RecName: Full=D-aminoacyl-tRNA deacylase 2; AltName: Full=Animalia-specific tRNA deacylase; Short=ATD; AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase 2; AltName: Full=L-alanyl-tRNA deacylase
D-aminoacyl-tRNA deacylase( domain architecture ID 10495419)
D-aminoacyl-tRNA deacylase hydrolyzes D-aminoacyl-tRNA into D-amino acids and free tRNA which may be a defense mechanism against harmful effects of incorporating D-amino acids
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Tyr_Deacylase | pfam02580 | D-Tyr-tRNA(Tyr) deacylase; This family comprises of several D-Tyr-tRNA(Tyr) deacylase proteins. ... |
11-167 | 9.95e-47 | |||
D-Tyr-tRNA(Tyr) deacylase; 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.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. : Pssm-ID: 460603 Cd Length: 144 Bit Score: 149.05 E-value: 9.95e-47
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Name | Accession | Description | Interval | E-value | |||
Tyr_Deacylase | pfam02580 | D-Tyr-tRNA(Tyr) deacylase; This family comprises of several D-Tyr-tRNA(Tyr) deacylase proteins. ... |
11-167 | 9.95e-47 | |||
D-Tyr-tRNA(Tyr) deacylase; 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.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. Pssm-ID: 460603 Cd Length: 144 Bit Score: 149.05 E-value: 9.95e-47
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Dtyr_deacylase | cd00563 | D-Tyrosyl-tRNAtyr deacylases; a class of tRNA-dependent hydrolases which are capable of ... |
11-167 | 8.82e-15 | |||
D-Tyrosyl-tRNAtyr deacylases; a class of tRNA-dependent hydrolases which are capable of hydrolyzing the ester bond of D-Tyrosyl-tRNA reducing the level of cellular D-Tyrosine while recycling the peptidyl-tRNA; found in bacteria and in eukaryotes but not in archea; beta barrel-like fold structure; forms homodimers in which two surface cavities serve as the active site for tRNA binding Pssm-ID: 238316 Cd Length: 145 Bit Score: 67.30 E-value: 8.82e-15
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PTZ00120 | PTZ00120 | D-tyrosyl-tRNA(Tyr) deacylase; Provisional |
11-167 | 7.96e-11 | |||
D-tyrosyl-tRNA(Tyr) deacylase; Provisional Pssm-ID: 185458 Cd Length: 154 Bit Score: 56.93 E-value: 7.96e-11
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Name | Accession | Description | Interval | E-value | |||
Tyr_Deacylase | pfam02580 | D-Tyr-tRNA(Tyr) deacylase; This family comprises of several D-Tyr-tRNA(Tyr) deacylase proteins. ... |
11-167 | 9.95e-47 | |||
D-Tyr-tRNA(Tyr) deacylase; 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.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. Pssm-ID: 460603 Cd Length: 144 Bit Score: 149.05 E-value: 9.95e-47
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Dtyr_deacylase | cd00563 | D-Tyrosyl-tRNAtyr deacylases; a class of tRNA-dependent hydrolases which are capable of ... |
11-167 | 8.82e-15 | |||
D-Tyrosyl-tRNAtyr deacylases; a class of tRNA-dependent hydrolases which are capable of hydrolyzing the ester bond of D-Tyrosyl-tRNA reducing the level of cellular D-Tyrosine while recycling the peptidyl-tRNA; found in bacteria and in eukaryotes but not in archea; beta barrel-like fold structure; forms homodimers in which two surface cavities serve as the active site for tRNA binding Pssm-ID: 238316 Cd Length: 145 Bit Score: 67.30 E-value: 8.82e-15
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PTZ00120 | PTZ00120 | D-tyrosyl-tRNA(Tyr) deacylase; Provisional |
11-167 | 7.96e-11 | |||
D-tyrosyl-tRNA(Tyr) deacylase; Provisional Pssm-ID: 185458 Cd Length: 154 Bit Score: 56.93 E-value: 7.96e-11
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Blast search parameters | ||||
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