SYTM2_ARATH
ID SYTM2_ARATH Reviewed; 650 AA.
AC F4IFC5; Q56XW1;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Threonine--tRNA ligase, chloroplastic/mitochondrial 2 {ECO:0000305};
DE EC=6.1.1.3 {ECO:0000305};
DE AltName: Full=Protein EMBRYO DEFECTIVE 2761 {ECO:0000303|PubMed:16297076};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000305};
DE Short=ThrRS {ECO:0000305};
DE Flags: Precursor;
GN Name=EMB2761 {ECO:0000303|PubMed:16297076};
GN OrderedLocusNames=At2g04842 {ECO:0000312|Araport:AT2G04842};
GN ORFNames=F28I8 {ECO:0000312|EMBL:AC006955};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [5]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC Evidence={ECO:0000305};
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 globular stage. {ECO:0000305|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94986.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC006955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC05873.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63276.1; -; Genomic_DNA.
DR EMBL; AK221562; BAD94986.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001318198.1; NM_001335263.1.
DR RefSeq; NP_671778.1; NM_147245.2.
DR AlphaFoldDB; F4IFC5; -.
DR BMRB; F4IFC5; -.
DR SMR; F4IFC5; -.
DR IntAct; F4IFC5; 1.
DR MINT; F4IFC5; -.
DR STRING; 3702.AT2G04842.1; -.
DR PaxDb; F4IFC5; -.
DR PRIDE; F4IFC5; -.
DR ProteomicsDB; 233023; -.
DR EnsemblPlants; AT2G04842.1; AT2G04842.1; AT2G04842.
DR EnsemblPlants; AT2G04842.2; AT2G04842.2; AT2G04842.
DR GeneID; 815029; -.
DR Gramene; AT2G04842.1; AT2G04842.1; AT2G04842.
DR Gramene; AT2G04842.2; AT2G04842.2; AT2G04842.
DR KEGG; ath:AT2G04842; -.
DR Araport; AT2G04842; -.
DR TAIR; locus:504956029; AT2G04842.
DR eggNOG; KOG1637; Eukaryota.
DR HOGENOM; CLU_008554_0_1_1; -.
DR InParanoid; F4IFC5; -.
DR OMA; DAHIFML; -.
DR OrthoDB; 813937at2759; -.
DR BRENDA; 6.1.1.3; 399.
DR PRO; PR:F4IFC5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IFC5; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Plastid; Protein biosynthesis;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..650
FT /note="Threonine--tRNA ligase, chloroplastic/mitochondrial
FT 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433549"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 461
FT /note="K -> R (in Ref. 3; BAD94986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 74785 MW; 66EA72022DD35AFE CRC64;
MASSHSLLFS SSFLSKPSSF TSSLRRFVYL PTRQFWPRQR HGFSTVFAVA TEPAISSSGP
KKAEPSTVVL PSNESSDKLL KIRHTCAHVM AMAVQKLFPD AKVTIGPWID NGFYYDFDME
PLTDKDLKRI KKEMDRIISR NLPLLREEVS REEAKKRIMA INEPYKMEIL DGIKEEPITV
YHIGNEWWDL CAGPHVETTG KINKKAVELE SVAGAYWRGD EKRQMLQRIY GTAWESEEQL
KAYLHFKEEA KRRDHRRIGQ DLDLFSIQDE AGGGLVFWHP KGAIVRNIIE ESWKKMHVEH
GYDLIYTPHV AKADLWKISG HLDFYRENMY DQMEIEDELY QLRPMNCPYH ILLYQRKRQS
YRDLPIRVAE LGTVYRYELS GSLHGLFRVR GFTQDDAHIF CLEDQIKDEI RGVLDLTEEI
LSRFGFNKYE VNLSTRPEKS VGGDDIWEKA TCALRDALDD KGWSYEVDEG GGAFYGPKID
LKIEDALGRK WQCSTIQVDF NLPQRFDITY VDTNSDKKRP IMIHRAVLGS LERFFGVLIE
HYAGDFPLWL SPVQVRVLPV TDNQLEFCKE VSKKLRACGV RAELCHGERL PKLIRNAETQ
KIPLMAVVGP KEVETGTVTV RSRFGGELGT IPVDDLINKI NIAVETRTAL
