SYI_ECOLI
ID SYI_ECOLI Reviewed; 938 AA.
AC P00956; P78038; Q59429;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Isoleucine--tRNA ligase;
DE EC=6.1.1.5 {ECO:0000269|PubMed:3282306};
DE AltName: Full=Isoleucyl-tRNA synthetase;
DE Short=IleRS;
GN Name=ileS; Synonyms=ilvS; OrderedLocusNames=b0026, JW0024;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12, and MRE-600;
RX PubMed=6390679; DOI=10.1126/science.6390679;
RA Webster T., Tsai H., Kula M., Mackie G.A., Schimmel P.;
RT "Specific sequence homology and three-dimensional structure of an aminoacyl
RT transfer RNA synthetase.";
RL Science 226:1315-1317(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11 AND
RP 606-615.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574, and PS102;
RX PubMed=7929087; DOI=10.1016/s0021-9258(19)51082-1;
RA Yanagisawa T., Lee J.T., Wu H.C., Kawakami M.;
RT "Relationship of protein structure of isoleucyl-tRNA synthetase with
RT pseudomonic acid resistance of Escherichia coli. A proposed mode of action
RT of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase.";
RL J. Biol. Chem. 269:24304-24309(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RX PubMed=2985604; DOI=10.1016/s0021-9258(18)89067-6;
RA Kamio Y., Lin C.-K., Regue M., Wu H.C.;
RT "Characterization of the ileS-lsp operon in Escherichia coli.
RT Identification of an open reading frame upstream of the ileS gene and
RT potential promoter(s) for the ileS-lsp operon.";
RL J. Biol. Chem. 260:5616-5620(1985).
RN [7]
RP PROTEIN SEQUENCE OF 2-938, FUNCTION, AND ATP-BINDING.
RC STRAIN=EM20031;
RX PubMed=19557155; DOI=10.2174/1874091x00903010026;
RA Baouz S., Schmitter J.M., Chenoune L., Beauvallet C., Blanquet S.,
RA Woisard A., Hountondji C.;
RT "Primary Structure Revision and Active Site Mapping of E. Coli Isoleucyl-
RT tRNA Synthetase by Means of Maldi Mass Spectrometry.";
RL Open Biochem. J. 3:26-38(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 794-938.
RX PubMed=6378662; DOI=10.1016/0014-5793(84)81060-1;
RA Yu F., Yamada H., Daishima K., Mizushima S.;
RT "Nucleotide sequence of the lspA gene, the structural gene for lipoprotein
RT signal peptidase of Escherichia coli.";
RL FEBS Lett. 173:264-268(1984).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 795-938.
RX PubMed=6374664; DOI=10.1073/pnas.81.12.3708;
RA Innis M.A., Tokunaga M., Williams M.E., Loranger J.M., Chang S.-Y.,
RA Chang S., Wu H.C.;
RT "Nucleotide sequence of the Escherichia coli prolipoprotein signal
RT peptidase (lsp) gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3708-3712(1984).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-94; CYS-97 AND ILE-102,
RP AND KINETIC PARAMETERS.
RX PubMed=3282306; DOI=10.1126/science.3282306;
RA Clarke N.D., Lien D.C., Schimmel P.;
RT "Evidence from cassette mutagenesis for a structure-function motif in a
RT protein of unknown structure.";
RL Science 240:521-523(1988).
RN [11]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF THR-241; THR-243; THR-246 AND ASN-250.
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 [13]
RP FUNCTION IN EDITING ACTIVITY.
RX PubMed=10549284; DOI=10.1016/s1097-2765(00)80203-8;
RA Nomanbhoy T.K., Hendrickson T.L., Schimmel P.;
RT "Transfer RNA-dependent translocation of misactivated amino acids to
RT prevent errors in protein synthesis.";
RL Mol. Cell 4:519-528(1999).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF THR-242 AND ASN-250.
RX PubMed=10889024; DOI=10.1021/bi0004798;
RA Hendrickson T.L., Nomanbhoy T.K., Schimmel P.;
RT "Errors from selective disruption of the editing center in a tRNA
RT synthetase.";
RL Biochemistry 39:8180-8186(2000).
RN [15]
RP FUNCTION, MUTAGENESIS OF THR-243 AND HIS-333, AND PRESENCE OF TWO EDITING
RP SUBSITES.
RX PubMed=11864608; DOI=10.1016/s1097-2765(02)00449-5;
RA Hendrickson T.L., Nomanbhoy T.K., de Crecy-Lagard V., Fukai S., Nureki O.,
RA Yokoyama S., Schimmel P.;
RT "Mutational separation of two pathways for editing by a class I tRNA
RT synthetase.";
RL Mol. Cell 9:353-362(2002).
RN [16]
RP FUNCTION, MUTAGENESIS OF ASP-342, AND TRANSLOCATION OF MISACTIVATED VALINE.
RX PubMed=11782529; DOI=10.1073/pnas.012611299;
RA Bishop A.C., Nomanbhoy T.K., Schimmel P.;
RT "Blocking site-to-site translocation of a misactivatd amino acid by
RT mutation of a class I tRNA synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:585-590(2002).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF LYS-183 AND TRP-421.
RX PubMed=12515858; DOI=10.1073/pnas.0237335100;
RA Bishop A.C., Beebe K., Schimmel P.R.;
RT "Interstice mutations that block site-to-site translocation of a
RT misactivated amino acid bound to a class I tRNA synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:490-494(2003).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-183, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
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).
CC {ECO:0000269|PubMed:10549284, ECO:0000269|PubMed:10889024,
CC ECO:0000269|PubMed:11782529, ECO:0000269|PubMed:11864608,
CC ECO:0000269|PubMed:12515858, ECO:0000269|PubMed:19557155,
CC ECO:0000269|PubMed:3282306, ECO:0000269|PubMed:9554847}.
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 Evidence={ECO:0000269|PubMed:3282306};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for isoleucine {ECO:0000269|PubMed:3282306};
CC KM=0.4 mM for ATP {ECO:0000269|PubMed:3282306};
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P00956; P19930: hyaD; NbExp=3; IntAct=EBI-552928, EBI-552940;
CC P00956; P02925: rbsB; NbExp=3; IntAct=EBI-552928, EBI-369930;
CC P00956; P0CE47: tufA; NbExp=2; IntAct=EBI-552928, EBI-301077;
CC P00956; P39336: yjgL; NbExp=3; IntAct=EBI-552928, EBI-549937;
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)).
CC -!- MISCELLANEOUS: Strain PS102 is resistant to the antibiotic mupirocin
CC (pseudomonic acid A), an Ile-analog that competitively inhibits
CC activation by Ile-tRNA synthetase, thus inhibiting protein
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC73137.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96595.2; -; Genomic_DNA.
DR EMBL; M10428; AAA24606.1; -; Genomic_DNA.
DR EMBL; X00776; CAA25352.1; -; Genomic_DNA.
DR EMBL; K01990; AAA24091.1; -; Genomic_DNA.
DR PIR; B64723; SYECIT.
DR RefSeq; NP_414567.1; NC_000913.3.
DR RefSeq; WP_001286857.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P00956; -.
DR SMR; P00956; -.
DR BioGRID; 4261375; 35.
DR BioGRID; 849163; 6.
DR DIP; DIP-10017N; -.
DR IntAct; P00956; 17.
DR STRING; 511145.b0026; -.
DR BindingDB; P00956; -.
DR ChEMBL; CHEMBL3657; -.
DR DrugCentral; P00956; -.
DR iPTMnet; P00956; -.
DR jPOST; P00956; -.
DR PaxDb; P00956; -.
DR PRIDE; P00956; -.
DR EnsemblBacteria; AAC73137; AAC73137; b0026.
DR EnsemblBacteria; BAB96595; BAB96595; BAB96595.
DR GeneID; 944761; -.
DR KEGG; ecj:JW0024; -.
DR KEGG; eco:b0026; -.
DR PATRIC; fig|1411691.4.peg.2259; -.
DR EchoBASE; EB0487; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_6; -.
DR InParanoid; P00956; -.
DR OMA; HLGTAWN; -.
DR PhylomeDB; P00956; -.
DR BioCyc; EcoCyc:ILES-MON; -.
DR BioCyc; MetaCyc:ILES-MON; -.
DR BRENDA; 6.1.1.5; 2026.
DR SABIO-RK; P00956; -.
DR PRO; PR:P00956; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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; IDA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IDA:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
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 InterPro; IPR010663; Znf_FPG/IleRS.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 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 Acetylation; Aminoacyl-tRNA synthetase; Antibiotic resistance; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6390679,
FT ECO:0000269|PubMed:7929087"
FT CHAIN 2..938
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098384"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT MOTIF 602..606
FT /note="'KMSKS' region"
FT BINDING 561
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000250"
FT BINDING 602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19557155"
FT BINDING 605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19557155"
FT BINDING 901
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 921
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 924
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 183
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT VARIANT 300..301
FT /note="EL -> DV (in strain: EM20031, MRE-600; AA sequence)"
FT /evidence="ECO:0000269|PubMed:19557155,
FT ECO:0000269|PubMed:6390679"
FT VARIANT 587
FT /note="R -> C (in strain: MRE-600; AA sequence)"
FT /evidence="ECO:0000269|PubMed:6390679"
FT VARIANT 594
FT /note="F -> L (in strain: PS102)"
FT /evidence="ECO:0000269|PubMed:7929087"
FT VARIANT 637
FT /note="E -> Q (in strain: MRE-600; AA sequence)"
FT /evidence="ECO:0000269|PubMed:6390679"
FT VARIANT 724
FT /note="G -> V (in strain: EM20031; AA sequence)"
FT /evidence="ECO:0000269|PubMed:19557155"
FT VARIANT 738
FT /note="A -> P (in strain: EM20031, MRE-600; AA sequence)"
FT /evidence="ECO:0000269|PubMed:19557155,
FT ECO:0000269|PubMed:6390679"
FT VARIANT 740..743
FT /note="ADSV -> RTVW (in strain: EM20031; AA sequence)"
FT /evidence="ECO:0000269|PubMed:19557155"
FT VARIANT 787
FT /note="F -> L (in strain: MRE-600; AA sequence)"
FT /evidence="ECO:0000269|PubMed:6390679"
FT VARIANT 830
FT /note="K -> N (in strain: MRE-600; AA sequence)"
FT /evidence="ECO:0000269|PubMed:6390679"
FT MUTAGEN 94
FT /note="G->R: 6000-fold increase in Km for isoleucine and 4-
FT fold increase in Km for ATP, with no effect on activity."
FT /evidence="ECO:0000269|PubMed:3282306"
FT MUTAGEN 97
FT /note="C->S: No effect on activity."
FT /evidence="ECO:0000269|PubMed:3282306"
FT MUTAGEN 102
FT /note="I->N: No significant effect on activity."
FT /evidence="ECO:0000269|PubMed:3282306"
FT MUTAGEN 183
FT /note="K->A: Abolishes translocation from the
FT aminoacylation site to the editing site, without effect on
FT aminoacylation activity and posttransfer editing; when
FT associated with A-421."
FT /evidence="ECO:0000269|PubMed:12515858"
FT MUTAGEN 241
FT /note="T->A: Nearly the same editing activity as the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:9554847"
FT MUTAGEN 242
FT /note="T->A: Abolishes editing activity against valine,
FT with little change in aminoacylation activity; when
FT associated with A-250."
FT /evidence="ECO:0000269|PubMed:10889024"
FT MUTAGEN 242
FT /note="T->P: Abolishes editing activity against valine,
FT with little change in aminoacylation activity."
FT /evidence="ECO:0000269|PubMed:10889024"
FT MUTAGEN 243
FT /note="T->A: Abolishes editing activity against valine,
FT with little change in aminoacylation activity."
FT /evidence="ECO:0000269|PubMed:11864608,
FT ECO:0000269|PubMed:9554847"
FT MUTAGEN 243
FT /note="T->R: Abolishes pretransfer editing."
FT /evidence="ECO:0000269|PubMed:11864608,
FT ECO:0000269|PubMed:9554847"
FT MUTAGEN 246
FT /note="T->A: Nearly the same editing activity as the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:9554847"
FT MUTAGEN 250
FT /note="N->A: Abolishes editing activity against valine,
FT with little change in aminoacylation activity."
FT /evidence="ECO:0000269|PubMed:10889024,
FT ECO:0000269|PubMed:9554847"
FT MUTAGEN 333
FT /note="H->A: Alters the specificity for hydrolysis of the
FT aminoacyl tRNA ester, with no effect on pretransfer
FT editing."
FT /evidence="ECO:0000269|PubMed:11864608"
FT MUTAGEN 342
FT /note="D->A,N: Strong decrease in total editing and
FT deacylation activities. Severely deficient in translocation
FT from the aminoacylation site to the editing site."
FT /evidence="ECO:0000269|PubMed:11782529"
FT MUTAGEN 342
FT /note="D->E: Reduces 2- to 3-fold the total editing
FT activity and 2-fold the deacylation activity. Moderately
FT reduces translocation from the aminoacylation site to the
FT editing site."
FT /evidence="ECO:0000269|PubMed:11782529"
FT MUTAGEN 421
FT /note="W->A: Abolishes translocation from the
FT aminoacylation site to the editing site, without effect on
FT aminoacylation activity and posttransfer editing; when
FT associated with A-183."
FT /evidence="ECO:0000269|PubMed:12515858"
SQ SEQUENCE 938 AA; 104297 MW; 238CEDAF461F01D5 CRC64;
MSDYKSTLNL PETGFPMRGD LAKREPGMLA RWTDDDLYGI IRAAKKGKKT FILHDGPPYA
NGSIHIGHSV NKILKDIIVK SKGLSGYDSP YVPGWDCHGL PIELKVEQEY GKPGEKFTAA
EFRAKCREYA ATQVDGQRKD FIRLGVLGDW SHPYLTMDFK TEANIIRALG KIIGNGHLHK
GAKPVHWCVD CRSALAEAEV EYYDKTSPSI DVAFQAVDQD ALKAKFAVSN VNGPISLVIW
TTTPWTLPAN RAISIAPDFD YALVQIDGQA VILAKDLVES VMQRIGVTDY TILGTVKGAE
LELLRFTHPF MGFDVPAILG DHVTLDAGTG AVHTAPGHGP DDYVIGQKYG LETANPVGPD
GTYLPGTYPT LDGVNVFKAN DIVVALLQEK GALLHVEKMQ HSYPCCWRHK TPIIFRATPQ
WFVSMDQKGL RAQSLKEIKG VQWIPDWGQA RIESMVANRP DWCISRQRTW GVPMSLFVHK
DTEELHPRTL ELMEEVAKRV EVDGIQAWWD LDAKEILGDE ADQYVKVPDT LDVWFDSGST
HSSVVDVRPE FAGHAADMYL EGSDQHRGWF MSSLMISTAM KGKAPYRQVL THGFTVDGQG
RKMSKSIGNT VSPQDVMNKL GADILRLWVA STDYTGEMAV SDEILKRAAD SYRRIRNTAR
FLLANLNGFD PAKDMVKPEE MVVLDRWAVG CAKAAQEDIL KAYEAYDFHE VVQRLMRFCS
VEMGSFYLDI IKDRQYTAKA DSVARRSCQT ALYHIAEALV RWMAPILSFT ADEVWGYLPG
EREKYVFTGE WYEGLFGLAD SEAMNDAFWD ELLKVRGEVN KVIEQARADK KVGGSLEAAV
TLYAEPELSA KLTALGDELR FVLLTSGATV ADYNDAPADA QQSEVLKGLK VALSKAEGEK
CPRCWHYTQD VGKVAEHAEI CGRCVSNVAG DGEKRKFA
