Q07648 · DTD_YEAST

Function

function

An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs (Probable). Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr) (PubMed:10766779).
May also deacylate mischarged D-leucyl-tRNA(Leu) (PubMed:10918062).
Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS (By similarity).
Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site (By similarity).
By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality (By similarity).

Miscellaneous

Present with 4610 molecules/cell in log phase SD medium.

Catalytic activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionD-leucyl-tRNA(Leu) deacylase activity
Molecular FunctionD-tyrosyl-tRNA(Tyr) deacylase activity
Molecular FunctiontRNA binding
Biological ProcessD-leucine catabolic process
Biological ProcessD-tyrosine catabolic process
Biological ProcesstRNA metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    D-aminoacyl-tRNA deacylase
  • EC number
  • Short names
    DTD
  • Alternative names
    • D-tyrosyl-tRNA(Tyr) deacylase
    • Gly-tRNA(Ala) deacylase

Gene names

    • Name
      DTD1
    • Ordered locus names
      YDL219W

Organism names

Accessions

  • Primary accession
    Q07648
  • Secondary accessions
    • D6VRD5

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

10-fold decrease in D-tyrosyl-tRNA(Tyr) deacylase activity, growth becomes more sensitive to D-tyrosine and is inhibited at 0.1 mM D-Tyr (PubMed:10766779, PubMed:10918062).
Growth is also inhibited in the presence of 0.3 mM D-leucine; wild-type cells grow well in up to 0.3 mM D-Tyr and 10 mM D-Leu (PubMed:10918062).
No growth differences observed in the presence of the other D-amino acids (PubMed:10918062).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001646341-150D-aminoacyl-tRNA deacylase

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif140-141Gly-cisPro motif, important for rejection of L-amino acids

Domain

A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.

Sequence similarities

Belongs to the DTD family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    150
  • Mass (Da)
    16,746
  • Last updated
    1996-11-01 v1
  • Checksum
    7773D8A1FBA5E982
MKIVLQKVSQASVVVDSKVISSIKHGYMLLVGISIDDSMAEIDKLSKKVLSLRIFEDESRNLWKKNIKEANGEILSVSQFTLMAKTKKGTKPDFHLAQKGHIAKELYEEFLKLLRSDLGEEKVKDGEFGAMMSCSLTNEGPVTIILDSDQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z74267
EMBL· GenBank· DDBJ
CAA98798.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006938
EMBL· GenBank· DDBJ
DAA11645.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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