SYYM_ARATH
ID SYYM_ARATH Reviewed; 511 AA.
AC Q9M876;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Tyrosine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.1 {ECO:0000250|UniProtKB:Q9Y2Z4};
DE AltName: Full=Protein EMBRYO DEFECTIVE 2768 {ECO:0000303|PubMed:16297076};
DE AltName: Full=Protein EMBRYONIC FACTOR 31 {ECO:0000303|PubMed:22714903};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000305};
DE Short=TyrRS {ECO:0000305};
DE Flags: Precursor;
GN Name=EMB2768 {ECO:0000303|PubMed:16297076};
GN Synonyms=FAC31 {ECO:0000303|PubMed:22714903};
GN OrderedLocusNames=At3g02660 {ECO:0000312|Araport:AT3G02660};
GN ORFNames=F16B3.29 {ECO:0000312|EMBL:AAF32473.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=16297076; DOI=10.1111/j.1365-313x.2005.02580.x;
RA Berg M., Rogers R., Muralla R., Meinke D.;
RT "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo
RT development in Arabidopsis.";
RL Plant J. 44:866-878(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16251277; DOI=10.1073/pnas.0504682102;
RA Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
RA Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
RT "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=22714903; DOI=10.1007/s11033-012-1678-9;
RA Jiang L., Wang S., Li H., Zhang G., Li H.;
RT "EMBRYONIC FACTOR 31 encodes a tyrosyl-tRNA synthetase that is essential
RT for seed development.";
RL Mol. Biol. Rep. 39:8297-8305(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:0000250|UniProtKB:Q9Y2Z4}.
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:0000250|UniProtKB:Q9Y2Z4};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16251277}. Mitochondrion
CC {ECO:0000269|PubMed:16251277}.
CC -!- DISRUPTION PHENOTYPE: Embryo defective. Developmental arrest of the
CC embryo at the preglobular stage. {ECO:0000269|PubMed:22714903,
CC ECO:0000305|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AC021640; AAF32473.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73845.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63412.1; -; Genomic_DNA.
DR EMBL; AK221609; BAD95182.1; -; mRNA.
DR EMBL; BT029296; ABK32110.1; -; mRNA.
DR RefSeq; NP_001325501.1; NM_001337429.1.
DR RefSeq; NP_186915.1; NM_111134.5.
DR AlphaFoldDB; Q9M876; -.
DR SMR; Q9M876; -.
DR STRING; 3702.AT3G02660.1; -.
DR PaxDb; Q9M876; -.
DR PRIDE; Q9M876; -.
DR ProteomicsDB; 245302; -.
DR EnsemblPlants; AT3G02660.1; AT3G02660.1; AT3G02660.
DR EnsemblPlants; AT3G02660.2; AT3G02660.2; AT3G02660.
DR GeneID; 821282; -.
DR Gramene; AT3G02660.1; AT3G02660.1; AT3G02660.
DR Gramene; AT3G02660.2; AT3G02660.2; AT3G02660.
DR KEGG; ath:AT3G02660; -.
DR Araport; AT3G02660; -.
DR TAIR; locus:2076879; AT3G02660.
DR eggNOG; KOG2623; Eukaryota.
DR HOGENOM; CLU_024003_0_0_1; -.
DR InParanoid; Q9M876; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 914272at2759; -.
DR PhylomeDB; Q9M876; -.
DR PRO; PR:Q9M876; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M876; baseline and differential.
DR Genevisible; Q9M876; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00165; S4; 1.
DR CDD; cd00805; TyrRS_core; 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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Mitochondrion;
KW Nucleotide-binding; Plastid; Protein biosynthesis; Reference proteome;
KW RNA-binding; Transit peptide.
FT CHAIN 1..511
FT /note="Tyrosine--tRNA ligase, chloroplastic/mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433555"
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000305"
FT DOMAIN 444..510
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT MOTIF 123..132
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 318..322
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT BINDING 118
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 162
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 256
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 260
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 263
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 282
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 511 AA; 56619 MW; 43DECC2C66FF95DA CRC64;
MAYATGITFA SRSILPICSR TFLSPLRVAS LLVFPEKSSA TFFRRVQVPH LFSTSTTTLF
SSVKCSIHST SSPETENQAV FRPNVVDILE ERGLLESITS ENLRSACSDP KVAPLRVYCG
FDPTAESLHL GNLLGIIVLS WFQRCGHQAV GLIGGATGRV GDPSGKSLER PELDADTLEK
NIAGITKIII KILGSNPSPG GSYVIFNNYD WWKDMTMLDF LNKVGRFARV GTMMAKESVK
KRLESEQGMS YTEFTYQLLQ AYDFLHLFKN EGINVQIGGS DQWGNITAGT DLIRKILQAE
EAAYGLTFPL LLKNDGTKFG KSEDGAIWLS PSMLSPYKFY QYFFSVPDVD VIRFLKTLTF
LSLDEIKILE DQMSKPGYVP NTAQIKLAEE VTRFVHGEEG LKEAIKATEA LRPGAETKLD
WNLIERIAED IPSCSLPIDR VSGLSIVDLS VSAGLFESKS AARRMLKQGG FYMNNERVDD
ENKRVDEEDI VEGRGLVLSA GKKNKVVVRI S
