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O04630 (SYTM_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Threonine--tRNA ligase, mitochondrial
EC=6.1.1.3
Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS
Gene names
Name:THRRS
Ordered Locus Names:At5g26830
ORF Names:F2P16.7
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length709 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Mitochondrion. Cytoplasm.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Sequence caution

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
Mitochondrion
   Coding sequence diversityAlternative initiation
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processthreonyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell wall

Inferred from direct assay. Source: TAIR

chloroplast

Inferred from direct assay. Source: TAIR

cytosol

Inferred from direct assay. Source: TAIR

mitochondrion

Inferred from direct assay. Source: TAIR

plasma membrane

Inferred from direct assay. Source: TAIR

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

threonine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Mitochondrial (identifier: O04630-1)

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.
Isoform Cytoplasmic (identifier: O04630-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion Potential
Chain22 – 709688Threonine--tRNA ligase, mitochondrial
PRO_0000035824

Natural variations

Alternative sequence1 – 3333Missing in isoform Cytoplasmic.
VSP_018908

Experimental info

Sequence conflict1211M → V in AAK82468. Ref.4
Sequence conflict1211M → V in AAO64760. Ref.4
Sequence conflict4261M → L in CAA74705. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Mitochondrial [UniParc].

Last modified January 10, 2003. Version 3.
Checksum: A74FFFD7A6B0B5CF

FASTA70980,936
        10         20         30         40         50         60 
MLLRLTARSI RRFTTSSSSL PLLSSSSFCT VPTMAANHPK DEAYLSAVIP KRIKLFEQIQ 

        70         80         90        100        110        120 
ANQLENLKSL PHDPIKVTLP DGNVKEGKKW ETTPMDIAAQ ISKGLANSAL ISAVDDVLWD 

       130        140        150        160        170        180 
MNRPLEGDCK LELFKFDSDK GRDTLWHSSA HILGQALEQE YGCQLCIGPC TTRGEGFYYD 

       190        200        210        220        230        240 
GFYGELGLSD NHFPSIEAGA AKAAKEAQPF ERIEVTKDQA LEMFSENNFK VELINGLPAD 

       250        260        270        280        290        300 
MTITVYRCGP LVDLCRGPHI PNTSFVKAFK CLRASSAYWK GDKDRESLQR VYGISYPDQK 

       310        320        330        340        350        360 
QLKKYLQFLE EAKKYDHRLL GQKQELFFSH QLSPGSYFFL PLGTRVYNRL MDFIKNQYWH 

       370        380        390        400        410        420 
RGYTEVITPN MYNMELWQTS GHADNYKDNM FTFNIEKQEF GLKPMNCPGH CLIFQHRVRS 

       430        440        450        460        470        480 
YRELPMRLAD FGVLHRNEAS GALSGLTRVR RFQQDDAHIF CTTEQVKGEV QGVLEFIDYV 

       490        500        510        520        530        540 
YKVFGFTYEL KLSTRPEKYL GDLETWDKAE ADLKEAIEAF GKPLVLNEGD GAFYGPKIDI 

       550        560        570        580        590        600 
TVSDAMNRKF QCATLQLDFQ LPIRFNLEYA AEDEAKKSRP VMIHRAVLGS VERMFAILLE 

       610        620        630        640        650        660 
HYKGKWPFWI SPRQAIVCPI SEKSQQYAEK VQKQIKDAGF YVDADLTDRK IDKKVREAQL 

       670        680        690        700 
AQYNYILVVG ETEAATGQVS VRVRDNAAHS VKSIEDLLEE FKAKTAEFV

« Hide

Isoform Cytoplasmic [UniParc].

Checksum: B57A2A7581BFA4C5
Show »

FASTA67677,337

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 11130714] [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. expand/collapse author list , 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00531047.
IPI00760335.
PIRT01763.
T51624.
RefSeqNP_198035.2. NM_122565.2.
UniGeneAt.23575.
At.55026.

3D structure databases

ProteinModelPortalO04630.
SMRO04630. Positions 69-708.
ModBaseSearch...

Protein-protein interaction databases

IntActO04630. 1 interaction.
STRINGO04630.

Proteomic databases

PRIDEO04630.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G26830.1; AT5G26830.1; AT5G26830.
GeneID832741.
GenomeReviewsGene locus AT5G26830 in contig BA000015_GR.
KEGGath:AT5G26830.
NMPDRfig|3702.1.peg.24884.

Organism-specific databases

GeneFarm2462. 210.
TAIRAt5g26830.

Phylogenomic databases

eggNOGKOG1637.
GeneTreeEPGT00070000029226.
HOGENOMHBG352811.
InParanoidO04630.
OMAHYAENMF.
PhylomeDBO04630.
ProtClustDBPLN02908.

Gene expression databases

ArrayExpressO04630.
GenevestigatorO04630.
GermOnlineAT5G26830. Arabidopsis thaliana.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_ferredoxin-type.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-synth_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KOK01868.
PfamPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF81271. TGS-like. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR00418. ThrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYTM_ARATH
AccessionPrimary (citable) accession number: O04630
Secondary accession number(s): O81907, Q84TG4, Q94AG0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 10, 2003
Last modified: January 25, 2012
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents