id: Pfam:PF02580
pfam_id: PF02580
name: D-Tyr-tRNA(Tyr) deacylase
short_name: Tyr_Deacylase
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF02580
counters:
  proteins: 19377
  matches: 19510
  proteomes: 17291
  taxa: 28568
  structures: 22
  alphafold_models: 13734
  domain_architectures: 110
provenance:
  snapshot_id: interpro-pfam-duf-2026-10-10
  path: data/worklists/interpro-pfam-duf-2026-10-10.json
  sha256: 17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383
  generated_at: '2026-10-10T07:44:21.614711Z'
  source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/
interpro_id: InterPro:IPR003732
description: This family comprises of several D-Tyr-tRNA(Tyr) deacylase proteins. Cell growth inhibition
  by several d-amino acids can be explained by an in vivo production of d-aminoacyl-tRNA molecules. Escherichia
  coli and yeast cells express an enzyme, d-Tyr-tRNA(Tyr) deacylase, capable of recycling such d-aminoacyl-tRNA
  molecules into free tRNA and d-amino acid. Accordingly, upon inactivation of the genes of the above
  deacylases, the toxicity of d-amino acids increases. Orthologues of the deacylase are found in many
  cells [[cite:PUB00017393]].The D-aminoacyl-tRNA deacylase (DTD) enzyme is homodimeric with two active
  sites located at the dimeric interface. Each active site carries an invariant Gly-cisPro dipeptide motif
  in each monomer. The interaction between the dipeptide motifs from each monomer ensures substrate stereospecificity.
  This family also includes a subclass of DTDs which is present in Chordata and harbors a Gly-transPro
  motif. The cis to trans switch is the key to Animal DTDs (ATD) gaining of L-chiral selectivity. This
  'gain of function' through relaxation of substrate chiral specificity underlies ATD's capability of
  correcting the error in tRNA selection [[cite:PUB00109228]].