SYY_GEOSE
ID SYY_GEOSE Reviewed; 419 AA.
AC P00952;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tyrosine--tRNA ligase;
DE EC=6.1.1.1 {ECO:0000269|PubMed:1542120};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000303|PubMed:6315404};
DE Short=TyrRS {ECO:0000303|PubMed:6315404};
DE Short=TyrTS {ECO:0000303|PubMed:7120416};
GN Name=tyrS;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-124; 136-157
RP AND 172-419.
RX PubMed=6840095; DOI=10.1111/j.1432-1033.1983.tb07374.x;
RA Winter G., Koch G.L.E., Hartley B.S., Barker D.G.;
RT "The amino acid sequence of the tyrosyl-tRNA synthetase from Bacillus
RT stearothermophilus.";
RL Eur. J. Biochem. 132:383-387(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX PubMed=3525162; DOI=10.1111/j.1432-1033.1986.tb09783.x;
RA Waye M.M.Y., Winter G.;
RT "A transcription terminator in the 5' non-coding region of the tyrosyl tRNA
RT synthetase gene from Bacillus stearothermophilus.";
RL Eur. J. Biochem. 158:505-510(1986).
RN [3]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6315404; DOI=10.1002/j.1460-2075.1983.tb01665.x;
RA Waye M.M.Y., Winter G., Wilkinson A.J., Fersht A.R.;
RT "Deletion mutagenesis using an 'M13 splint': the N-terminal structural
RT domain of tyrosyl-tRNA synthetase (B. stearothermophilus) catalyses the
RT formation of tyrosyl adenylate.";
RL EMBO J. 2:1827-1829(1983).
RN [4]
RP INTERACTION WITH TRNA(TYR), AND SUBUNIT.
RX PubMed=3006039; DOI=10.1073/pnas.83.5.1189;
RA Carter P., Bedouelle H., Winter G.;
RT "Construction of heterodimer tyrosyl-tRNA synthetase shows tRNATyr
RT interacts with both subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1189-1192(1986).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-45; GLU-152; THR-224;
RP LYS-410 AND LYS-411.
RX PubMed=1542120; DOI=10.1016/0022-2836(92)90991-r;
RA Vidal-Cros A., Bedouelle H.;
RT "Role of residue Glu152 in the discrimination between transfer RNAs by
RT tyrosyl-tRNA synthetase from Bacillus stearothermophilus.";
RL J. Mol. Biol. 223:801-810(1992).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, MOTIF, AND MUTAGENESIS OF LYS-230; PHE-231;
RP GLY-232; LYS-233 AND THR-234.
RX PubMed=10630994; DOI=10.1021/bi991675l;
RA Xin Y., Li W., First E.A.;
RT "The 'KMSKS' motif in tyrosyl-tRNA synthetase participates in the initial
RT binding of tRNA(Tyr).";
RL Biochemistry 39:340-347(2000).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-40; HIS-45; HIS-48;
RP LYS-82 AND ARG-86.
RX PubMed=11023793; DOI=10.1006/jmbi.2000.4125;
RA Xin Y., Li W., Dwyer D.S., First E.A.;
RT "Correlating amino acid conservation with function in tyrosyl-tRNA
RT synthetase.";
RL J. Mol. Biol. 303:287-298(2000).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, MOTIF, AND MUTAGENESIS OF ASP-78; TYR-169;
RP GLN-173; ASP-194 AND GLN-195.
RX PubMed=11023794; DOI=10.1006/jmbi.2000.4126;
RA Xin Y., Li W., First E.A.;
RT "Stabilization of the transition state for the transfer of tyrosine to
RT tRNA(Tyr) by tyrosyl-tRNA synthetase.";
RL J. Mol. Biol. 303:299-310(2000).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-322; PHE-323; SER-324;
RP GLY-325 AND PHE-339.
RX PubMed=11401566; DOI=10.1021/bi010208c;
RA Gaillard C., Bedouelle H.;
RT "An essential residue in the flexible peptide linking the two
RT idiosynchratic domains of bacterial tyrosyl-tRNA synthetases.";
RL Biochemistry 40:7192-7199(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=7120416; DOI=10.1016/0022-2836(82)90255-8;
RA Bhat T.N., Blow D.M., Brick P., Nyborg J.;
RT "Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold.";
RL J. Mol. Biol. 158:699-709(1982).
RN [11] {ECO:0007744|PDB:1TYD, ECO:0007744|PDB:2TS1, ECO:0007744|PDB:3TS1}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH TYROSINE.
RX PubMed=2504923; DOI=10.1016/0022-2836(89)90090-9;
RA Brick P., Bhat T.N., Blow D.M.;
RT "Structure of tyrosyl-tRNA synthetase refined at 2.3-A resolution.
RT Interaction of the enzyme with the tyrosyl adenylate intermediate.";
RL J. Mol. Biol. 208:83-98(1989).
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr).
CC {ECO:0000269|PubMed:10630994, ECO:0000269|PubMed:11023793,
CC ECO:0000269|PubMed:11023794, ECO:0000269|PubMed:1542120,
CC ECO:0000269|PubMed:6315404}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC Evidence={ECO:0000269|PubMed:10630994, ECO:0000269|PubMed:11023793,
CC ECO:0000269|PubMed:11023794, ECO:0000269|PubMed:11401566,
CC ECO:0000269|PubMed:1542120};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.35 mM for ATP {ECO:0000269|PubMed:6315404};
CC KM=1.8 uM for tyrosine {ECO:0000269|PubMed:6315404};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:3006039}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 1 subfamily. {ECO:0000305}.
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DR EMBL; J01546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X04193; CAA27784.1; -; Genomic_DNA.
DR PIR; A01179; SYBSYF.
DR RefSeq; WP_033014498.1; NZ_RCTK01000009.1.
DR PDB; 1JH3; NMR; -; A=321-419.
DR PDB; 1TYA; X-ray; 2.80 A; E=1-319.
DR PDB; 1TYB; X-ray; 2.50 A; E=1-319.
DR PDB; 1TYC; X-ray; 2.50 A; A=1-319.
DR PDB; 1TYD; X-ray; 2.50 A; E=1-319.
DR PDB; 2TS1; X-ray; 2.30 A; A=1-419.
DR PDB; 3TS1; X-ray; 2.70 A; A=1-419.
DR PDB; 4TS1; X-ray; 2.50 A; A/B=1-317.
DR PDBsum; 1JH3; -.
DR PDBsum; 1TYA; -.
DR PDBsum; 1TYB; -.
DR PDBsum; 1TYC; -.
DR PDBsum; 1TYD; -.
DR PDBsum; 2TS1; -.
DR PDBsum; 3TS1; -.
DR PDBsum; 4TS1; -.
DR AlphaFoldDB; P00952; -.
DR BMRB; P00952; -.
DR SMR; P00952; -.
DR GeneID; 58573035; -.
DR BRENDA; 6.1.1.1; 623.
DR SABIO-RK; P00952; -.
DR EvolutionaryTrace; P00952; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0000049; F:tRNA binding; IDA:CAFA.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IDA:CAFA.
DR GO; GO:0061635; P:regulation of protein complex stability; IMP:CAFA.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IDA:CAFA.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR InterPro; IPR024107; Tyr-tRNA-ligase_bac_1.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF01479; S4; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Nucleotide-binding;
KW Protein biosynthesis; RNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6840095"
FT CHAIN 2..419
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000055642"
FT DOMAIN 352..419
FT /note="S4 RNA-binding"
FT MOTIF 39..48
FT /note="'HIGH' region"
FT /evidence="ECO:0000305|PubMed:11023794"
FT MOTIF 230..234
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305|PubMed:10630994"
FT BINDING 34
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0007744|PDB:1TYD"
FT BINDING 169
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0007744|PDB:1TYD"
FT BINDING 173
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250, ECO:0007744|PDB:1TYD"
FT BINDING 176
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250, ECO:0007744|PDB:1TYD"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 40
FT /note="T->A: Destabilizes the transition states for both
FT steps of the reaction."
FT /evidence="ECO:0000269|PubMed:11023793"
FT MUTAGEN 45
FT /note="H->A: Does not affect the second step of the
FT reaction."
FT /evidence="ECO:0000269|PubMed:11023793,
FT ECO:0000269|PubMed:1542120"
FT MUTAGEN 45
FT /note="H->N: Decreases the rate of formation of Tyr-AMP
FT and, as a consequence, abolishes the aminoacylation
FT activity. Strongly increases the toxicity; when associated
FT with A-152."
FT /evidence="ECO:0000269|PubMed:11023793,
FT ECO:0000269|PubMed:1542120"
FT MUTAGEN 48
FT /note="H->A: Does not affect the second step of the
FT reaction."
FT /evidence="ECO:0000269|PubMed:11023793"
FT MUTAGEN 78
FT /note="D->A: Does not affect the initial binding of
FT tRNA(Tyr) and the stability of the transition state for the
FT second step of the reaction."
FT /evidence="ECO:0000269|PubMed:11023794"
FT MUTAGEN 82
FT /note="K->A: Destabilizes the transition states for both
FT steps of the reaction."
FT /evidence="ECO:0000269|PubMed:11023793"
FT MUTAGEN 86
FT /note="R->A: Destabilizes the transition states for both
FT steps of the reaction."
FT /evidence="ECO:0000269|PubMed:11023793"
FT MUTAGEN 152
FT /note="E->A: Mischarges tRNA(Phe) with tyrosine in vitro.
FT Toxic for the cell, probably because it alters the
FT discrimination of TyrRS against non-cognate tRNAs. The
FT toxicity is abolished; when associated with N-410 or N-411.
FT Strongly increases toxicity; when associated with N-45.
FT Enhances the toxicity; when associated with A-224."
FT /evidence="ECO:0000269|PubMed:1542120"
FT MUTAGEN 152
FT /note="E->D: Does not charge tRNA(Phe) in vitro with
FT tyrosine."
FT /evidence="ECO:0000269|PubMed:1542120"
FT MUTAGEN 152
FT /note="E->Q: Mischarges tRNA(Phe) with tyrosine in vitro
FT but this mutation is not toxic in vivo."
FT /evidence="ECO:0000269|PubMed:1542120"
FT MUTAGEN 169
FT /note="Y->A: Does not affect the initial binding of
FT tRNA(Tyr) and the stability of the transition state for the
FT second step of the reaction."
FT /evidence="ECO:0000269|PubMed:11023794"
FT MUTAGEN 173
FT /note="Q->A: Destabilizes the transition state for the
FT second step of the reaction."
FT /evidence="ECO:0000269|PubMed:11023794"
FT MUTAGEN 194
FT /note="D->A: Destabilizes the transition state for the
FT first step of the reaction, but does not affect the
FT transition state for the second step."
FT /evidence="ECO:0000269|PubMed:11023794"
FT MUTAGEN 195
FT /note="Q->A: Destabilizes the transition state for the
FT first step of the reaction, but does not affect the
FT transition state for the second step."
FT /evidence="ECO:0000269|PubMed:11023794"
FT MUTAGEN 224
FT /note="T->A: Is not toxic in itself. Enhances the toxicity;
FT when associated with A-152."
FT /evidence="ECO:0000269|PubMed:1542120"
FT MUTAGEN 230
FT /note="K->A: Decreases the binding affinity between
FT tRNA(Tyr) and TyrRS-Tyr-AMP complex."
FT /evidence="ECO:0000269|PubMed:10630994"
FT MUTAGEN 231
FT /note="F->L: No effect on the binding affinity between
FT tRNA(Tyr) and TyrRS-Tyr-AMP complex."
FT /evidence="ECO:0000269|PubMed:10630994"
FT MUTAGEN 232
FT /note="G->A: No effect on the binding affinity between
FT tRNA(Tyr) and TyrRS-Tyr-AMP complex."
FT /evidence="ECO:0000269|PubMed:10630994"
FT MUTAGEN 233
FT /note="K->A: Decreases the binding affinity between
FT tRNA(Tyr) and TyrRS-Tyr-AMP complex."
FT /evidence="ECO:0000269|PubMed:10630994"
FT MUTAGEN 234
FT /note="T->A: No effect on the binding affinity between
FT tRNA(Tyr) and TyrRS-Tyr-AMP complex."
FT /evidence="ECO:0000269|PubMed:10630994"
FT MUTAGEN 322
FT /note="L->P: 50-fold decrease in charging of tRNA(Tyr) with
FT tyrosine."
FT /evidence="ECO:0000269|PubMed:11401566"
FT MUTAGEN 323
FT /note="F->A: 90-fold decrease in charging of tRNA(Tyr) with
FT tyrosine, without effect on the first step of the
FT reaction."
FT /evidence="ECO:0000269|PubMed:11401566"
FT MUTAGEN 323
FT /note="F->L: 67-fold decrease in charging of tRNA(Tyr) with
FT tyrosine, without effect on the first step of the
FT reaction."
FT /evidence="ECO:0000269|PubMed:11401566"
FT MUTAGEN 323
FT /note="F->W: Weak decrease in charging of tRNA(Tyr) with
FT tyrosine, without effect on the first step of the
FT reaction."
FT /evidence="ECO:0000269|PubMed:11401566"
FT MUTAGEN 323
FT /note="F->Y: 3-fold decrease in charging of tRNA(Tyr) with
FT tyrosine, without effect on the first step of the
FT reaction."
FT /evidence="ECO:0000269|PubMed:11401566"
FT MUTAGEN 324
FT /note="S->A: 2-fold increase in charging of tRNA(Tyr) with
FT tyrosine."
FT /evidence="ECO:0000269|PubMed:11401566"
FT MUTAGEN 325
FT /note="G->A: 5-fold increase in charging of tRNA(Tyr) with
FT tyrosine."
FT /evidence="ECO:0000269|PubMed:11401566"
FT MUTAGEN 339
FT /note="F->L: Has no effect on charging of tRNA(Tyr) with
FT tyrosine."
FT /evidence="ECO:0000269|PubMed:11401566"
FT MUTAGEN 410
FT /note="K->N: Decreases the binding of tRNA(Tyr), without
FT affecting the formation of Tyr-AMP. Abolishes the toxicity;
FT when associated with A-152."
FT /evidence="ECO:0000269|PubMed:1542120"
FT MUTAGEN 411
FT /note="K->N: Decreases the binding of tRNA(Tyr), without
FT affecting the formation of Tyr-AMP. Abolishes the toxicity;
FT when associated with A-152."
FT /evidence="ECO:0000269|PubMed:1542120"
FT HELIX 2..10
FT /evidence="ECO:0007829|PDB:2TS1"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:2TS1"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2TS1"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:2TS1"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1TYC"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2TS1"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:2TS1"
FT TURN 156..160
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 164..184
FT /evidence="ECO:0007829|PDB:2TS1"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 196..210
FT /evidence="ECO:0007829|PDB:2TS1"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:2TS1"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:4TS1"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2TS1"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:2TS1"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1TYB"
FT HELIX 293..307
FT /evidence="ECO:0007829|PDB:2TS1"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:2TS1"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1JH3"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:1JH3"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:1JH3"
FT HELIX 354..361
FT /evidence="ECO:0007829|PDB:1JH3"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:1JH3"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:1JH3"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:1JH3"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:1JH3"
FT STRAND 399..408
FT /evidence="ECO:0007829|PDB:1JH3"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:1JH3"
SQ SEQUENCE 419 AA; 47303 MW; B9CB64AEEEE2010F CRC64;
MDLLAELQWR GLVNQTTDED GLRKLLNEER VTLYCGFDPT ADSLHIGHLA TILTMRRFQQ
AGHRPIALVG GATGLIGDPS GKKSERTLNA KETVEAWSAR IKEQLGRFLD FEADGNPAKI
KNNYDWIGPL DVITFLRDVG KHFSVNYMMA KESVQSRIET GISFTEFSYM MLQAYDFLRL
YETEGCRLQI GGSDQWGNIT AGLELIRKTK GEARAFGLTI PLVTKADGTK FGKTESGTIW
LDKEKTSPYE FYQFWINTDD RDVIRYLKYF TFLSKEEIEA LEQELREAPE KRAAQKTLAE
EVTKLVHGEE ALRQAIRISE ALFSGDIANL TAAEIEQGFK DVPSFVHEGG DVPLVELLVS
AGISPSKRQA REDIQNGAIY VNGERLQDVG AILTAEHRLE GRFTVIRRGK KKYYLIRYA
