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Conserved domains on  [gi|22328775|ref|NP_193582|]
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D-Tyr-tRNA(Tyr) deacylase family protein [Arabidopsis thaliana]

Protein Classification

D-aminoacyl-tRNA deacylase( domain architecture ID 10015219)

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

EC:  3.1.1.96
Gene Ontology:  GO:0006399|GO:0051499

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PTZ00120 PTZ00120
D-tyrosyl-tRNA(Tyr) deacylase; Provisional
 1-153 3.65e-86

D-tyrosyl-tRNA(Tyr) deacylase; Provisional


:

Pssm-ID: 185458  Cd Length: 154  Bit Score: 248.76  E-value: 3.65e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775    1 MRAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNETtGKGWDQNVMQRNYGVLLVSQ 80
Cdd:PTZ00120   1 MRVVIQRVLSASVTVEGEVVGSIGKGLVLLVGIHEEDTWEDADYIIRKCLKLRLWPDEG-GKMWDRSVKDKDYEVLVVSQ 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328775   81 FTLYGFLKGNKPDFHVAMPPDKAKPFYASLVEKFQKAYNPDAVKDGVFGAMMQVNLVNDGPVTMQLDSPQSTK 153
Cdd:PTZ00120  80 FTLFNVKKGNKPDFHLAMSPEDALPLYNKFVEKFKKEYAPEKIKTGKFGQYMNVSLVNDGPVTIILDSKEKNL 152
 
Name Accession Description Interval E-value
PTZ00120 PTZ00120
D-tyrosyl-tRNA(Tyr) deacylase; Provisional
 1-153 3.65e-86

D-tyrosyl-tRNA(Tyr) deacylase; Provisional


Pssm-ID: 185458  Cd Length: 154  Bit Score: 248.76  E-value: 3.65e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775    1 MRAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNETtGKGWDQNVMQRNYGVLLVSQ 80
Cdd:PTZ00120   1 MRVVIQRVLSASVTVEGEVVGSIGKGLVLLVGIHEEDTWEDADYIIRKCLKLRLWPDEG-GKMWDRSVKDKDYEVLVVSQ 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328775   81 FTLYGFLKGNKPDFHVAMPPDKAKPFYASLVEKFQKAYNPDAVKDGVFGAMMQVNLVNDGPVTMQLDSPQSTK 153
Cdd:PTZ00120  80 FTLFNVKKGNKPDFHLAMSPEDALPLYNKFVEKFKKEYAPEKIKTGKFGQYMNVSLVNDGPVTIILDSKEKNL 152
Dtyr_deacylase cd00563
D-Tyrosyl-tRNAtyr deacylases; a class of tRNA-dependent hydrolases which are capable of ...
 1-148 1.37e-81

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: 236.79  E-value: 1.37e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775   1 MRAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNETTgkGWDQNVMQRNYGVLLVSQ 80
Cdd:cd00563   1 MRAVIQRVSEASVTVDGEVVGAIGQGLLVLVGVTHDDTEEDAEYLARKILNLRIFEDEEG--KMNLSVKDVNGEILVVSQ 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328775  81 FTLYGFL-KGNKPDFHVAMPPDKAKPFYASLVEKFQKAYnpDAVKDGVFGAMMQVNLVNDGPVTMQLDS 148
Cdd:cd00563  79 FTLYADTkKGRRPSFSAAAPPDKAEPLYESFVELLREKG--IKVETGVFGAMMQVSLVNDGPVTIILDS 145
Tyr_Deacylase pfam02580
D-Tyr-tRNA(Tyr) deacylase; This family comprises of several D-Tyr-tRNA(Tyr) deacylase proteins. ...
 2-147 2.07e-79

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: 231.10  E-value: 2.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775     2 RAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNEtTGKgWDQNVMQRNYGVLLVSQF 81
Cdd:pfam02580   1 RAVIQRVSSASVTVDGEVVGSIGRGLLVLVGVGKGDTEEDADKLAKKILNLRIFEDE-NGK-MNLSLKDVGGEILVVSQF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328775    82 TLYG-FLKGNKPDFHVAMPPDKAKPFYASLVEKFQKAYNPdAVKDGVFGAMMQVNLVNDGPVTMQLD 147
Cdd:pfam02580  79 TLYAdTRKGRRPSFHAAAPPEEAEPLYERFVEKLRKEYGE-KVETGVFGADMQVSLVNDGPVTILLD 144
Dtd COG1490
D-aminoacyl-tRNA deacylase [Translation, ribosomal structure and biogenesis];
1-150 4.60e-73

D-aminoacyl-tRNA deacylase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441099  Cd Length: 147  Bit Score: 215.24  E-value: 4.60e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775   1 MRAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNEtTGKgWDQNVMQRNYGVLLVSQ 80
Cdd:COG1490   1 MRAVIQRVSEASVTVDGEVVGEIGKGLLVLLGVEKGDTEEDADWLARKILNLRIFEDE-NGK-MNLSLLDVGGELLVVSQ 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328775  81 FTLYGFL-KGNKPDFHVAMPPDKAKPFYASLVEKFQKAYNPdaVKDGVFGAMMQVNLVNDGPVTMQLDSPQ 150
Cdd:COG1490  79 FTLYADTrKGRRPSFSKAAPPEEAEPLYEYFVEALRELGLP--VETGVFGADMQVSLVNDGPVTILLDSKK 147
TIGR00256 TIGR00256
D-tyrosyl-tRNA(Tyr) deacylase; This homodimeric enzyme appears able to cleave any D-amino acid ...
 1-148 1.16e-49

D-tyrosyl-tRNA(Tyr) deacylase; This homodimeric enzyme appears able to cleave any D-amino acid (and glycine, which does not have distinct D/L forms) from charged tRNA. The name reflects characterization with respect to D-Tyr on tRNA(Tyr) as established in the literature, but substrate specificity seems much broader. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129358  Cd Length: 145  Bit Score: 156.16  E-value: 1.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775     1 MRAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNETtGKgWDQNVMQRNYGVLLVSQ 80
Cdd:TIGR00256   1 MIALIQRVSQASVTVEGEVIGEIGAGLLVLLGVEKDDDEQKADKLAEKVLNYRIFSDSE-GK-MNLNVQQAGGEILSVSQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328775    81 FTLYGFL-KGNKPDFHVAMPPDKAKPFYASLVEKFQKAYNPdaVKDGVFGAMMQVNLVNDGPVTMQLDS 148
Cdd:TIGR00256  79 FTLAADTkKGMRPSFSKGASPDRAEELYEYFVELCREKGMK--VQTGRFAADMQVSLTNDGPVTFWLDV 145
 
Name Accession Description Interval E-value
PTZ00120 PTZ00120
D-tyrosyl-tRNA(Tyr) deacylase; Provisional
 1-153 3.65e-86

D-tyrosyl-tRNA(Tyr) deacylase; Provisional


Pssm-ID: 185458  Cd Length: 154  Bit Score: 248.76  E-value: 3.65e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775    1 MRAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNETtGKGWDQNVMQRNYGVLLVSQ 80
Cdd:PTZ00120   1 MRVVIQRVLSASVTVEGEVVGSIGKGLVLLVGIHEEDTWEDADYIIRKCLKLRLWPDEG-GKMWDRSVKDKDYEVLVVSQ 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328775   81 FTLYGFLKGNKPDFHVAMPPDKAKPFYASLVEKFQKAYNPDAVKDGVFGAMMQVNLVNDGPVTMQLDSPQSTK 153
Cdd:PTZ00120  80 FTLFNVKKGNKPDFHLAMSPEDALPLYNKFVEKFKKEYAPEKIKTGKFGQYMNVSLVNDGPVTIILDSKEKNL 152
Dtyr_deacylase cd00563
D-Tyrosyl-tRNAtyr deacylases; a class of tRNA-dependent hydrolases which are capable of ...
 1-148 1.37e-81

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: 236.79  E-value: 1.37e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775   1 MRAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNETTgkGWDQNVMQRNYGVLLVSQ 80
Cdd:cd00563   1 MRAVIQRVSEASVTVDGEVVGAIGQGLLVLVGVTHDDTEEDAEYLARKILNLRIFEDEEG--KMNLSVKDVNGEILVVSQ 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328775  81 FTLYGFL-KGNKPDFHVAMPPDKAKPFYASLVEKFQKAYnpDAVKDGVFGAMMQVNLVNDGPVTMQLDS 148
Cdd:cd00563  79 FTLYADTkKGRRPSFSAAAPPDKAEPLYESFVELLREKG--IKVETGVFGAMMQVSLVNDGPVTIILDS 145
Tyr_Deacylase pfam02580
D-Tyr-tRNA(Tyr) deacylase; This family comprises of several D-Tyr-tRNA(Tyr) deacylase proteins. ...
 2-147 2.07e-79

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: 231.10  E-value: 2.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775     2 RAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNEtTGKgWDQNVMQRNYGVLLVSQF 81
Cdd:pfam02580   1 RAVIQRVSSASVTVDGEVVGSIGRGLLVLVGVGKGDTEEDADKLAKKILNLRIFEDE-NGK-MNLSLKDVGGEILVVSQF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328775    82 TLYG-FLKGNKPDFHVAMPPDKAKPFYASLVEKFQKAYNPdAVKDGVFGAMMQVNLVNDGPVTMQLD 147
Cdd:pfam02580  79 TLYAdTRKGRRPSFHAAAPPEEAEPLYERFVEKLRKEYGE-KVETGVFGADMQVSLVNDGPVTILLD 144
Dtd COG1490
D-aminoacyl-tRNA deacylase [Translation, ribosomal structure and biogenesis];
1-150 4.60e-73

D-aminoacyl-tRNA deacylase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441099  Cd Length: 147  Bit Score: 215.24  E-value: 4.60e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775   1 MRAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNEtTGKgWDQNVMQRNYGVLLVSQ 80
Cdd:COG1490   1 MRAVIQRVSEASVTVDGEVVGEIGKGLLVLLGVEKGDTEEDADWLARKILNLRIFEDE-NGK-MNLSLLDVGGELLVVSQ 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328775  81 FTLYGFL-KGNKPDFHVAMPPDKAKPFYASLVEKFQKAYNPdaVKDGVFGAMMQVNLVNDGPVTMQLDSPQ 150
Cdd:COG1490  79 FTLYADTrKGRRPSFSKAAPPEEAEPLYEYFVEALRELGLP--VETGVFGADMQVSLVNDGPVTILLDSKK 147
TIGR00256 TIGR00256
D-tyrosyl-tRNA(Tyr) deacylase; This homodimeric enzyme appears able to cleave any D-amino acid ...
 1-148 1.16e-49

D-tyrosyl-tRNA(Tyr) deacylase; This homodimeric enzyme appears able to cleave any D-amino acid (and glycine, which does not have distinct D/L forms) from charged tRNA. The name reflects characterization with respect to D-Tyr on tRNA(Tyr) as established in the literature, but substrate specificity seems much broader. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129358  Cd Length: 145  Bit Score: 156.16  E-value: 1.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328775     1 MRAVIQRVSSSSVTVDGRIVSEIGPGLLVLIGIHESDTESDADYICRKVLNMRLFSNETtGKgWDQNVMQRNYGVLLVSQ 80
Cdd:TIGR00256   1 MIALIQRVSQASVTVEGEVIGEIGAGLLVLLGVEKDDDEQKADKLAEKVLNYRIFSDSE-GK-MNLNVQQAGGEILSVSQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328775    81 FTLYGFL-KGNKPDFHVAMPPDKAKPFYASLVEKFQKAYNPdaVKDGVFGAMMQVNLVNDGPVTMQLDS 148
Cdd:TIGR00256  79 FTLAADTkKGMRPSFSKGASPDRAEELYEYFVELCREKGMK--VQTGRFAADMQVSLTNDGPVTFWLDV 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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