SYEC_YEAST
ID SYEC_YEAST Reviewed; 708 AA.
AC P46655; D6VV90;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Glutamate--tRNA ligase, cytoplasmic;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase;
DE Short=(c)ERS;
DE Short=GluRS;
DE AltName: Full=P85;
GN Name=GUS1; OrderedLocusNames=YGL245W; ORFNames=G0583, HRB724;
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 [GENOMIC DNA].
RA Frantz J.D., Gilbert W.;
RT "Isolation and sequence characterization of the gene encoding the yeast
RT cytosolic glutamyl-tRNA synthetase.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8750240; DOI=10.1002/yea.320111507;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left
RT arm of chromosome VII, reveals the presence of eight open reading frames.";
RL Yeast 11:1519-1523(1995).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972578;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1555::aid-yea43>3.0.co;2-q;
RA Coissac E., Maillier E., Robineau S., Netter P.;
RT "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome
RT VII of Saccharomyces cerevisiae.";
RL Yeast 12:1555-1562(1996).
RN [6]
RP INTERACTION WITH ARC1.
RX PubMed=8895587; DOI=10.1002/j.1460-2075.1996.tb00927.x;
RA Simos G., Segref A., Fasiolo F., Hellmuth K., Shevshenko A., Mann M.,
RA Hurt E.C.;
RT "The yeast protein Arc1p binds to tRNA and functions as a cofactor for the
RT methionyl- and glutamyl-tRNA synthetases.";
RL EMBO J. 15:5437-5448(1996).
RN [7]
RP INTERACTION WITH ARC1.
RX PubMed=9659920; DOI=10.1016/s1097-2765(00)80024-6;
RA Simos G., Sauer A., Fasiolo F., Hurt E.C.;
RT "A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA
RT synthetases.";
RL Mol. Cell 1:235-242(1998).
RN [8]
RP SUBUNIT, INTERACTION WITH ARC1, AND SUBCELLULAR LOCATION.
RX PubMed=11726524; DOI=10.1093/emboj/20.23.6889;
RA Galani K., Grosshans H., Deinert K., Hurt E.C., Simos G.;
RT "The intracellular location of two aminoacyl-tRNA synthetases depends on
RT complex formation with Arc1p.";
RL EMBO J. 20:6889-6898(2001).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11069915; DOI=10.1074/jbc.m008682200;
RA Deinert K., Fasiolo F., Hurt E.C., Simos G.;
RT "Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes
RT its interaction with the cognate tRNAs.";
RL J. Biol. Chem. 276:6000-6008(2001).
RN [10]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [11]
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-300, AND IDENTIFICATION BY
RP 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 [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19417106; DOI=10.1101/gad.518109;
RA Frechin M., Senger B., Braye M., Kern D., Martin R.P., Becker H.D.;
RT "Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated
RT transamidation pathway involving Arc1p-controlled subcellular sorting of
RT cytosolic GluRS.";
RL Genes Dev. 23:1119-1130(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-191, AND INTERACTION WITH ARC1.
RX PubMed=17139087; DOI=10.1107/s0907444906039850;
RA Simader H., Hothorn M., Suck D.;
RT "Structures of the interacting domains from yeast glutamyl-tRNA synthetase
RT and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel
RT function for an old fold.";
RL Acta Crystallogr. D 62:1510-1519(2006).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-191 IN COMPLEX WITH ARC1, AND
RP MUTAGENESIS OF ARG-148.
RX PubMed=16914447; DOI=10.1093/nar/gkl560;
RA Simader H., Hothorn M., Koehler C., Basquin J., Simos G., Suck D.;
RT "Structural basis of yeast aminoacyl-tRNA synthetase complex formation
RT revealed by crystal structures of two binary sub-complexes.";
RL Nucleic Acids Res. 34:3968-3979(2006).
CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC then transferred to the acceptor end of tRNA(Glu). In mitochondria,
CC constitutes the nondiscriminating glutamyl-tRNA synthase that generates
CC the mitochondrial mischarged glutamyl-tRNA(Gln) substrate for the tRNA-
CC dependent amidotransferase (AdT), which generates mitochondrial
CC glutaminyl-tRNA(Gln) by transamidation of glutamyl-tRNA(Gln).
CC {ECO:0000269|PubMed:11069915, ECO:0000269|PubMed:19417106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; EC=6.1.1.17;
CC Evidence={ECO:0000269|PubMed:11069915};
CC -!- SUBUNIT: Component of a yeast aminoacyl-tRNA synthase (aaRS) complex
CC formed by methionyl-tRNA synthase MES1, glutamyl-tRNA synthase GUS1 and
CC the tRNA aminoacylation cofactor ARC1 in a stoichiometric complex.
CC Interacts (via N-ter) with ARC1 (via N-ter). Can also form a stable
CC binary complex with ARC1 that is functional in terms of aminoacylation.
CC ARC1 increases the affinity for cognate tRNAs due to the presence of a
CC tRNA binding domain in the middle and C-terminal part of ARC1.
CC {ECO:0000269|PubMed:11726524, ECO:0000269|PubMed:16914447,
CC ECO:0000269|PubMed:17139087, ECO:0000269|PubMed:8895587,
CC ECO:0000269|PubMed:9659920}.
CC -!- INTERACTION:
CC P46655; P46672: ARC1; NbExp=7; IntAct=EBI-18665, EBI-7224;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Note=Largely excluded
CC from the nucleus.
CC -!- MISCELLANEOUS: Present with 48700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA78905.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA78905.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA64142.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA89009.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA96964.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U32265; AAA78905.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z49149; CAA89009.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z72767; CAA96964.1; ALT_INIT; Genomic_DNA.
DR EMBL; X94357; CAA64142.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006941; DAA07874.1; -; Genomic_DNA.
DR PIR; S53934; S53934.
DR RefSeq; NP_011269.2; NM_001181111.1.
DR PDB; 2HRA; X-ray; 1.90 A; A/B=1-191.
DR PDB; 2HRK; X-ray; 2.05 A; A=1-191.
DR PDB; 2HSM; X-ray; 3.00 A; A=1-191.
DR PDBsum; 2HRA; -.
DR PDBsum; 2HRK; -.
DR PDBsum; 2HSM; -.
DR AlphaFoldDB; P46655; -.
DR SMR; P46655; -.
DR BioGRID; 32995; 393.
DR ComplexPortal; CPX-1947; Methionyl glutamyl tRNA synthetase complex.
DR DIP; DIP-2212N; -.
DR IntAct; P46655; 48.
DR MINT; P46655; -.
DR STRING; 4932.YGL245W; -.
DR iPTMnet; P46655; -.
DR MaxQB; P46655; -.
DR PaxDb; P46655; -.
DR PRIDE; P46655; -.
DR EnsemblFungi; YGL245W_mRNA; YGL245W; YGL245W.
DR GeneID; 852606; -.
DR KEGG; sce:YGL245W; -.
DR SGD; S000003214; GUS1.
DR VEuPathDB; FungiDB:YGL245W; -.
DR eggNOG; KOG1147; Eukaryota.
DR GeneTree; ENSGT00550000074815; -.
DR HOGENOM; CLU_001882_1_2_1; -.
DR InParanoid; P46655; -.
DR OMA; NLTRWFT; -.
DR BioCyc; YEAST:G3O-30716-MON; -.
DR BRENDA; 6.1.1.17; 984.
DR SABIO-RK; P46655; -.
DR EvolutionaryTrace; P46655; -.
DR PRO; PR:P46655; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P46655; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IDA:SGD.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IC:ComplexPortal.
DR Gene3D; 1.10.1160.10; -; 1.
DR Gene3D; 2.40.240.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00463; gltX_arch; 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 Mitochondrion; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..708
FT /note="Glutamate--tRNA ligase, cytoplasmic"
FT /id="PRO_0000119739"
FT REGION 106..115
FT /note="Interaction with ARC1"
FT REGION 141..157
FT /note="Interaction with ARC1"
FT MOTIF 210..219
FT /note="'HIGH' region"
FT MOTIF 437..441
FT /note="'KMSKS' region"
FT BINDING 205..207
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 382..386
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 437..441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 148
FT /note="R->A: Abolishes interaction with ARC1."
FT /evidence="ECO:0000269|PubMed:16914447"
FT CONFLICT 209
FT /note="E -> D (in Ref. 1; AAA78905)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="V -> A (in Ref. 1; AAA78905)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="P -> S (in Ref. 1; AAA78905)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="V -> M (in Ref. 1; AAA78905)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2HRA"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:2HRA"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2HRA"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2HSM"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2HRA"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:2HRA"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:2HRA"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:2HRA"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:2HRA"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:2HRA"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2HRK"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:2HRA"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:2HRA"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:2HRA"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:2HRA"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:2HRA"
SQ SEQUENCE 708 AA; 80843 MW; EADAD430A2D98974 CRC64;
MPSTLTINGK APIVAYAELI AARIVNALAP NSIAIKLVDD KKAPAAKLDD ATEDVFNKIT
SKFAAIFDNG DKEQVAKWVN LAQKELVIKN FAKLSQSLET LDSQLNLRTF ILGGLKYSAA
DVACWGALRS NGMCGSIIKN KVDVNVSRWY TLLEMDPIFG EAHDFLSKSL LELKKSANVG
KKKETHKANF EIDLPDAKMG EVVTRFPPEP SGYLHIGHAK AALLNQYFAQ AYKGKLIIRF
DDTNPSKEKE EFQDSILEDL DLLGIKGDRI TYSSDYFQEM YDYCVQMIKD GKAYCDDTPT
EKMREERMDG VASARRDRSV EENLRIFTEE MKNGTEEGLK NCVRAKIDYK ALNKTLRDPV
IYRCNLTPHH RTGSTWKIYP TYDFCVPIVD AIEGVTHALR TIEYRDRNAQ YDWMLQALRL
RKVHIWDFAR INFVRTLLSK RKLQWMVDKD LVGNWDDPRF PTVRGVRRRG MTVEGLRNFV
LSQGPSRNVI NLEWNLIWAF NKKVIDPIAP RHTAIVNPVK IHLEGSEAPQ EPKIEMKPKH
KKNPAVGEKK VIYYKDIVVD KDDADVINVD EEVTLMDWGN VIITKKNDDG SMVAKLNLEG
DFKKTKHKLT WLADTKDVVP VDLVDFDHLI TKDRLEEDES FEDFLTPQTE FHTDAIADLN
VKDMKIGDII QFERKGYYRL DALPKDGKPY VFFTIPDGKS VNKYGAKK
