SYYC_YEAST
ID SYYC_YEAST Reviewed; 394 AA.
AC P36421; D6VUW8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Tyrosine--tRNA ligase, cytoplasmic {ECO:0000305};
DE EC=6.1.1.1 {ECO:0000269|PubMed:8509419};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000303|PubMed:8509419};
DE Short=TyrRS {ECO:0000303|PubMed:8509419};
GN Name=TYS1 {ECO:0000303|PubMed:8509419}; Synonyms=MGM104;
GN OrderedLocusNames=YGR185C; ORFNames=G7522;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8509419; DOI=10.1016/s0021-9258(18)31466-2;
RA Chow C.M., RajBhandary U.L.;
RT "Saccharomyces cerevisiae cytoplasmic tyrosyl-tRNA synthetase gene.
RT Isolation by complementation of a mutant Escherichia coli suppressor tRNA
RT defective in aminoacylation and sequence analysis.";
RL J. Biol. Chem. 268:12855-12863(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9294037; DOI=10.1007/s004380050525;
RA Guan M.-X.;
RT "Cytoplasmic tyrosyl-tRNA synthetase rescues the defect in mitochondrial
RT genome maintenance caused by the nuclear mutation mgm104-1 in the yeast
RT Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 255:525-532(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9133739;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<357::aid-yea77>3.0.co;2-j;
RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M.,
RA Nombela C.;
RT "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:357-363(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RC STRAIN=ATCC 208279 / BJ926;
RX PubMed=7995524; DOI=10.1101/gad.8.23.2868;
RA Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A., Kornberg R.D.;
RT "TFIIF-TAF-RNA polymerase II connection.";
RL Genes Dev. 8:2868-2878(1994).
RN [7]
RP PROTEIN SEQUENCE OF 2-18 AND 324-338, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [8]
RP SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=328277; DOI=10.1111/j.1432-1033.1977.tb11556.x;
RA Faulhammer H.G., Cramer F.;
RT "Tyroslyl-tRNA synthetase from baker's yeast. Rapid isolation by affinity
RT elution, molecular weight of the enzyme, and determination of essential
RT sulfhydryl groups.";
RL Eur. J. Biochem. 75:561-570(1977).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3535890; DOI=10.1021/bi00367a072;
RA Bare L.A., Uhlenbeck O.C.;
RT "Specific substitution into the anticodon loop of yeast tyrosine transfer
RT RNA.";
RL Biochemistry 25:5825-5830(1986).
RN [10]
RP FUNCTION.
RX PubMed=10588711; DOI=10.1073/pnas.96.25.14366;
RA Sarkar S., Azad A.K., Hopper A.K.;
RT "Nuclear tRNA aminoacylation and its role in nuclear export of endogenous
RT tRNAs in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14366-14371(1999).
RN [11]
RP FUNCTION.
RX PubMed=10677221; DOI=10.1021/bi992276t;
RA Fechter P., Rudinger-Thirion J., Theobald-Dietrich A., Giege R.;
RT "Identity of tRNA for yeast tyrosyl-tRNA synthetase: tyrosylation is more
RT sensitive to identity nucleotides than to structural features.";
RL Biochemistry 39:1725-1733(2000).
RN [12]
RP FUNCTION.
RC STRAIN=YP-ALS;
RX PubMed=10766779; DOI=10.1074/jbc.275.16.11626;
RA Soutourina J., Blanquet S., Plateau P.;
RT "D-tyrosyl-tRNA(Tyr) metabolism in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:11626-11630(2000).
RN [13]
RP INTERACTION WITH KNR4/SMI1.
RX PubMed=11410349; DOI=10.1111/j.1574-6968.2001.tb10692.x;
RA Dagkessamanskaia A., Martin-Yken H., Basmaji F., Briza P., Francois J.;
RT "Interaction of Knr4 protein, a protein involved in cell wall synthesis,
RT with tyrosine tRNA synthetase encoded by TYS1 in Saccharomyces
RT cerevisiae.";
RL FEMS Microbiol. Lett. 200:53-58(2001).
RN [14]
RP MUTAGENESIS OF TYR-43.
RX PubMed=11530018; DOI=10.1093/oxfordjournals.jbchem.a003001;
RA Ohno S., Yokogawa T., Nishikawa K.;
RT "Changing the amino acid specificity of yeast tyrosyl-tRNA synthetase by
RT genetic engineering.";
RL J. Biochem. 130:417-423(2001).
RN [15]
RP MUTAGENESIS OF 364-LYS--LYS-368, AND SUBCELLULAR LOCATION.
RX PubMed=11359929; DOI=10.1091/mbc.12.5.1381;
RA Azad A.K., Stanford D.R., Sarkar S., Hopper A.K.;
RT "Role of nuclear pools of aminoacyl-tRNA synthetases in tRNA nuclear
RT export.";
RL Mol. Biol. Cell 12:1381-1392(2001).
RN [16]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [17]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND THR-359, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [20] {ECO:0007744|PDB:2DLC}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RX PubMed=17576676; DOI=10.1093/nar/gkm417;
RA Tsunoda M., Kusakabe Y., Tanaka N., Ohno S., Nakamura M., Senda T.,
RA Moriguchi T., Asai N., Sekine M., Yokogawa T., Nishikawa K., Nakamura K.T.;
RT "Structural basis for recognition of cognate tRNA by tyrosyl-tRNA
RT synthetase from three kingdoms.";
RL Nucleic Acids Res. 35:4289-4300(2007).
CC -!- FUNCTION: Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-
CC step reaction: L-tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr) (PubMed:8509419,
CC PubMed:3535890, PubMed:10588711, PubMed:10677221, PubMed:10766779). The
CC specificity determinants on tRNA(Tyr) are the base pair C1-G72, the
CC discriminator residue A73, and the three anticodon bases G34, U35 and
CC A36 (PubMed:10677221). Also involved in nuclear tRNA export
CC (PubMed:10588711). Also attaches D-Tyr to tRNA(Tyr), this reaction is
CC about 150-fold less efficient than attachment of L-Tyr
CC (PubMed:10766779). {ECO:0000269|PubMed:10588711,
CC ECO:0000269|PubMed:10677221, ECO:0000269|PubMed:10766779,
CC ECO:0000269|PubMed:3535890, ECO:0000269|PubMed:8509419}.
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:3535890, ECO:0000269|PubMed:8509419};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide and p-
CC chloromercuribenzoate. {ECO:0000269|PubMed:328277}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=54 nM for tRNA(Tyr) {ECO:0000269|PubMed:3535890};
CC Vmax=280 nmol/min/mg enzyme for tRNA(Tyr)
CC {ECO:0000269|PubMed:3535890};
CC Note=The catalytic activity is reduced by substitutions of residues
CC forming the specificity determinant on the target tRNA(Tyr).
CC {ECO:0000269|PubMed:3535890};
CC -!- SUBUNIT: Homodimer. Interacts with KNR4/SMI1.
CC {ECO:0000269|PubMed:11410349, ECO:0000269|PubMed:328277}.
CC -!- INTERACTION:
CC P36421; P32566: SMI1; NbExp=3; IntAct=EBI-18843, EBI-17452;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic, only a small fraction (about 1.5%) found in the nucleus.
CC -!- MISCELLANEOUS: Present with 2710 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; L12221; AAB59329.1; -; mRNA.
DR EMBL; X71998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X99074; CAA67529.1; -; Genomic_DNA.
DR EMBL; Z72970; CAA97211.1; -; Genomic_DNA.
DR EMBL; U13015; AAA61641.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08279.1; -; Genomic_DNA.
DR PIR; A45999; A45999.
DR RefSeq; NP_011701.3; NM_001181314.3.
DR PDB; 2DLC; X-ray; 2.40 A; X=1-394.
DR PDBsum; 2DLC; -.
DR AlphaFoldDB; P36421; -.
DR SMR; P36421; -.
DR BioGRID; 33437; 226.
DR DIP; DIP-5548N; -.
DR IntAct; P36421; 17.
DR MINT; P36421; -.
DR STRING; 4932.YGR185C; -.
DR iPTMnet; P36421; -.
DR MaxQB; P36421; -.
DR PaxDb; P36421; -.
DR PRIDE; P36421; -.
DR EnsemblFungi; YGR185C_mRNA; YGR185C; YGR185C.
DR GeneID; 853097; -.
DR KEGG; sce:YGR185C; -.
DR SGD; S000003417; TYS1.
DR VEuPathDB; FungiDB:YGR185C; -.
DR eggNOG; KOG2144; Eukaryota.
DR HOGENOM; CLU_035267_0_1_1; -.
DR InParanoid; P36421; -.
DR OMA; YIGFEIS; -.
DR BioCyc; YEAST:G3O-30875-MON; -.
DR BRENDA; 6.1.1.1; 984.
DR EvolutionaryTrace; P36421; -.
DR PRO; PR:P36421; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P36421; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IDA:SGD.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IDA:SGD.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 2..394
FT /note="Tyrosine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000055676"
FT REGION 348..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 48..56
FT /note="'HIGH' region"
FT MOTIF 227..231
FT /note="'KMSKS' region"
FT MOTIF 360..378
FT /note="Nuclear localization signal"
FT BINDING 43
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 170
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 174
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 177
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 192
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 359
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 43
FT /note="Y->G: Decreases catalytic activity for L-tyrosine
FT 400-fold, but allows the utilization of 3-iodo-L-tyrosine
FT and other 3-modified tyrosines as substrates."
FT /evidence="ECO:0000269|PubMed:11530018"
FT MUTAGEN 364..368
FT /note="KKAKK->EEAEE: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:11359929"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:2DLC"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:2DLC"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:2DLC"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:2DLC"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 93..111
FT /evidence="ECO:0007829|PDB:2DLC"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:2DLC"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:2DLC"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:2DLC"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:2DLC"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:2DLC"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:2DLC"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 305..313
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 319..343
FT /evidence="ECO:0007829|PDB:2DLC"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:2DLC"
SQ SEQUENCE 394 AA; 44020 MW; 57E8DB9BE6D054B7 CRC64;
MSSAATVDPN EAFGLITKNL QEVLNPQIIK DVLEVQKRHL KLYWGTAPTG RPHCGYFVPM
TKLADFLKAG CEVTVLLADL HAFLDNMKAP LEVVNYRAKY YELTIKAILR SINVPIEKLK
FVVGSSYQLT PDYTMDIFRL SNIVSQNDAK RAGADVVKQV ANPLLSGLIY PLMQALDEQF
LDVDCQFGGV DQRKIFVLAE ENLPSLGYKK RAHLMNPMVP GLAQGGKMSA SDPNSKIDLL
EEPKQVKKKI NSAFCSPGNV EENGLLSFVQ YVIAPIQELK FGTNHFEFFI DRPEKFGGPI
TYKSFEEMKL AFKEEKLSPP DLKIGVADAI NELLEPIRQE FANNKEFQEA SEKGYPVATP
QKSKKAKKPK NKGTKYPGAT KTNEIATKLE ETKL
