ID A0A0D0AM01_9HOMO Unreviewed; 1590 AA. AC A0A0D0AM01; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 22-NOV-2017, entry version 26. DE RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_03143}; DE Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_03143}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_03143}; DE Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_03143}; DE Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_03143}; DE Short=DHQS {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_03143}; DE Short=SK {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143}; GN ORFNames=CY34DRAFT_804457 {ECO:0000313|EMBL:KIK42886.1}; OS Suillus luteus UH-Slu-Lm8-n1. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Agaricomycetidae; Boletales; Suillineae; Suillaceae; OC Suillus. OX NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK42886.1, ECO:0000313|Proteomes:UP000054485}; RN [1] {ECO:0000313|EMBL:KIK42886.1, ECO:0000313|Proteomes:UP000054485} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK42886.1, RC ECO:0000313|Proteomes:UP000054485}; RG DOE Joint Genome Institute; RA Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G., RA Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., RA LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., RA Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., RA Martin F., Nordberg H.P., Cantor M.N., Hua S.X.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000054485} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485}; RG DOE Joint Genome Institute; RG Mycorrhizal Genomics Consortium; RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W., RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., RA Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.; RT "Evolutionary Origins and Diversification of the Mycorrhizal RT Mutualists."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic CC reactions in prechorismate polyaromatic amino acid biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514, CC ECO:0000256|SAAS:SAAS00712173}. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712185}. CC -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate CC = 3-dehydroquinate + phosphate. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|SAAS:SAAS00858949}. CC -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00629607}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712174}. CC -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate + CC NADPH. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|SAAS:SAAS00712180}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858971}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 3/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712175}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712177}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629576}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712169}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712187}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629599}. CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase CC family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712186}. CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase CC family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712182}. CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3- CC dehydroquinase family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712184}. CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate CC dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712181}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC dehydroquinate synthase family. {ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar CC phosphate cyclases superfamily. Dehydroquinate synthase family. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00858969}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03143}. 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; KN835227; KIK42886.1; -; Genomic_DNA. DR EnsemblFungi; KIK42886; KIK42886; CY34DRAFT_804457. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000054485; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00502; DHQase_I; 1. DR CDD; cd01556; EPSP_synthase; 1. DR CDD; cd00464; SK; 1. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.65.10.10; -; 2. DR HAMAP; MF_00110; DHQ_synthase; 1. DR HAMAP; MF_00210; EPSP_synth; 1. DR HAMAP; MF_03143; Pentafunct_AroM; 1. DR HAMAP; MF_00222; Shikimate_DH_AroE; 1. DR HAMAP; MF_00109; Shikimate_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016037; DHQ_synth_AroB. DR InterPro; IPR030960; DHQS/DOIS. DR InterPro; IPR001381; DHquinase_I. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf. DR InterPro; IPR006264; EPSP_synthase. DR InterPro; IPR023193; EPSP_synthase_CS. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008289; Pentafunct_AroM. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR InterPro; IPR031322; Shikimate/glucono_kinase. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR InterPro; IPR010110; Shikimate_DH_AroM-type. DR InterPro; IPR022893; Shikimate_DH_fam. DR InterPro; IPR000623; Shikimate_kinase/TSH1. DR InterPro; IPR023000; Shikimate_kinase_CS. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR Pfam; PF01761; DHQ_synthase; 1. DR Pfam; PF01487; DHquinase_I; 1. DR Pfam; PF00275; EPSP_synthase; 1. DR Pfam; PF01488; Shikimate_DH; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR Pfam; PF01202; SKI; 1. DR PIRSF; PIRSF000514; Pentafunct_AroM; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF55205; SSF55205; 1. DR TIGRFAMs; TIGR01356; aroA; 1. DR TIGRFAMs; TIGR01357; aroB; 1. DR TIGRFAMs; TIGR01093; aroD; 1. DR TIGRFAMs; TIGR01809; Shik-DH-AROM; 1. DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1. DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1. DR PROSITE; PS01128; SHIKIMATE_KINASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858961}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00629580}; KW Complete proteome {ECO:0000313|Proteomes:UP000054485}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629621}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00629772}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00727050}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00629584}; KW NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00858973}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172}; KW Reference proteome {ECO:0000313|Proteomes:UP000054485}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629569}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00712179}. FT DOMAIN 80 363 DHQ_synthase. {ECO:0000259|Pfam:PF01761}. FT DOMAIN 417 845 EPSP_synthase. {ECO:0000259|Pfam: FT PF00275}. FT DOMAIN 1307 1388 Shikimate_dh_N. {ECO:0000259|Pfam: FT PF08501}. FT DOMAIN 1424 1476 Shikimate_DH. {ECO:0000259|Pfam:PF01488}. FT NP_BIND 46 48 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 84 87 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 115 117 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 140 141 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 180 183 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 884 891 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}. FT REGION 1 389 3-dehydroquinate synthase. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT REGION 195 198 Substrate binding 2. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT REGION 269 273 Substrate binding 2. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT REGION 1302 1590 Shikimate dehydrogenase. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT ACT_SITE 265 265 Proton acceptor; for 3-dehydroquinate FT synthase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 280 280 Proton acceptor; for 3-dehydroquinate FT synthase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 833 833 For EPSP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT ACT_SITE 1191 1191 Proton acceptor; for 3-dehydroquinate FT dehydratase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 1219 1219 Schiff-base intermediate with substrate; FT for 3-dehydroquinate dehydratase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 195 195 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 276 276 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 292 292 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 120 120 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 131 131 Substrate 1. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 147 147 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 153 153 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 162 162 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 163 163 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 191 191 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 255 255 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 276 276 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 292 292 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 361 361 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. SQ SEQUENCE 1590 AA; 170223 MW; EF30A9B7658682A2 CRC64; MDTVPDILKV SILGRESIHC GFHLIPYIAH TVLTTLPASV YVLVTDTNVA QFYLSAFEKA FSAEISKLSS AKPRFLSRVI FPGETTKSRE GKADIEDFLL LERCTRDTVI LALGGGVIGD LVGFVAATFM RGVRFVQIPT TLLAMVDSSV GGKTAIDTPA GKNLIGAFWQ PEYIFIDAAF LESLPEREFS NGMAEVVKTA AIWDETEFTS LESNAQLIYN AIRTPSTGNA GRHISTRSTS QSLLLSVIRG SIYVKSHIVT IDERETGLRN LVNFGHTIGH AIEAVLTPHM LHGECVSIGM IFEAEVSRAM GILKQVAVGR LVRCLRAYGL PVSLADQRVT RCPGARGLGV DRLLDIMRVD KKNSGPQKKV VILSSIGATY EQKATAVDDA LIAKVLSEAV TVKVDLSTTS GIQHVKMATP GSKSISNRAL VLAALAQGTC RLKNLLHSDD TQVMMAALQE LKGASFAWED GGETLVVTGG AGSLEVPTAG KEIYLGNAGT AARFLTTVCS LVSPSAAPDA GTATIITGNA RMKQRPIGPL VDALRANGSE ITYNESEGCL PLSIAPKGLQ GGVIRLAASV SSQYVSSILL CAPYAREAVT LELVGGAVIS QPYIDMTIAM MRTFGVLVTR DPGTDVYRIP QGTYVNPAQY AIESDASSAT YPLAIAAITG TKCTLENIGS ESLQGDARFA VDVLARMGCE VVQTANETTV TGPKRGELKA IGEVDMEPMT DAFLTACALA AVAQGGEGNT TRILGIANQR VKECNRIKAM IDQLAKFGVQ TKELDDGLEV YGCPFNTLTR GASVHCYDDH RVAMAFSVLG TVVPDTIIEE KRCVEKTWPN WWDDLENKIG LKVGGIELPR AEGSNTATSG TPSPAASASV ILIGMRGSGK SHIGKLASAA LSRQFIDADI YFETKHNIGV REFVSVNGWP AFRAAETELL KEIIQKAGTG HVISMGGGIV ETPQARDVLK DYAKTGPVVH VLRDIEEIVN YLGDETARPA YGEPITEVFK RREPWFIECA NYDFVNHITV GDSEATNSEI SRFFKHITGQ PNLSENVAAG KRSYFVALTY PDVIPALRHM SDLTTGVDAV ELRVDLLRAH NALGAIPSQA YVTAQLAALR RATSLPIIFT VRTISQGGAF PDNSERDAFE LLALALRLGV EYIDVEISAS ERLITELAAR KGFSQIIASW HDWSGKMKWN EDVVRSKYTL ASRFGDIVKI VGKADTLQDN FVLHDFVAKA NLQRGAKPII AINMGVEGQM SRILNATLSP VTHPLLPSKA APGQLSFAQI QKALNLLGQL PAKRYFLFGN PIAHSMSPTL HNTGFEVLGL PHTYELLETA SVGEELKATL AAPDFGGASV TIPFKLDVIP LLDKLSPAAE AIGAVNTIIP VIEEGNRILY GDNTDWLGIR ESIRSRAPSI GAPAAALVIG AGGTARAAIF ALQSLGAQRI YLFNRTASKA QALVDAFPDA PVKLIETLDV WPAEGPAPTV IVSTVPASAT TTDGTSPGAV LLPLALFDAT ANGVVVDMAY KPAETPLLTL AKSAAPKWAR VMGVEVLLEQ GYVQFETWTG RRCPKHVVSK SVLEKYFAAA //