SYI_THET8
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 03-AUG-2022, entry version 146.
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; Deinococcus-Thermus; 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}.
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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 STRING; 300852.55772449; -.
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 OMA; HLGTAWN; -.
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 Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR42780; PTHR42780; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 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
