ID SYI_THET8 Reviewed; 1043 AA. AC P56690; Q5SJE7; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 27-MAR-2024, entry version 153. DE RecName: Full=Isoleucine--tRNA ligase; DE EC=6.1.1.5; DE AltName: Full=Isoleucyl-tRNA synthetase; DE Short=IleRS; GN Name=ileS; OrderedLocusNames=TTHA1067; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007744|PDB:1ILE} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-821 IN COMPLEX WITH ZINC IONS, RP AND COFACTOR. RX PubMed=9554847; DOI=10.1126/science.280.5363.578; RA Nureki O., Vassylyev D.G., Tateno M., Shimada A., Nakama T., Fukai S., RA Konno M., Hendrickson T.L., Schimmel P., Yokoyama S.; RT "Enzyme structure with two catalytic sites for double-sieve selection of RT substrate."; RL Science 280:578-582(1998). RN [3] {ECO:0007744|PDB:1JZQ, ECO:0007744|PDB:1JZS} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-821 IN COMPLEXES WITH ZINC IONS; RP ILE-ADENYLATE ANALOG AND MUPIROCIN, AND COFACTOR. RX PubMed=11584022; DOI=10.1074/jbc.m109089200; RA Nakama T., Nureki O., Yokoyama S.; RT "Structural basis for the recognition of isoleucyl-adenylate and an RT antibiotic, mupirocin, by isoleucyl-tRNA synthetase."; RL J. Biol. Chem. 276:47387-47393(2001). RN [4] {ECO:0007744|PDB:1UDZ, ECO:0007744|PDB:1UE0} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH VAL, RP AND MUTAGENESIS OF THR-228; THR-229; THR-230; THR-233 AND ASP-328. RX PubMed=14672940; DOI=10.1074/jbc.m312830200; RA Fukunaga R., Fukai S., Ishitani R., Nureki O., Yokoyama S.; RT "Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl- RT tRNA synthetase and its complex with L-valine."; RL J. Biol. Chem. 279:8396-8402(2004). CC -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS CC can inadvertently accommodate and process structurally similar amino CC acids such as valine, to avoid such errors it has two additional CC distinct tRNA(Ile)-dependent editing activities. One activity is CC designated as 'pretransfer' editing and involves the hydrolysis of CC activated Val-AMP. The other activity is designated 'posttransfer' CC editing and involves deacylation of mischarged Val-tRNA(Ile) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L- CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, CC ChEBI:CHEBI:456215; EC=6.1.1.5; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000305|PubMed:11584022, ECO:0000305|PubMed:9554847}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:11584022, CC ECO:0000269|PubMed:9554847}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11584022, CC ECO:0000269|PubMed:14672940, ECO:0000269|PubMed:9554847}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and CC one for editing. The misactivated valine is translocated from the CC active site to the editing site, which sterically excludes the CC correctly activated isoleucine. The single editing site contains two CC valyl binding pockets, one specific for each substrate (Val-AMP or Val- CC tRNA(Ile)) (By similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: The ATP consumption with regard to L-valine is CC nonproductive and is solely for substrate selection, which demonstrates CC the high cost of accuracy. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC IleS type 2 subfamily. {ECO:0000305}. 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; AP008226; BAD70890.1; -; Genomic_DNA. DR RefSeq; WP_011228416.1; NC_006461.1. DR RefSeq; YP_144333.1; NC_006461.1. DR PDB; 1ILE; X-ray; 2.50 A; A=1-821. DR PDB; 1JZQ; X-ray; 3.00 A; A=1-821. DR PDB; 1JZS; X-ray; 2.50 A; A=1-821. DR PDB; 1UDZ; X-ray; 1.80 A; A/B=201-381. DR PDB; 1UE0; X-ray; 2.00 A; A/B=201-381. DR PDB; 1WK8; X-ray; 1.70 A; A/B=196-388. DR PDB; 1WNY; X-ray; 1.60 A; A/B=201-385. DR PDB; 1WNZ; X-ray; 1.70 A; A=201-385. DR PDBsum; 1ILE; -. DR PDBsum; 1JZQ; -. DR PDBsum; 1JZS; -. DR PDBsum; 1UDZ; -. DR PDBsum; 1UE0; -. DR PDBsum; 1WK8; -. DR PDBsum; 1WNY; -. DR PDBsum; 1WNZ; -. DR AlphaFoldDB; P56690; -. DR SMR; P56690; -. DR ChEMBL; CHEMBL3879837; -. DR DrugBank; DB01755; N-[Isoleucinyl]-N'-[adenosyl]-diaminosufone. DR EnsemblBacteria; BAD70890; BAD70890; BAD70890. DR GeneID; 3168241; -. DR KEGG; ttj:TTHA1067; -. DR PATRIC; fig|300852.9.peg.1047; -. DR eggNOG; COG0060; Bacteria. DR HOGENOM; CLU_001493_1_1_0; -. DR PhylomeDB; P56690; -. DR BRENDA; 6.1.1.5; 2305. DR EvolutionaryTrace; P56690; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1. DR CDD; cd00818; IleRS_core; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR033709; Anticodon_Ile_ABEc. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023586; Ile-tRNA-ligase_type2. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR NCBIfam; TIGR00392; ileS; 1. DR PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1. DR PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF19302; DUF5915; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR PRINTS; PR00984; TRNASYNTHILE. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1..1043 FT /note="Isoleucine--tRNA ligase" FT /id="PRO_0000098567" FT MOTIF 47..57 FT /note="'HIGH' region" FT MOTIF 591..595 FT /note="'KMSKS' region" FT BINDING 46 FT /ligand="L-isoleucyl-5'-AMP" FT /ligand_id="ChEBI:CHEBI:178002" FT /evidence="ECO:0000305|PubMed:11584022, FT ECO:0007744|PDB:1JZQ" FT BINDING 57 FT /ligand="L-isoleucyl-5'-AMP" FT /ligand_id="ChEBI:CHEBI:178002" FT /evidence="ECO:0000305|PubMed:11584022, FT ECO:0007744|PDB:1JZQ" FT BINDING 181 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, FT ECO:0007744|PDB:1JZS" FT BINDING 184 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, FT ECO:0007744|PDB:1JZS" FT BINDING 319 FT /ligand="L-valine" FT /ligand_id="ChEBI:CHEBI:57762" FT /evidence="ECO:0000269|PubMed:14672940" FT BINDING 328 FT /ligand="L-valine" FT /ligand_id="ChEBI:CHEBI:57762" FT /evidence="ECO:0000269|PubMed:14672940" FT BINDING 389 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, FT ECO:0007744|PDB:1JZS" FT BINDING 392 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, FT ECO:0007744|PDB:1JZS" FT BINDING 461 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ" FT BINDING 464 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007744|PDB:1ILE" FT BINDING 502 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, FT ECO:0007744|PDB:1JZS" FT BINDING 504 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, FT ECO:0007744|PDB:1JZS" FT BINDING 550 FT /ligand="L-isoleucyl-5'-AMP" FT /ligand_id="ChEBI:CHEBI:178002" FT /evidence="ECO:0000305|PubMed:11584022, FT ECO:0007744|PDB:1JZQ" FT BINDING 551 FT /ligand="L-isoleucyl-5'-AMP" FT /ligand_id="ChEBI:CHEBI:178002" FT /evidence="ECO:0000305|PubMed:11584022, FT ECO:0007744|PDB:1JZQ" FT BINDING 553 FT /ligand="L-isoleucyl-5'-AMP" FT /ligand_id="ChEBI:CHEBI:178002" FT /evidence="ECO:0000305|PubMed:11584022, FT ECO:0007744|PDB:1JZQ" FT BINDING 554 FT /ligand="L-isoleucyl-5'-AMP" FT /ligand_id="ChEBI:CHEBI:178002" FT /evidence="ECO:0000305|PubMed:11584022, FT ECO:0007744|PDB:1JZQ" FT BINDING 581 FT /ligand="L-isoleucyl-5'-AMP" FT /ligand_id="ChEBI:CHEBI:178002" FT /evidence="ECO:0000305|PubMed:11584022, FT ECO:0007744|PDB:1JZQ" FT BINDING 594 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT MUTAGEN 228 FT /note="T->A: Has some defects in posttransfer editing FT activity." FT /evidence="ECO:0000269|PubMed:14672940" FT MUTAGEN 229 FT /note="T->A: Has some defects in posttransfer editing FT activity." FT /evidence="ECO:0000269|PubMed:14672940" FT MUTAGEN 230 FT /note="T->A: No change in posttransfer editing activity." FT /evidence="ECO:0000269|PubMed:14672940" FT MUTAGEN 233 FT /note="T->A: No change in posttransfer editing activity." FT /evidence="ECO:0000269|PubMed:14672940" FT MUTAGEN 328 FT /note="D->A: Has some defects in posttransfer editing FT activity." FT /evidence="ECO:0000269|PubMed:14672940" FT HELIX 10..23 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 26..33 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 34..36 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 57..73 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 81..84 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 88..98 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 104..110 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 112..122 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 123..126 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 127..130 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 133..136 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 142..148 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 152..167 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 171..174 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 182..185 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 190..195 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 204..212 FT /evidence="ECO:0007829|PDB:1WNY" FT HELIX 214..217 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 220..229 FT /evidence="ECO:0007829|PDB:1WNY" FT HELIX 231..236 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 239..242 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 246..253 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 256..261 FT /evidence="ECO:0007829|PDB:1WNY" FT HELIX 262..269 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 275..280 FT /evidence="ECO:0007829|PDB:1WNY" FT HELIX 281..284 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 302..305 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 311..314 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 318..320 FT /evidence="ECO:0007829|PDB:1WNY" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:1WNY" FT HELIX 326..335 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:1WNY" FT HELIX 352..354 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 359..372 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 376..380 FT /evidence="ECO:0007829|PDB:1WNY" FT STRAND 390..392 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 397..400 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 403..406 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 408..411 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 412..421 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 422..426 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 430..434 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 435..439 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:1JZS" FT STRAND 451..453 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 458..465 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 473..479 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 492..495 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 499..501 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 505..510 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 517..527 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 528..533 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 536..542 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 543..551 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 552..556 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 558..570 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 574..581 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 587..589 FT /evidence="ECO:0007829|PDB:1JZS" FT TURN 594..597 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 602..606 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 607..609 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 611..621 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 624..626 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 632..641 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 643..660 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 670..672 FT /evidence="ECO:0007829|PDB:1JZS" FT HELIX 675..696 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 700..714 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 717..719 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 720..728 FT /evidence="ECO:0007829|PDB:1ILE" FT STRAND 733..735 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 738..754 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 755..757 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 761..769 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 770..773 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 774..776 FT /evidence="ECO:0007829|PDB:1JZQ" FT HELIX 781..783 FT /evidence="ECO:0007829|PDB:1ILE" FT TURN 791..793 FT /evidence="ECO:0007829|PDB:1ILE" FT HELIX 796..812 FT /evidence="ECO:0007829|PDB:1ILE" SQ SEQUENCE 1043 AA; 119247 MW; 0F8010BBE8F83A30 CRC64; MFKEVGEPNF PKLEEEVLAF WKREKIFQKS VENRKGGPRY TVYEGPPTAN GLPHVGHAQA RSYKDLFPRY KTMRGYYAPR RAGWDTHGLP VELEVEKKLG LKSKREIEAY GIERFNQACR ESVFTYEKEW EAFTERIAYW VDLENAYATL EPTYIESIWW SLKNLFDRGL LYRDHKVVPY CPRCGTPLSS HEVALGYKEI QDPSVYVRFP LKEPKKLGLE KASLLIWTTT PWTLPGNVAA AVHPEYTYAA FQVGDEALIL EEGLGRKLLG EGTPVLKTFP GKALEGLPYT PPYPQALEKG YFVVLADYVS QEDGTGIVHQ APAFGAEDLE TARVYGLPLL KTVDEEGKLL VEPFKGLYFR EANRAILRDL RGRGLLFKEE SYLHSYPHCW RCSTPLMYYA TESWFIKNTL FKDELIRKNQ EIHWVPPHIK EGRYGEWLKN LVDWALSRNR YWGTPLPIWV CQACGKEEAI GSFQELKARA TKPLPEPFDP HRPYVDQVEL ACACGGTMRR VPYVIDVWYD SGAMPFASLH YPFEHEEVFR ESFPADFIAE GIDQTRGWFN SLHQLGVMLF GSIAFKNVIC HGLILDEKGQ KMSKSKGNVV DPWDIIREFG ADALRWYIYV SAPPEADRRF GPNLVRETVR DYFLTLWNVY SFFVTYANLD RPDLKNPPPP EKRPEMDRWL LARMQDLIQR VTEALEAYDP TTSARALRDF VVEDLSQWYV RRNRRRFWKN EDALDREAAY ATLYEALVLV ATLAAPFTPF LAEVLWQNLV RSVRPEAKES VHLADWPEAD PALADEALVA QMRAVLKVVD LARAARAKSG VKTRTPLPLL LVTAPTALER EGLKRFAHEI AEELNVKEVR VLEPGEEILS YRVLPNLKLL GRKYGKLVPK IREALQRERE RAAALALKGE AIPLEVEGEA LTLLPEEVLL EAEAPKGYQA LEKDGYVAAL KVEVTEALRM EGLARDLIRL LQQARKDMGL KVSDRIRVGY EAEGPYLEAL KRHGPWIAEE VLATAFGEGL FGGFEARVED EEGKAVFHLA RAE //