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Conserved domains on  [gi|14714923|gb|AAH10618|]
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C14orf126 protein [Homo sapiens]

Protein Classification

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

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

Graphical summary

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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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14714923    11 RALLQQCLHARLQIrpaDGDVAAqwvEVQRGLVIYVCFFKGADKELLPKMVNTLLNVKLSETENGKHV-SILDLPGNILI 89
Cdd:pfam02580   1 RAVIQRVSSASVTV---DGEVVG---SIGRGLLVLVGVGKGDTEEDADKLAKKILNLRIFEDENGKMNlSLKDVGGEILV 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14714923    90 IPQATLGGR-LKGRNMQYHSNSGKEEGFELYSQFVTLCEKEVAanskcaearVVVEHGTYGNRQVLKLDTNGPFTHLIE 167
Cdd:pfam02580  75 VSQFTLYADtRKGRRPSFHAAAPPEEAEPLYERFVEKLRKEYG---------EKVETGVFGADMQVSLVNDGPVTILLD 144
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14714923    11 RALLQQCLHARLQIrpaDGDVAAqwvEVQRGLVIYVCFFKGADKELLPKMVNTLLNVKLSETENGKHV-SILDLPGNILI 89
Cdd:pfam02580   1 RAVIQRVSSASVTV---DGEVVG---SIGRGLLVLVGVGKGDTEEDADKLAKKILNLRIFEDENGKMNlSLKDVGGEILV 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14714923    90 IPQATLGGR-LKGRNMQYHSNSGKEEGFELYSQFVTLCEKEVAanskcaearVVVEHGTYGNRQVLKLDTNGPFTHLIE 167
Cdd:pfam02580  75 VSQFTLYADtRKGRRPSFHAAAPPEEAEPLYERFVEKLRKEYG---------EKVETGVFGADMQVSLVNDGPVTILLD 144
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14714923  11 RALLQQCLHARLQIrpaDGDVAAqwvEVQRGLVIYVCFFKGADKELLPKMVNTLLNVKLSETENGKH-VSILDLPGNILI 89
Cdd:cd00563   2 RAVIQRVSEASVTV---DGEVVG---AIGQGLLVLVGVTHDDTEEDAEYLARKILNLRIFEDEEGKMnLSVKDVNGEILV 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14714923  90 IPQATLGGRL-KGRNMQYHSNSGKEEGFELYSQFVTLCEKEVAAnskcaearvvVEHGTYGNRQVLKLDTNGPFTHLIE 167
Cdd:cd00563  76 VSQFTLYADTkKGRRPSFSAAAPPDKAEPLYESFVELLREKGIK----------VETGVFGAMMQVSLVNDGPVTIILD 144
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14714923   11 RALLQQCLHARLQIrpaDGDVAAqwvEVQRGLVIYVCFFKGADKELLPKMVNTLLNVKLSETENGKH--VSILDLPGNIL 88
Cdd:PTZ00120   2 RVVIQRVLSASVTV---EGEVVG---SIGKGLVLLVGIHEEDTWEDADYIIRKCLKLRLWPDEGGKMwdRSVKDKDYEVL 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14714923   89 IIPQATLGGRLKGRNMQYHSNSGKEEGFELYSQFVTLCEKEVAANSkcaearvvVEHGTYGNRQVLKLDTNGPFTHLIE 167
Cdd:PTZ00120  76 VVSQFTLFNVKKGNKPDFHLAMSPEDALPLYNKFVEKFKKEYAPEK--------IKTGKFGQYMNVSLVNDGPVTIILD 146
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14714923    11 RALLQQCLHARLQIrpaDGDVAAqwvEVQRGLVIYVCFFKGADKELLPKMVNTLLNVKLSETENGKHV-SILDLPGNILI 89
Cdd:pfam02580   1 RAVIQRVSSASVTV---DGEVVG---SIGRGLLVLVGVGKGDTEEDADKLAKKILNLRIFEDENGKMNlSLKDVGGEILV 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14714923    90 IPQATLGGR-LKGRNMQYHSNSGKEEGFELYSQFVTLCEKEVAanskcaearVVVEHGTYGNRQVLKLDTNGPFTHLIE 167
Cdd:pfam02580  75 VSQFTLYADtRKGRRPSFHAAAPPEEAEPLYERFVEKLRKEYG---------EKVETGVFGADMQVSLVNDGPVTILLD 144
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14714923  11 RALLQQCLHARLQIrpaDGDVAAqwvEVQRGLVIYVCFFKGADKELLPKMVNTLLNVKLSETENGKH-VSILDLPGNILI 89
Cdd:cd00563   2 RAVIQRVSEASVTV---DGEVVG---AIGQGLLVLVGVTHDDTEEDAEYLARKILNLRIFEDEEGKMnLSVKDVNGEILV 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14714923  90 IPQATLGGRL-KGRNMQYHSNSGKEEGFELYSQFVTLCEKEVAAnskcaearvvVEHGTYGNRQVLKLDTNGPFTHLIE 167
Cdd:cd00563  76 VSQFTLYADTkKGRRPSFSAAAPPDKAEPLYESFVELLREKGIK----------VETGVFGAMMQVSLVNDGPVTIILD 144
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14714923   11 RALLQQCLHARLQIrpaDGDVAAqwvEVQRGLVIYVCFFKGADKELLPKMVNTLLNVKLSETENGKH--VSILDLPGNIL 88
Cdd:PTZ00120   2 RVVIQRVLSASVTV---EGEVVG---SIGKGLVLLVGIHEEDTWEDADYIIRKCLKLRLWPDEGGKMwdRSVKDKDYEVL 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14714923   89 IIPQATLGGRLKGRNMQYHSNSGKEEGFELYSQFVTLCEKEVAANSkcaearvvVEHGTYGNRQVLKLDTNGPFTHLIE 167
Cdd:PTZ00120  76 VVSQFTLFNVKKGNKPDFHLAMSPEDALPLYNKFVEKFKKEYAPEK--------IKTGKFGQYMNVSLVNDGPVTIILD 146
 
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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