ID E9EGX3_METAQ Unreviewed; 1570 AA. AC E9EGX3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 02-DEC-2020, entry version 77. DE RecName: Full=Pentafunctional AROM polypeptide {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=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=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=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=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143}; GN ORFNames=MAC_09121 {ECO:0000313|EMBL:EFY84835.1}; OS Metarhizium acridum (strain CQMa 102). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium. OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499}; RN [1] {ECO:0000313|EMBL:EFY84835.1, ECO:0000313|Proteomes:UP000002499} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY84835.1, RC ECO:0000313|Proteomes:UP000002499}; RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264; RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X., RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S., RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y., RA Wang C.; RT "Genome sequencing and comparative transcriptomics of the model RT entomopathogenic fungi Metarhizium anisopliae and M. acridum."; RL PLoS Genet. 7:E1001264-E1001264(2011). 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 -!- CATALYTIC ACTIVITY: CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, CC ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1- CC carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, CC ChEBI:CHEBI:145989; EC=2.5.1.19; CC Evidence={ECO:0000256|ARBA:ARBA00001901, ECO:0000256|HAMAP- CC Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; CC -!- CATALYTIC ACTIVITY: CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3- CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); CC Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; CC EC=2.7.1.71; Evidence={ECO:0000256|ARBA:ARBA00000172, CC ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; CC Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 2/7. {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 3/7. {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 4/7. {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 5/7. {ECO:0000256|ARBA:ARBA00004842, ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 6/7. {ECO:0000256|ARBA:ARBA00004811, ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. CC {ECO:0000256|ARBA:ARBA00009948}. CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase CC family. {ECO:0000256|ARBA:ARBA00006477}. CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase CC family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. 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}. CC -!- SIMILARITY: In the N-terminal section; belongs to the dehydroquinate CC synthase family. {ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase CC family. {ECO:0000256|ARBA:ARBA00009349}. CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate CC cyclases superfamily. Dehydroquinate synthase family. CC {ECO:0000256|HAMAP-Rule:MF_03143}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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; GL698603; EFY84835.1; -; Genomic_DNA. DR RefSeq; XP_007815461.1; XM_007817270.1. DR STRING; 92637.XP_007815461.1; -. DR EnsemblFungi; EFY84835; EFY84835; MAC_09121. DR GeneID; 19253432; -. DR KEGG; maw:MAC_09121; -. DR eggNOG; KOG0692; Eukaryota. DR HOGENOM; CLU_001201_1_2_1; -. DR InParanoid; E9EGX3; -. DR OrthoDB; 39786at2759; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000002499; 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_00210; EPSP_synth; 1. DR HAMAP; MF_03143; Pentafunct_AroM; 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; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03143}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; KW Reference proteome {ECO:0000313|Proteomes:UP000002499}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514}. FT DOMAIN 78..356 FT /note="DHQ_synthase" FT /evidence="ECO:0000259|Pfam:PF01761" FT DOMAIN 401..830 FT /note="EPSP_synthase" FT /evidence="ECO:0000259|Pfam:PF00275" FT DOMAIN 1287..1367 FT /note="Shikimate_dh_N" FT /evidence="ECO:0000259|Pfam:PF08501" FT DOMAIN 1404..1485 FT /note="Shikimate_DH" FT /evidence="ECO:0000259|Pfam:PF01488" FT NP_BIND 49..51 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT NP_BIND 84..87 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT NP_BIND 115..117 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT NP_BIND 140..141 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT NP_BIND 868..875 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT REGION 1..382 FT /note="3-dehydroquinate synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT REGION 195..198 FT /note="Substrate binding 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT REGION 262..266 FT /note="Substrate binding 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT REGION 1282..1570 FT /note="Shikimate dehydrogenase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 258 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 273 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 818 FT /note="For EPSP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 1172 FT /note="Proton acceptor; for 3-dehydroquinate dehydratase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 1200 FT /note="Schiff-base intermediate with substrate; for 3- FT dehydroquinate dehydratase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT METAL 195 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT METAL 269 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT METAL 285 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 120 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 131 FT /note="Substrate 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 147 FT /note="Substrate 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 153 FT /note="Substrate 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 162 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 163 FT /note="Substrate 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 191 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 248 FT /note="Substrate 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 269 FT /note="Substrate 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 285 FT /note="Substrate 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 354 FT /note="Substrate 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" SQ SEQUENCE 1570 AA; 170852 MW; C0ACFE1DC33729B5 CRC64; MSTVDMGSPQ KISILGEDSI IADYGLWPEF VATDLVNHVQ SSTYVLITDT NLHDIYVPPF QAWFKSQQLA DNARLLTYAI PPGEASKSRE TKAEIEDWML SQKCTRDTVI IALGGGVIGD MIGYVAATFM RGVRCVQVPT TLLAMVDSSI GGKTAIDTPM GKNLVGAFWQ PKRIYIDLAF MKTLPVREFI NGMAEVIKTA AIWNEDDFTI LEQSAADILA CVRSKGLDRL LPIKDTLTRI VVGSARVKAE VVSADEREGG LRNLLNFGHS IGHAIEAILT PQLLHGEAVA IGMVKEAELA RFLGILRPHA VSRLSKCIAS YGLPTSLKDK RVIKLTAGKK CGIDTLLEKM SVDKKNDGDR KKIVLLSRIG QTFESKASFV ADSDIRTILS ASISVTPGIP NGLKVTVTPP GSKSISNRAL ILAALGSGPC KIKNLLHSDD TEFMLSAIQQ LGGASYSWYD AGEILEVTGN GGKLSASRED LYIGNAGTAS RFLTTVLTLC SSTQESNSTV LTGNTRMKVR PIGPLVDALR QNGAQIEYLE QEKSLPIRVH STGGFQGGMI ELAATVSSQY VSSILMAAPY AKTPVTLRLI GGKPISQPYI DMTISMMSSF GISVTKSTTD MDTYHIPLGA YKNPSEYVIE SDASSATYPL AVAAITGTTC TIPNIGSASL QGDARFAIDV LRPMGCSVQQ DEHSTTVTGP VTGQLKPLPH VDMEPMTDAF LTASVLAAVA NGETQITGIA NQRVKECDRI AAMKEQLAKF GVTCTELDDG IQISGKSLSD IRTPNVGIHC YDDHRVAMSL SVLSVVAPGS TIITERECVG KTWPGWWDTL AQSFKVKLDG PDTTDGDSDI KHASPQRLHA KRSIFVIGMR GAGKTTAGRW MAKLLDWKFI DLDEELERRS GKTIPEIINS PKGWDGFRQD ELDLLQDVAE NMPECHVLSC GGGIVEMPKA RELLQNYCNS GGMVVLVHRN TDQVIEYLMR DTTRPAYTTE IRQVYERRKA WYEVCCNHIY YSPHSAPNTG YNSIPDDFKR FVTSITVGNS SVKNIAKKDE SFFVSLTVPK LNESLHAISS ASVGSDAVEI RVDLLDDWSL EAVTEQLSLL RFVSKLPVIF TVRTVSQGGR FPDAANDHRY DLYRLALRLG VEYLDAEVTS TDEILQELTE SRRNTLIVSS HHDPSGSLSW KNASWVPFYN RALQYGDVIK LVGNAKSIED NFDLANFKSR MMADHKTPII AINMGVAGQL SRILNGFLTP VSHPNLPFKA APGQLSASEI RQGRALLGQI RKREFYLFGS PISQSRSPAL HNALFGITGL PHEYHLHETS SAENLGEVLH SESFGGASVT IPLKRDVMAL VDELTPAAQA IGAVNTIIPL NDDISSNRRR LLGDNTDWKG MVYTLSEAGV ISPVQNESAA VIGSGGTTRA AIYALHFMGF DTIYVVGRDA HKVNTLASEF PRDYNVNAIT EQAQAADLAH SPSVIISTIP ADQPIDDGVK GAVFTLLSLS AVSRVKRVLL EMAYKPHHTQ IVQMAESTST WTVIPGLEVL ASQGWYQFEA WTGIQPLYRQ ARDAVVGSTL //