ID A0A286UDT6_9AGAM Unreviewed; 1761 AA. AC A0A286UDT6; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 22-FEB-2023, entry version 27. 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=PNOK_0623600 {ECO:0000313|EMBL:PAV17750.1}; OS Pyrrhoderma noxium. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Hymenochaetales; Hymenochaetaceae; Pyrrhoderma. OX NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV17750.1, ECO:0000313|Proteomes:UP000217199}; RN [1] {ECO:0000313|Proteomes:UP000217199} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199}; RA Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M., RA Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N., RA Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F., RA Kikuchi T., Tsai I.J.; RT "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its RT Hymenochaetales Members."; RL bioRxiv 0:0-0(2017). CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic CC reactions in prechorismate polyaromatic amino acid biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_03143}. 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}; 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|RuleBase:RU004164}; 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 -!- 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|HAMAP-Rule:MF_03143}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03143}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_03143}; 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}. 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}. 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}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 5/7. {ECO:0000256|HAMAP-Rule:MF_03143}. 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|RuleBase:RU004164}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. CC {ECO:0000256|ARBA:ARBA00009948, ECO:0000256|RuleBase:RU004164}. CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase CC family. {ECO:0000256|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate CC dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143}. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PAV17750.1}. 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; NBII01000006; PAV17750.1; -; Genomic_DNA. DR STRING; 2282107.A0A286UDT6; -. DR OrthoDB; 865at2759; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000217199; Chromosome 6. 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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00502; DHQase_I; 1. DR CDD; cd08195; DHQS; 1. DR CDD; cd01556; EPSP_synthase; 1. DR CDD; cd01065; NAD_bind_Shikimate_DH; 1. DR CDD; cd00464; SK; 1. DR Gene3D; 3.40.50.1970; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1. DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2. DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. 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; IPR046346; Aminiacid_DH-like_N_sf. 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; IPR041121; SDH_C. 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 PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1. DR PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1. DR Pfam; PF01761; DHQ_synthase; 1. DR Pfam; PF01487; DHquinase_I; 1. DR Pfam; PF00275; EPSP_synthase; 1. DR Pfam; PF18317; SDH_C; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR Pfam; PF01202; SKI; 1. DR PRINTS; PR01100; SHIKIMTKNASE. DR SUPFAM; SSF51569; Aldolase; 1. DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1. DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1. DR SUPFAM; SSF55205; EPT/RTPC-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_03143}; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03143}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03143}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03143}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000217199}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03143}. FT DOMAIN 114..400 FT /note="3-dehydroquinate synthase" FT /evidence="ECO:0000259|Pfam:PF01761" FT DOMAIN 453..904 FT /note="Enolpyruvate transferase" FT /evidence="ECO:0000259|Pfam:PF00275" FT DOMAIN 1421..1502 FT /note="Shikimate dehydrogenase substrate binding N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08501" FT DOMAIN 1683..1712 FT /note="SDH C-terminal" FT /evidence="ECO:0000259|Pfam:PF18317" FT REGION 1..426 FT /note="3-dehydroquinate synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT REGION 1416..1761 FT /note="Shikimate dehydrogenase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 302 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 317 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 892 FT /note="For EPSP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 1305 FT /note="Proton acceptor; for 3-dehydroquinate dehydratase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 1333 FT /note="Schiff-base intermediate with substrate; for 3- FT dehydroquinate dehydratase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 119..122 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 150..152 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 155 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 166 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 175..176 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 182 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 188 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 197 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 198 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 215..218 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 226 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 230..233 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 230 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 292 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 306..310 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 313 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 329 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 329 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 398 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 952..959 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" SQ SEQUENCE 1761 AA; 190948 MW; C885679856E34154 CRC64; MMVAASVRTH HQRHCHICVN NAGDTTMAVR ASSESENGIR KVSILGKNSI HCGFELIPYI VSTVLNTLPS STYVLITDTV VASYHLKKFQ DEFKLAIKTA KEGGKSAPRF IHKVIPPGET SKSRQGKADI EDFLLEHKCT RDTVVLALGG GVIGDLVGFV AATFMRGVRF VQIPTTLLAM VDSSVGGKTA IDTPHGKNLI GAFWQPEYIF IDASFLSTLP AREFANGMAE VIKTAAIWDE HEFLKLEERS AEIFAAISGS GNSQGEDVSD EEKVKQQREL LLSVIAGSIG VKAHIVTVDE RETGLRNLVN FGHTIGHAIE AVLTPSLLHG ECVAIGMVLE AEVARAKGVL TQVAVGRITR TLKAYNLPTS LSDARVRAIP ASAGLDVERL LDIMAIDKKN SGKEKKVVLL SRIGKTYEEK ASVVADDIIR RTLCEAAKVI PRPLSSEESC EVTMTTPGSK SISNRALLLA ALSRGTCRLT NLLHSDDTQV MMAALQDLRG ARFSWEDGGE TVVVEGGEGR LSVPDAGKEI YLGNAGTAAR FLTTVCTLVQ DGDLSAAGEN VRETVITGNA RMKQRPVGPL VSALQSNGSS IKYLESQGCL PLSITPGGLY GGHIQLAASI SSQYVSSILL CAPYAQEEVT LELVGGSVIS QPYIDMTLAM MSSFGITATR HKGADGKLLD IYTIPKGCYV SPPEYAIESD ASSATYPLAV AAITGTTCTV LNIGSASLQG DARFAIEVLR PMGCEVIQSE NKTTVRGPPL GKLKAVGEID MEVMTDAFLT ACVLAAVANE PVEEARRLPA EDGRDKLRTT RIIGIANQRV KECNRIKAMI DELAKFGVET TELPDGLEVH GRPLSELVKG ASIHCYDDHR VAMAFSVLGS VVPETMIEEK RCVEKTWPNW WDDLENKLGF KVEGVELPSA PKGSPSLSTS STVVNESDVA AADTDASVVI IGMRGSGKTC IGTLAAQSDW KFVDADHLFE SIYKTTVREF VHSRGWEAFR SSELEVLRSL LTTAEYSKKH VISLGGGIVE TPAARDLIKE YASSYGPVVE VRRETEEIVR YLGAETARPQ YASGEPIADV CKRRAPWFEE CASYLFVNYT GTNHLGPNGK IRDHLSPGAI ALEHRREVER FFGHVTGVKR NTVPLVDAKG ELRRSYFLSL TYPDVTFALD KLETLTVGAD AIELRVDLLR APEYWQDASP YKFEGKGYIP PVSYVLSQLA ALRQATTLPI VFTVRTLAQG GSFPNPEGPS ASNIENAAFE LFELAARMGA EYLDVELVWD ESRVETFLAK WRKRGCKPEV IASWHDWSGN LKWDGNEVET IYERASRIGD IVKIVGKATE LEDNTKLHAF AVTKRESVNN KPLIAINTSP LGQLSRILNV TLTPITHPDL PAAAAPGQLS FAQIQQGLHL HGVIPSKKFY LFGSPISQSP SPTLHNTGFR LLGLPWNYGL LESGVVDERI EEAIRKDDFG GASVTIPLKL DIMKALDQLS EHVKAIGAVN TVAVAYDKTN KKILYGDNTD WLGIKRCIIT QSRGLSTTLN FSTSTGMVIG AGGTARAALY ALHSLGIRTI YLINRTRAKA ELLRDDPTFK GYGIKVLDAN IFSSGKKPEW VSGPPSVIVS TVPGSATTTS LSESKTGASL YLSRELFSVA QGVVVDMAYK PAETPFLSLA GLENPTKWRI VRGVDVLLEQ GYAQFQLWTD RRCPESEVKK AVWEKYAENG SSGSTLVAWE RVGGRYSWLV AGVTAGAIAA TTLSRWVKKG L //