED GCWYGMEIRP ISEKEENMVK SLVSAGSGKV DNCTMGVLCL AILFEDVMRG KFGKKHMIAG VFFTFVLLLS GQITWRDMAH TLIMIGSNAS DRMGMGVTYL ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMATTLQ LPEDIEQMAN GIALGLMALK LITQFETYQL WTALISLTCS NTMFTLTVAW RTATLILAGV SLLPVCQSSS MRKTDWLPMA VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL LIACYVITGT SADLTVEKAA DITWEEEAEQ TGVSHNLMTT VDDDGTMRIK DDETENILTV LLKTALTIVS GVFPYSIPAT LLVWHTWQKQ TQRSGVLWDV PSPPETQKAE QEEGVYRIKQ QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTYNGKRLEP NWASVKKDLI SYGGGWRLSA QWQKGEEVQV IAVEPGKNPK NFQTMPGTFQ TTTGEIGAIA LDFKPGTSGS PIINREGKVV GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA IVREAIKRRL RTLILAPTRV VAAEMEEALK GLPIRYQTTA TKSEHTGREI VDLMCHATFT MRLLSPVRVP TYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP QSNAPIQDEE RDIPERSWNS GNEWITDFAG KTVWFVPSIK AGNDIANCLR KNGKKVIQLS RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FKADRVIDPR RCLKPVILTD GPERVILAGP MPVTAASAAQ RRGRVGRNPQ KENDQYIFTG QPLNNDEDHA HWTEAKMLLD NINTPEGIIP ALFEPEREKS AAIDGEYRLK GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG QRNNQILEEN MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL GLMILLTGGA MLFLISGKGI GKTSIGLICV IASSGMLWMA EIPLQWIASA IVLEFFMMVL LIPEPEKQRT PQDNQLAYVV IGILTLAAII AANEMGLLET TKRDLGMSKE PGVVSPTSYL DVDLHPASAW TLYAVATTVI TPMLRHTIEN STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC YSQVNPLTLT AAVLLLITHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEALTLAT GPITTLWEGS PGKFWNTTIA VSMANIFRGS YLAGAGLAFS IMKSVGTGKR GTGSQGETLG EKWKKKLNQL SRKEFDLYKK SGITEVDRTE AKEGLKRGEI THHAVSRGSA KLQWFVERNM VIPEGRVIDL GCGRGGWSYY CAGLKKVTEV RGYTKGGPGH EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES SPSPTVEESR TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS RNSTHEMYWI SNGTGNIVAS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG TRHVNAEPET PNMDVIGERI KRTKEEHNST WHYDDENPYK TWAYHGSYEV KATGSASSMI NGVVKLLTKP WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT RTPRSMPGTR RVMGITAEWL WRTLGRNKKP RLCTREEFTK KVRTNAAMGA VFTEENQWDS AKAAVEDEDF WKLVDREREL HKLGKCGSCV YNMMGKREKK LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KITQQMDPEH RQLANAIFKL TYQNKVVKVQ RPTPTGTVMD IISRKDQRGS GQVGTYGLNT FTNMEAQLIR QMEGEGVLSK ADLENPHLPE KKITQWLETK GVERLKRMAI SGDDCVVKPI DDRFANALLA LNDMGKVRKD IPQWQPSKGW HDWQQVPFCS HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE TACLGKAYAQ MWSLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML TVWNRVWIED NPWMEDKTPV TTWENVPYLG KREDQWCGSL IGLTSRATWA QNIPTAIQQV RSLIGNEEFL DYMPSMKRFR KEEESEGAIW //