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Protein

Threonine--tRNA ligase, mitochondrial 1

Gene

THRRS

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi407 – 4071Zinc; catalyticBy similarity
Metal bindingi458 – 4581Zinc; catalyticBy similarity
Metal bindingi584 – 5841Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT5G26830-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine--tRNA ligase, mitochondrial 1Curated (EC:6.1.1.3Curated)
Alternative name(s):
AtSYT11 Publication
Threonyl-tRNA synthetaseCurated
Short name:
ThrRSCurated
Gene namesi
Name:THRRS1 Publication
Ordered Locus Names:At5g26830
ORF Names:F2P16.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G26830.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
  • chloroplast Source: TAIR
  • cytoplasm Source: GO_Central
  • cytosol Source: TAIR
  • membrane Source: TAIR
  • mitochondrion Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121MitochondrionSequence analysisAdd
BLAST
Chaini22 – 709688Threonine--tRNA ligase, mitochondrial 1PRO_0000035824Add
BLAST

Proteomic databases

PaxDbiO04630.
PRIDEiO04630.

Expressioni

Gene expression databases

GenevisibleiO04630. AT.

Interactioni

Protein-protein interaction databases

BioGridi18016. 4 interactions.
IntActiO04630. 1 interaction.
STRINGi3702.AT5G26830.1.

Structurei

3D structure databases

ProteinModelPortaliO04630.
SMRiO04630. Positions 74-707.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1637. Eukaryota.
COG0441. LUCA.
HOGENOMiHOG000003878.
InParanoidiO04630.
KOiK01868.
OMAiFKLEYMS.
PhylomeDBiO04630.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR01047. TRNASYNTHTHR.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00418. thrS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Mitochondrial (identifier: O04630-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLLRLTARSI RRFTTSSSSL PLLSSSSFCT VPTMAANHPK DEAYLSAVIP
60 70 80 90 100
KRIKLFEQIQ ANQLENLKSL PHDPIKVTLP DGNVKEGKKW ETTPMDIAAQ
110 120 130 140 150
ISKGLANSAL ISAVDDVLWD MNRPLEGDCK LELFKFDSDK GRDTLWHSSA
160 170 180 190 200
HILGQALEQE YGCQLCIGPC TTRGEGFYYD GFYGELGLSD NHFPSIEAGA
210 220 230 240 250
AKAAKEAQPF ERIEVTKDQA LEMFSENNFK VELINGLPAD MTITVYRCGP
260 270 280 290 300
LVDLCRGPHI PNTSFVKAFK CLRASSAYWK GDKDRESLQR VYGISYPDQK
310 320 330 340 350
QLKKYLQFLE EAKKYDHRLL GQKQELFFSH QLSPGSYFFL PLGTRVYNRL
360 370 380 390 400
MDFIKNQYWH RGYTEVITPN MYNMELWQTS GHADNYKDNM FTFNIEKQEF
410 420 430 440 450
GLKPMNCPGH CLIFQHRVRS YRELPMRLAD FGVLHRNEAS GALSGLTRVR
460 470 480 490 500
RFQQDDAHIF CTTEQVKGEV QGVLEFIDYV YKVFGFTYEL KLSTRPEKYL
510 520 530 540 550
GDLETWDKAE ADLKEAIEAF GKPLVLNEGD GAFYGPKIDI TVSDAMNRKF
560 570 580 590 600
QCATLQLDFQ LPIRFNLEYA AEDEAKKSRP VMIHRAVLGS VERMFAILLE
610 620 630 640 650
HYKGKWPFWI SPRQAIVCPI SEKSQQYAEK VQKQIKDAGF YVDADLTDRK
660 670 680 690 700
IDKKVREAQL AQYNYILVVG ETEAATGQVS VRVRDNAAHS VKSIEDLLEE

FKAKTAEFV
Length:709
Mass (Da):80,936
Last modified:January 10, 2003 - v3
Checksum:iA74FFFD7A6B0B5CF
GO
Isoform Cytoplasmic (identifier: O04630-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Show »
Length:676
Mass (Da):77,337
Checksum:iB57A2A7581BFA4C5
GO

Sequence cautioni

The sequence AAB61048.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211M → V in AAK82468 (PubMed:14593172).Curated
Sequence conflicti121 – 1211M → V in AAO64760 (PubMed:14593172).Curated
Sequence conflicti426 – 4261M → L in CAA74705 (Ref. 1) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333Missing in isoform Cytoplasmic. CuratedVSP_018908Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14329 mRNA. Translation: CAA74705.1.
AF007270 Genomic DNA. Translation: AAB61048.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED93610.1.
AY048205 mRNA. Translation: AAK82468.1.
BT005825 mRNA. Translation: AAO64760.1.
PIRiT01763.
T51624.
RefSeqiNP_198035.2. NM_122565.2. [O04630-1]
UniGeneiAt.23575.
At.55026.

Genome annotation databases

EnsemblPlantsiAT5G26830.1; AT5G26830.1; AT5G26830. [O04630-1]
GeneIDi832741.
KEGGiath:AT5G26830.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14329 mRNA. Translation: CAA74705.1.
AF007270 Genomic DNA. Translation: AAB61048.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED93610.1.
AY048205 mRNA. Translation: AAK82468.1.
BT005825 mRNA. Translation: AAO64760.1.
PIRiT01763.
T51624.
RefSeqiNP_198035.2. NM_122565.2. [O04630-1]
UniGeneiAt.23575.
At.55026.

3D structure databases

ProteinModelPortaliO04630.
SMRiO04630. Positions 74-707.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi18016. 4 interactions.
IntActiO04630. 1 interaction.
STRINGi3702.AT5G26830.1.

Proteomic databases

PaxDbiO04630.
PRIDEiO04630.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G26830.1; AT5G26830.1; AT5G26830. [O04630-1]
GeneIDi832741.
KEGGiath:AT5G26830.

Organism-specific databases

TAIRiAT5G26830.

Phylogenomic databases

eggNOGiKOG1637. Eukaryota.
COG0441. LUCA.
HOGENOMiHOG000003878.
InParanoidiO04630.
KOiK01868.
OMAiFKLEYMS.
PhylomeDBiO04630.

Enzyme and pathway databases

BioCyciARA:AT5G26830-MONOMER.

Miscellaneous databases

PROiO04630.

Gene expression databases

GenevisibleiO04630. AT.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR01047. TRNASYNTHTHR.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00418. thrS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a cDNA encoding the cytosolic and the mitochondrial form of threonyl-tRNA synthetase in Arabidopsis thaliana."
    Ovesna J., Naneva H., Cosset A., Duchene A.-M., Marechal-Drouard L., Dietrich A., Souciet G.
    Plant Gene Register PGR99-169
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Characterization of two bifunctional Arabdopsis thaliana genes coding for mitochondrial and cytosolic forms of valyl-tRNA synthetase and threonyl-tRNA synthetase by alternative use of two in-frame AUGs."
    Souciet G., Menand B., Ovesna J., Cosset A., Dietrich A., Wintz H.
    Eur. J. Biochem. 266:848-854(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSYTM1_ARATH
AccessioniPrimary (citable) accession number: O04630
Secondary accession number(s): O81907, Q84TG4, Q94AG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 10, 2003
Last modified: July 6, 2016
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.