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Q7UJ52 · SYT_RHOBA

Function

function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

1743100200300400500600700
TypeIDPosition(s)Description
Binding site416Zn2+ (UniProtKB | ChEBI)
Binding site467Zn2+ (UniProtKB | ChEBI)
Binding site596Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionthreonine-tRNA ligase activity
Molecular FunctiontRNA binding
Biological Processthreonyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Threonine--tRNA ligase
  • EC number
  • Alternative names
    • Threonyl-tRNA synthetase
      (ThrRS
      )

Gene names

    • Name
      thrS
    • Ordered locus names
      RB12129

Organism names

Accessions

  • Primary accession
    Q7UJ52

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001010341-743Threonine--tRNA ligase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-15Polar residues
Region1-30Disordered
Domain13-76TGS
Region264-619Catalytic
Region354-404Insert

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    743
  • Mass (Da)
    83,078
  • Last updated
    2006-02-07 v2
  • MD5 Checksum
    1941FB0D2CFA193F29AE1DDE82CF49B9
MSADSPSSPASSQAAEVQVRLPDGSLKTQPADATAMDVAKEISEGLARSVVAAEVDGTIVDSFRPLGEIADDENVVPLRLLTTRDESALDVLRHSAAHVMARAIMRIYKGVSLAFGPTTSGGFYYDFDMPEKISEDDFPKIEAEIKKIIKAKEPFERFVLERDEARKLCDDLDQDLKVEHIETGLGDQATVSFYRQGEFVDLCRGPHIPHAGMIKAIKLLSVAGAYWKGDASGRQLQRVYGTAFFDKKELASYLEQIEEAKRRDHRVLGKQHGLFAINPEVGQGLCLWLPKGARVRVTLEDFLRRELLSRGYDPVYSPHIGRVEMYETSGHFPYYRDSQFAPLFGSEVGGLLDAWSTRLDKDDLSKDDEDKLIAAAEVFGVKLPDYKPSASNDAKKDVLHRWQLNHERYLLKPMNCPHHCQIFGAQPRSYRQLPLRLFEFGTVYRHEQTGELNGMMRVRGLTQDDAHIFCTADQVEEEFRATIELTKFVLESVGLDDYRVQLSLRDPDSSKYVGSEENWDHAEGALRGVLEQSGLSFNEEPGEAAFYGPKADFMVRDCIGRSWQLGTVQLDYNLPERFKLEYKGNDNATHRPVMIHRAPFGSLERFTGMLIEHFAGAFPMWLSPEQIRVLPLSDKSVEYATAVAKQLDEAGFKVTVDASDGKVQAKIRNAQIDLVNYMAVVGPKEAESGQVALRDRIEGDLGSMPIKEAIARLQKEVETRQVRQAVKGSTVSIAETGGAATDY

Sequence caution

The sequence CAD77406.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-15Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX294154
EMBL· GenBank· DDBJ
CAD77406.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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