SYTM1_ARATH
ID SYTM1_ARATH Reviewed; 709 AA.
AC O04630; O81907; Q84TG4; Q94AG0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Threonine--tRNA ligase, mitochondrial 1 {ECO:0000305};
DE EC=6.1.1.3 {ECO:0000305};
DE AltName: Full=AtSYT1 {ECO:0000303|PubMed:10583378};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000305};
DE Short=ThrRS {ECO:0000305};
DE Flags: Precursor;
GN Name=THRRS {ECO:0000303|Ref.1}; OrderedLocusNames=At5g26830;
GN ORFNames=F2P16.7;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Ovesna J., Naneva H., Cosset A., Duchene A.-M., Marechal-Drouard L.,
RA Dietrich A., Souciet G.;
RT "Isolation of a cDNA encoding the cytosolic and the mitochondrial form of
RT threonyl-tRNA synthetase in Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-169(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=10583378; DOI=10.1046/j.1432-1327.1999.00922.x;
RA Souciet G., Menand B., Ovesna J., Cosset A., Dietrich A., Wintz H.;
RT "Characterization of two bifunctional Arabdopsis thaliana genes coding for
RT mitochondrial and cytosolic forms of valyl-tRNA synthetase and threonyl-
RT tRNA synthetase by alternative use of two in-frame AUGs.";
RL Eur. J. Biochem. 266:848-854(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
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: Mitochondrion {ECO:0000269|PubMed:10583378}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:10583378}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=O04630-1; Sequence=Displayed;
CC Name=Cytoplasmic;
CC IsoId=O04630-2; Sequence=VSP_018908;
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61048.1; Type=Erroneous gene model prediction; Evidence={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; Y14329; CAA74705.1; -; mRNA.
DR EMBL; AF007270; AAB61048.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93610.1; -; Genomic_DNA.
DR EMBL; AY048205; AAK82468.1; -; mRNA.
DR EMBL; BT005825; AAO64760.1; -; mRNA.
DR PIR; T01763; T01763.
DR PIR; T51624; T51624.
DR RefSeq; NP_198035.2; NM_122565.3. [O04630-1]
DR AlphaFoldDB; O04630; -.
DR SMR; O04630; -.
DR BioGRID; 18016; 17.
DR IntAct; O04630; 2.
DR STRING; 3702.AT5G26830.1; -.
DR PaxDb; O04630; -.
DR PRIDE; O04630; -.
DR ProteomicsDB; 234108; -. [O04630-1]
DR EnsemblPlants; AT5G26830.1; AT5G26830.1; AT5G26830. [O04630-1]
DR GeneID; 832741; -.
DR Gramene; AT5G26830.1; AT5G26830.1; AT5G26830. [O04630-1]
DR KEGG; ath:AT5G26830; -.
DR Araport; AT5G26830; -.
DR TAIR; locus:2148538; AT5G26830.
DR eggNOG; KOG1637; Eukaryota.
DR HOGENOM; CLU_008554_0_2_1; -.
DR InParanoid; O04630; -.
DR OMA; IWDEAEK; -.
DR OrthoDB; 813937at2759; -.
DR PhylomeDB; O04630; -.
DR PRO; PR:O04630; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O04630; baseline and differential.
DR Genevisible; O04630; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA: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:0006435; P:threonyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 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; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
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; PF02824; TGS; 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 SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Ligase; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..709
FT /note="Threonine--tRNA ligase, mitochondrial 1"
FT /id="PRO_0000035824"
FT DOMAIN 73..135
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 584
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000305"
FT /id="VSP_018908"
FT CONFLICT 121
FT /note="M -> V (in Ref. 4; AAK82468/AAO64760)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="M -> L (in Ref. 1; CAA74705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 80936 MW; A74FFFD7A6B0B5CF CRC64;
MLLRLTARSI RRFTTSSSSL PLLSSSSFCT VPTMAANHPK DEAYLSAVIP KRIKLFEQIQ
ANQLENLKSL PHDPIKVTLP DGNVKEGKKW ETTPMDIAAQ ISKGLANSAL ISAVDDVLWD
MNRPLEGDCK LELFKFDSDK GRDTLWHSSA HILGQALEQE YGCQLCIGPC TTRGEGFYYD
GFYGELGLSD NHFPSIEAGA AKAAKEAQPF ERIEVTKDQA LEMFSENNFK VELINGLPAD
MTITVYRCGP LVDLCRGPHI PNTSFVKAFK CLRASSAYWK GDKDRESLQR VYGISYPDQK
QLKKYLQFLE EAKKYDHRLL GQKQELFFSH QLSPGSYFFL PLGTRVYNRL MDFIKNQYWH
RGYTEVITPN MYNMELWQTS GHADNYKDNM FTFNIEKQEF GLKPMNCPGH CLIFQHRVRS
YRELPMRLAD FGVLHRNEAS GALSGLTRVR RFQQDDAHIF CTTEQVKGEV QGVLEFIDYV
YKVFGFTYEL KLSTRPEKYL GDLETWDKAE ADLKEAIEAF GKPLVLNEGD GAFYGPKIDI
TVSDAMNRKF QCATLQLDFQ LPIRFNLEYA AEDEAKKSRP VMIHRAVLGS VERMFAILLE
HYKGKWPFWI SPRQAIVCPI SEKSQQYAEK VQKQIKDAGF YVDADLTDRK IDKKVREAQL
AQYNYILVVG ETEAATGQVS VRVRDNAAHS VKSIEDLLEE FKAKTAEFV
