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Reviewed, UniProtKB/Swiss-Prot Q5XHY5 (SYTC_RAT)

Last modified February 9, 2010. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Threonyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.3
Alternative name(s):
    Threonine--tRNA ligase
      Short name=ThrRS
Gene names
Name: Tars
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length695 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
Gene Ontology (GO)
   Biological processthreonyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

threonine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 695695Threonyl-tRNA synthetase, cytoplasmic
PRO_0000101121

Amino acid modifications

Modified residue2151N6-acetyllysine By similarity
Modified residue2701Phosphotyrosine By similarity
Cross-link194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5XHY5-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: B282CF7F5F47363A

FASTA69580,576
        10         20         30         40         50         60 
MSEEKASSPS GKMDGEKPLN PWPEYINTRL DMYHKLKAEH DSILAEKAAK DSKPIKVTLP 

        70         80         90        100        110        120 
DGKQVDAESW KTTPYQIACG ISQGLADNTV VAKVNKVVWD LDRPLETDCT LELLKFEDEE 

       130        140        150        160        170        180 
AQAVYWHSSA HIMGEAMERV YGGCLCYGPP IENGFYYDMY LEEGGVSSND FSSLETLCKK 

       190        200        210        220        230        240 
IIKEKQTFER LEVKKETLLE MFKYNKFKCR ILNEKVNTPT TTVYRCGPLI DLCRGPHVRH 

       250        260        270        280        290        300 
TGKIKTLKIH KNSSTYWEGK ADMETLQRIY GISFPDPKLL KEWEKFQEEA KNRDHRKIGR 

       310        320        330        340        350        360 
DQELYFFHEL SPGSCFFLPK GAYIYNTLME FIRSEYRKRG FQEVVTPNIF NSRLWMTSGH 

       370        380        390        400        410        420 
WQHYSENMFS FEVEKEQFAL KPMNCPGHCL MFDHRPRSWR ELPLRLADFG VLHRNELSGA 

       430        440        450        460        470        480 
LTGLTRVRRF QQDDAHIFCA MEQIEDEIKG CLDFLRTVYS VFGFSFKLNL STRPEKFLGD 

       490        500        510        520        530        540 
IEIWNQAEKQ LENSLNEFGE KWELNPGDGA FYGPKIDIQI KDAIGRYHQC ATIQLDFQLP 

       550        560        570        580        590        600 
IRFNLTYVSH DGDDKKRPVI VHRAILGSVE RMIAILTENY GGKWPFWLSP RQVMVVPVGP 

       610        620        630        640        650        660 
TCDEYAQKVR QEFHDAKFMV DIDLDPGCTL NKKIRNAQLA QYNFILVVGE KEKASGTVNI 

       670        680        690 
RTRDNKVHGE RTVGETVERL QQLKQLRSKQ AEEEF 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC083914 mRNA. Translation: AAH83914.1.
IPIIPI00559880.
RefSeqNP_001006977.1.
UniGeneRn.22757

3D structure databases

SMRQ5XHY5. Positions 53-125, 55-685, 293-692.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5XHY5.

PTM databases

PhosphoSiteQ5XHY5.

Genome annotation databases

EnsemblENSRNOT00000051910; ENSRNOP00000044467; ENSRNOG00000019023; Rattus norvegicus. [Genome view]
GeneID294810.
KEGGrno:294810.
NMPDRfig|10116.3.peg.15656.
UCSCNM_001006976. rat.

Organism-specific databases

CTD294810.
RGD1359527. Tars.

Phylogenomic databases

eggNOGroNOG15014.
HOVERGENQ5XHY5.
PhylomeDBQ5XHY5.

Enzyme and pathway databases

BRENDA6.1.1.3. 248.

Gene expression databases

ArrayExpressQ5XHY5.
GenevestigatorQ5XHY5.
GermOnlineENSRNOG00000019023. Rattus norvegicus.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II_cons-dom.
IPR004154. Anticodon_bd.
IPR012675. b-grasp_ferredoxin-like.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-synth_IIa.
IPR018158. Thr-tRNA-synth_IIa_cons-reg.
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.
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]
TIGRFAMsTIGR00418. thrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio638628.

Entry information

Entry nameSYTC_RAT
AccessionPrimary (citable) accession number: Q5XHY5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 23, 2004
Last modified: February 9, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents