A3DN67 · SYT_STAMF

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.

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TypeIDPosition(s)Description
Binding site289Zn2+ (UniProtKB | ChEBI)
Binding site340Zn2+ (UniProtKB | ChEBI)
Binding site461Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionthreonine-tRNA ligase activity
Molecular FunctiontRNA binding
Molecular Functionzinc ion 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
      Smar_0978

Organism names

Accessions

  • Primary accession
    A3DN67

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000205231-614Threonine--tRNA ligase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-138Editing domain
Region195-492Catalytic
Region196-492Catalytic

Domain

The N-terminal domain is an archaea-specific tRNA-editing domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis of tRNA editing is performed by the charged tRNA itself.

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    614
  • Mass (Da)
    71,876
  • Last updated
    2007-03-20 v1
  • Checksum
    87D1E0D61EB4B829
MRILTIHARKFHYKALSQALDKPEELTNENKEGFFENVLVVFTSVEEGDNEKVVEKAVTEILDIANRVKPKTILLYPYAHLSSDLASPSQALEIMKLLEQKLRGKTDLEVYRAPFGWYKEFMLDCYGHPLSELSKTIRITGGGEVVRRELKKEFYILTPDGKVYDPEKFNYDKYPDLKILVDKEVFGKELPGGVNRVNDYCRKFGFEWEPMSDHGHMRYGPHAVIIMESIMQYSWNIVRSLGIPVYKVMGTNMFNLSEKPVLEHALLFGDRLYELKVDNEKFVLRYAACHQQFAMLRDWIISYKNLPFGMFEVADSYRLEQRGELNLCFRLRKFYMPDLHILNRDLNEAIKISRIVQDKILEEIAKIGRKYVALYNVTSDFFDKYRDILIEFVRRENYPVLVSVIPSGIYYWVLNVEYHIIDNLNRPREIATFQIDIGNGERFNITYTDEKGEKHHPVIIHTAIIGGIERFIYTIFDTAALMEKEGKTPYIPTWLAPVQVRIIPIKNEYLDYAEKVAEKIENAGFRVDIDDRGESLGKKIRDAGREWIPYIVVIGEREVRSNTINVRIRRTNDQKVMVTDELIRILEEETKNYPRVSLTMPKYLSKRPIPSYHA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000575
EMBL· GenBank· DDBJ
ABN70077.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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