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Tyrosine--tRNA ligase, chloroplastic/mitochondrial (EC 6.1.1.1) (Protein EMBRYO DEFECTIVE 2768) (Protein EMBRYONIC FACTOR 31) (Tyrosyl-tRNA synthetase) (TyrRS)

 SYYM_ARATH              Reviewed;         511 AA.
Q9M876;
22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 146.
RecName: Full=Tyrosine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
EC=6.1.1.1 {ECO:0000250|UniProtKB:Q9Y2Z4};
AltName: Full=Protein EMBRYO DEFECTIVE 2768 {ECO:0000303|PubMed:16297076};
AltName: Full=Protein EMBRYONIC FACTOR 31 {ECO:0000303|PubMed:22714903};
AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000305};
Short=TyrRS {ECO:0000305};
Flags: Precursor;
Name=EMB2768 {ECO:0000303|PubMed:16297076};
Synonyms=FAC31 {ECO:0000303|PubMed:22714903};
OrderedLocusNames=At3g02660 {ECO:0000312|Araport:AT3G02660};
ORFNames=F16B3.29 {ECO:0000312|EMBL:AAF32473.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
"Arabidopsis ORF Clones.";
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[5]
DISRUPTION PHENOTYPE.
PubMed=16297076; DOI=10.1111/j.1365-313X.2005.02580.x;
Berg M., Rogers R., Muralla R., Meinke D.;
"Requirement of aminoacyl-tRNA synthetases for gametogenesis and
embryo development in Arabidopsis.";
Plant J. 44:866-878(2005).
[6]
SUBCELLULAR LOCATION.
PubMed=16251277; DOI=10.1073/pnas.0504682102;
Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
"Dual targeting is the rule for organellar aminoacyl-tRNA synthetases
in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
[7]
DISRUPTION PHENOTYPE.
PubMed=22714903; DOI=10.1007/s11033-012-1678-9;
Jiang L., Wang S., Li H., Zhang G., Li H.;
"EMBRYONIC FACTOR 31 encodes a tyrosyl-tRNA synthetase that is
essential for seed development.";
Mol. Biol. Rep. 39:8297-8305(2012).
-!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a
two-step reaction: tyrosine is first activated by ATP to form Tyr-
AMP and then transferred to the acceptor end of tRNA(Tyr).
{ECO:0000250|UniProtKB:Q9Y2Z4}.
-!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP +
diphosphate + L-tyrosyl-tRNA(Tyr). {ECO:0000250|UniProtKB:Q9Y2Z4}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:16251277}. Mitochondrion
{ECO:0000269|PubMed:16251277}.
-!- DISRUPTION PHENOTYPE: Embryo defective. Developmental arrest of
the embryo at the preglobular stage. {ECO:0000269|PubMed:22714903,
ECO:0000305|PubMed:16297076}.
-!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC021640; AAF32473.1; -; Genomic_DNA.
EMBL; CP002686; AEE73845.1; -; Genomic_DNA.
EMBL; CP002686; ANM63412.1; -; Genomic_DNA.
EMBL; AK221609; BAD95182.1; -; mRNA.
EMBL; BT029296; ABK32110.1; -; mRNA.
RefSeq; NP_001325501.1; NM_001337429.1.
RefSeq; NP_186915.1; NM_111134.5.
UniGene; At.41099; -.
ProteinModelPortal; Q9M876; -.
SMR; Q9M876; -.
STRING; 3702.AT3G02660.1; -.
PaxDb; Q9M876; -.
PRIDE; Q9M876; -.
EnsemblPlants; AT3G02660.1; AT3G02660.1; AT3G02660.
EnsemblPlants; AT3G02660.2; AT3G02660.2; AT3G02660.
GeneID; 821282; -.
Gramene; AT3G02660.1; AT3G02660.1; AT3G02660.
Gramene; AT3G02660.2; AT3G02660.2; AT3G02660.
KEGG; ath:AT3G02660; -.
Araport; AT3G02660; -.
TAIR; locus:2076879; AT3G02660.
eggNOG; KOG2623; Eukaryota.
eggNOG; COG0162; LUCA.
HOGENOM; HOG000242790; -.
InParanoid; Q9M876; -.
KO; K01866; -.
OMA; VNYMMAK; -.
OrthoDB; EOG093607YA; -.
PhylomeDB; Q9M876; -.
PRO; PR:Q9M876; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9M876; baseline and differential.
Genevisible; Q9M876; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0004831; F:tyrosine-tRNA ligase activity; IBA:GO_Central.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central.
GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
CDD; cd00165; S4; 1.
CDD; cd00805; TyrRS_core; 1.
Gene3D; 3.10.290.10; -; 1.
Gene3D; 3.40.50.620; -; 1.
HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1.
InterPro; IPR001412; aa-tRNA-synth_I_CS.
InterPro; IPR002305; aa-tRNA-synth_Ic.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR002942; S4_RNA-bd.
InterPro; IPR036986; S4_RNA-bd_sf.
InterPro; IPR002307; Tyr-tRNA-ligase.
InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
InterPro; IPR024107; Tyr-tRNA-ligase_bac_1.
PANTHER; PTHR11766; PTHR11766; 1.
Pfam; PF01479; S4; 1.
Pfam; PF00579; tRNA-synt_1b; 1.
PRINTS; PR01040; TRNASYNTHTYR.
SMART; SM00363; S4; 1.
TIGRFAMs; TIGR00234; tyrS; 1.
PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PROSITE; PS50889; S4; 1.
2: Evidence at transcript level;
Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast;
Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Plastid;
Protein biosynthesis; Reference proteome; RNA-binding;
Transit peptide.
CHAIN 1 511 Tyrosine--tRNA ligase,
chloroplastic/mitochondrial.
{ECO:0000305}.
/FTId=PRO_0000433555.
TRANSIT 1 ? Chloroplast and mitochondrion.
{ECO:0000305}.
DOMAIN 444 510 S4 RNA-binding. {ECO:0000255|PROSITE-
ProRule:PRU00182}.
MOTIF 123 132 "HIGH" region. {ECO:0000305}.
MOTIF 318 322 "KMSKS" region. {ECO:0000305}.
BINDING 118 118 Tyrosine. {ECO:0000250|UniProtKB:P54577}.
BINDING 122 122 ATP. {ECO:0000250|UniProtKB:Q9Y2Z4}.
BINDING 162 162 Tyrosine. {ECO:0000250|UniProtKB:Q9Y2Z4}.
BINDING 256 256 Tyrosine. {ECO:0000250|UniProtKB:P54577}.
BINDING 260 260 Tyrosine. {ECO:0000250|UniProtKB:P54577}.
BINDING 263 263 Tyrosine. {ECO:0000250|UniProtKB:P54577}.
BINDING 282 282 Tyrosine. {ECO:0000250|UniProtKB:P54577}.
BINDING 321 321 ATP. {ECO:0000250}.
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


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