{"metadata":{"accession":"PF02580","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR003732","hierarchy":null,"name":{"name":"D-Tyr-tRNA(Tyr) deacylase","short":"Tyr_Deacylase"},"description":[{"text":"<p>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]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00017393":{"PMID":11568181,"ISBN":null,"volume":"276","issue":"50","year":2001,"title":"Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases.","URL":null,"raw_pages":"47285-90","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Ferri-Fioni ML","Schmitt E","Soutourina J","Plateau P","Mechulam Y","Blanquet S."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M106550200"},"PUB00109228":{"PMID":29410408,"ISBN":null,"volume":"9","issue":"1","year":2018,"title":"A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia.","URL":null,"raw_pages":"511","medline_journal":"Nat Commun","ISO_journal":"Nat Commun","authors":["Kuncha SK","Mazeed M","Singh R","Kattula B","Routh SB","Sankaranarayanan R."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":110,"interactions":0,"matches":19510,"pathways":0,"proteins":19377,"proteomes":17291,"sets":0,"structural_models":{"alphafold":13734},"structures":22,"taxa":28568},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":597,"alignment:full":11132},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"1jke","name":"D-Tyr tRNATyr deacylase from Escherichia coli"}}}