SYYM_HUMAN
ID SYYM_HUMAN Reviewed; 477 AA.
AC Q9Y2Z4; D3DUW8; Q9H817;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Tyrosine--tRNA ligase, mitochondrial;
DE EC=6.1.1.1 {ECO:0000269|PubMed:15779907, ECO:0000269|PubMed:17997975};
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS {ECO:0000303|PubMed:17997975};
DE Flags: Precursor;
GN Name=YARS2; ORFNames=CGI-04;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-191.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=15779907; DOI=10.1021/bi047527z;
RA Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C.,
RA Sissler M.;
RT "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases:
RT characterization of AspRS and TyrRS.";
RL Biochemistry 44:4805-4816(2005).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-355, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10] {ECO:0007744|PDB:2PID}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 32-375 IN COMPLEX WITH SUBSTRATE
RP ANALOG TYROSYLADENYLATE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND
RP MUTAGENESIS OF SER-200 AND GLN-202.
RX PubMed=17997975; DOI=10.1016/j.str.2007.09.018;
RA Bonnefond L., Frugier M., Touze E., Lorber B., Florentz C., Giege R.,
RA Sauter C., Rudinger-Thirion J.;
RT "Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals
RT common and idiosyncratic features.";
RL Structure 15:1505-1516(2007).
RN [11]
RP VARIANT MLASA2 LEU-52, AND CHARACTERIZATION OF VARIANT MLASA2 LEU-52.
RX PubMed=20598274; DOI=10.1016/j.ajhg.2010.06.001;
RA Riley L.G., Cooper S., Hickey P., Rudinger-Thirion J., McKenzie M.,
RA Compton A., Lim S.C., Thorburn D., Ryan M.T., Giege R., Bahlo M.,
RA Christodoulou J.;
RT "Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes
RT myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome.";
RL Am. J. Hum. Genet. 87:52-59(2010).
RN [12]
RP VARIANT MLASA2 ASP-46.
RX PubMed=22504945; DOI=10.1002/humu.22098;
RA Sasarman F., Nishimura T., Thiffault I., Shoubridge E.A.;
RT "A novel mutation in YARS2 causes myopathy with lactic acidosis and
RT sideroblastic anemia.";
RL Hum. Mutat. 33:1201-1206(2012).
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:15779907, ECO:0000269|PubMed:17997975}.
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:15779907, ECO:0000269|PubMed:17997975};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15779907,
CC ECO:0000269|PubMed:17997975}.
CC -!- INTERACTION:
CC Q9Y2Z4; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-1049286, EBI-11522760;
CC Q9Y2Z4; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-1049286, EBI-10175124;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:15779907}.
CC -!- DISEASE: Myopathy with lactic acidosis and sideroblastic anemia 2
CC (MLASA2) [MIM:613561]: A rare oxidative phosphorylation disorder
CC specific to skeletal muscle and bone marrow. Affected individuals
CC manifest sideroblastic anemia, progressive lethargy, muscle weakness,
CC and exercise intolerance associated with persistent lactic acidemia.
CC {ECO:0000269|PubMed:20598274, ECO:0000269|PubMed:22504945}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF132939; AAD27714.1; -; mRNA.
DR EMBL; AK024057; BAB14806.1; -; mRNA.
DR EMBL; AC087588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88517.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88518.1; -; Genomic_DNA.
DR EMBL; BC015625; AAH15625.1; -; mRNA.
DR CCDS; CCDS31770.1; -.
DR RefSeq; NP_001035526.1; NM_001040436.2.
DR PDB; 2PID; X-ray; 2.20 A; A/B=32-375.
DR PDB; 3ZXI; X-ray; 2.75 A; A/B=32-375.
DR PDBsum; 2PID; -.
DR PDBsum; 3ZXI; -.
DR AlphaFoldDB; Q9Y2Z4; -.
DR SMR; Q9Y2Z4; -.
DR BioGRID; 119258; 232.
DR DIP; DIP-29487N; -.
DR IntAct; Q9Y2Z4; 51.
DR MINT; Q9Y2Z4; -.
DR STRING; 9606.ENSP00000320658; -.
DR DrugBank; DB00135; Tyrosine.
DR iPTMnet; Q9Y2Z4; -.
DR PhosphoSitePlus; Q9Y2Z4; -.
DR SwissPalm; Q9Y2Z4; -.
DR BioMuta; YARS2; -.
DR DMDM; 50401709; -.
DR EPD; Q9Y2Z4; -.
DR jPOST; Q9Y2Z4; -.
DR MassIVE; Q9Y2Z4; -.
DR MaxQB; Q9Y2Z4; -.
DR PaxDb; Q9Y2Z4; -.
DR PeptideAtlas; Q9Y2Z4; -.
DR PRIDE; Q9Y2Z4; -.
DR ProteomicsDB; 85948; -.
DR ABCD; Q9Y2Z4; 2 sequenced antibodies.
DR Antibodypedia; 24801; 146 antibodies from 25 providers.
DR DNASU; 51067; -.
DR Ensembl; ENST00000324868.13; ENSP00000320658.8; ENSG00000139131.13.
DR GeneID; 51067; -.
DR KEGG; hsa:51067; -.
DR MANE-Select; ENST00000324868.13; ENSP00000320658.8; NM_001040436.3; NP_001035526.1.
DR UCSC; uc001rli.4; human.
DR CTD; 51067; -.
DR DisGeNET; 51067; -.
DR GeneCards; YARS2; -.
DR HGNC; HGNC:24249; YARS2.
DR HPA; ENSG00000139131; Low tissue specificity.
DR MalaCards; YARS2; -.
DR MIM; 610957; gene.
DR MIM; 613561; phenotype.
DR neXtProt; NX_Q9Y2Z4; -.
DR OpenTargets; ENSG00000139131; -.
DR Orphanet; 2598; Mitochondrial myopathy and sideroblastic anemia.
DR PharmGKB; PA142670559; -.
DR VEuPathDB; HostDB:ENSG00000139131; -.
DR eggNOG; KOG2623; Eukaryota.
DR GeneTree; ENSGT00390000013709; -.
DR InParanoid; Q9Y2Z4; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 914272at2759; -.
DR PhylomeDB; Q9Y2Z4; -.
DR TreeFam; TF105974; -.
DR BRENDA; 6.1.1.1; 2681.
DR PathwayCommons; Q9Y2Z4; -.
DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
DR SignaLink; Q9Y2Z4; -.
DR BioGRID-ORCS; 51067; 596 hits in 1086 CRISPR screens.
DR ChiTaRS; YARS2; human.
DR EvolutionaryTrace; Q9Y2Z4; -.
DR GenomeRNAi; 51067; -.
DR Pharos; Q9Y2Z4; Tbio.
DR PRO; PR:Q9Y2Z4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y2Z4; protein.
DR Bgee; ENSG00000139131; Expressed in oocyte and 193 other tissues.
DR ExpressionAtlas; Q9Y2Z4; baseline and differential.
DR Genevisible; Q9Y2Z4; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; TAS:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:BHF-UCL.
DR GO; GO:0072545; F:tyrosine binding; IDA:BHF-UCL.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IDA:BHF-UCL.
DR GO; GO:0070184; P:mitochondrial tyrosyl-tRNA aminoacylation; IMP:BHF-UCL.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR GO; GO:0043039; P:tRNA aminoacylation; IDA:BHF-UCL.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 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; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Disease variant; Ligase; Mitochondrion; Nucleotide-binding;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..477
FT /note="Tyrosine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035830"
FT MOTIF 82..91
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 281..285
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT BINDING 77
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:17997975,
FT ECO:0007744|PDB:2PID, ECO:0007744|PDB:3ZXI"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17997975,
FT ECO:0007744|PDB:2PID, ECO:0007744|PDB:3ZXI"
FT BINDING 121
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:17997975,
FT ECO:0007744|PDB:2PID, ECO:0007744|PDB:3ZXI"
FT BINDING 221
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:17997975,
FT ECO:0007744|PDB:2PID"
FT BINDING 225
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:17997975,
FT ECO:0007744|PDB:2PID"
FT BINDING 228
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:17997975,
FT ECO:0007744|PDB:2PID"
FT BINDING 244..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17997975,
FT ECO:0007744|PDB:2PID"
FT BINDING 247
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:17997975,
FT ECO:0007744|PDB:2PID"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17997975,
FT ECO:0007744|PDB:2PID, ECO:0007744|PDB:3ZXI"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 355
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 367
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYL4"
FT VARIANT 46
FT /note="G -> D (in MLASA2; dbSNP:rs587777213)"
FT /evidence="ECO:0000269|PubMed:22504945"
FT /id="VAR_068646"
FT VARIANT 52
FT /note="F -> L (in MLASA2; has a 2-fold reduction in
FT catalytic activity and a reduction in affinity for tRNA-tyr
FT resulting in an overall 9-fold loss of catalytic
FT efficiency; dbSNP:rs267607180)"
FT /evidence="ECO:0000269|PubMed:20598274"
FT /id="VAR_064188"
FT VARIANT 191
FT /note="G -> V (in dbSNP:rs11539445)"
FT /evidence="ECO:0000269|PubMed:10810093"
FT /id="VAR_034534"
FT MUTAGEN 200
FT /note="S->E: Loss of tRNA ligase activity."
FT /evidence="ECO:0000269|PubMed:17997975"
FT MUTAGEN 202
FT /note="Q->A: Mildly decreased tRNA ligase activity."
FT /evidence="ECO:0000269|PubMed:17997975"
FT CONFLICT 1..4
FT /note="MAAP -> MGA (in Ref. 1; AAD27714)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="R -> A (in Ref. 1; AAD27714)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="P -> T (in Ref. 1; AAD27714)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="D -> E (in Ref. 1; AAD27714)"
FT /evidence="ECO:0000305"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:2PID"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2PID"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2PID"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2PID"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:2PID"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 134..158
FT /evidence="ECO:0007829|PDB:2PID"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:2PID"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3ZXI"
FT HELIX 216..236
FT /evidence="ECO:0007829|PDB:2PID"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:2PID"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:2PID"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2PID"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 326..338
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2PID"
FT HELIX 344..372
FT /evidence="ECO:0007829|PDB:2PID"
SQ SEQUENCE 477 AA; 53199 MW; C513B8FE1E7A09E4 CRC64;
MAAPILRSFS WGRWSGTLNL SVLLPLGLRK AHSGAQGLLA AQKARGLFKD FFPETGTKIE
LPELFDRGTA SFPQTIYCGF DPTADSLHVG HLLALLGLFH LQRAGHNVIA LVGGATARLG
DPSGRTKERE ALETERVRAN ARALRLGLEA LAANHQQLFT DGRSWGSFTV LDNSAWYQKQ
HLVDFLAAVG GHFRMGTLLS RQSVQLRLKS PEGMSLAEFF YQVLQAYDFY YLFQRYGCRV
QLGGSDQLGN IMSGYEFINK LTGEDVFGIT VPLITSTTGA KLGKSAGNAV WLNRDKTSPF
ELYQFFVRQP DDSVERYLKL FTFLPLPEID HIMQLHVKEP ERRGPQKRLA AEVTKLVHGR
EGLDSAKRCT QALYHSSIDA LEVMSDQELK ELFKEAPFSE FFLDPGTSVL DTCRKANAIP
DGPRGYRMIT EGGVSINHQQ VTNPESVLIV GQHILKNGLS LLKIGKRNFY IIKWLQL
