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Conserved domains on  [gi|1831512479|ref|NP_001368226|]
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peptidyl-tRNA hydrolase [Caenorhabditis elegans]

Protein Classification

aminoacyl-tRNA hydrolase( domain architecture ID 141542)

aminoacyl-tRNA hydrolase catalyzes the hydolysis of an N-substituted aminoacyl-tRNA to yield the N-substituted amino acid and tRNA to ensure the recycling of peptidyl-tRNAs produced when translation is aborted

CATH:  3.40.50.1470
EC:  3.1.1.29
Gene Ontology:  GO:0004045|GO:0006412
PubMed:  16849786|24768774
SCOP:  4000577

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTH2_family super family cl19212
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
 1-60 3.42e-28

Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA from the premature translation termination product peptidyl-tRNA. Two structurally different enzymes have been reported to encode such activity, Pth present in bacteria and eukaryotes and Pth2 present in archaea and eukaryotes.


The actual alignment was detected with superfamily member cd02429:

Pssm-ID: 473151  Cd Length: 116  Bit Score: 96.70  E-value: 3.42e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831512479   1 MHKVTLGVDSEEEIKKVADKLTARNVDHKVWIE--DGFPVCIALKPYPKEEVKNALKGLKLF 60
Cdd:cd02429    55 MHKVVLEVPDEAALKNLSSKLTENSIKHKLWIEqpENIPTCIALKPYPKETVASYLKKLKLL 116
 
Name Accession Description Interval E-value
PTH2_like cd02429
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
 1-60 3.42e-28

Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA from the premature translation termination product peptidyl-tRNA. Two structurally different enzymes have been reported to encode such activity, Pth present in bacteria and eukaryotes and Pth2 present in archaea and eukaryotes. There is no functional information for this eukaryote-specific subgroup.


Pssm-ID: 239107  Cd Length: 116  Bit Score: 96.70  E-value: 3.42e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831512479   1 MHKVTLGVDSEEEIKKVADKLTARNVDHKVWIE--DGFPVCIALKPYPKEEVKNALKGLKLF 60
Cdd:cd02429    55 MHKVVLEVPDEAALKNLSSKLTENSIKHKLWIEqpENIPTCIALKPYPKETVASYLKKLKLL 116
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
 1-60 1.86e-16

Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from peptidyl-tRNA during translation.


Pssm-ID: 460403  Cd Length: 115  Bit Score: 66.70  E-value: 1.86e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831512479   1 MHKVTLGVDSEEEIKKVADKLTARNVDHKVWIEDGF-------PVCIALKPYPKEEVKNALKGLKLF 60
Cdd:pfam01981  49 QKKVVLKVPSEEELLELAEKAKSLGLPHALIRDAGRtqiapgtPTVLAIGPAPKELVDKITGHLKLL 115
 
Name Accession Description Interval E-value
PTH2_like cd02429
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
 1-60 3.42e-28

Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA from the premature translation termination product peptidyl-tRNA. Two structurally different enzymes have been reported to encode such activity, Pth present in bacteria and eukaryotes and Pth2 present in archaea and eukaryotes. There is no functional information for this eukaryote-specific subgroup.


Pssm-ID: 239107  Cd Length: 116  Bit Score: 96.70  E-value: 3.42e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831512479   1 MHKVTLGVDSEEEIKKVADKLTARNVDHKVWIE--DGFPVCIALKPYPKEEVKNALKGLKLF 60
Cdd:cd02429    55 MHKVVLEVPDEAALKNLSSKLTENSIKHKLWIEqpENIPTCIALKPYPKETVASYLKKLKLL 116
PTH2_family cd02407
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
 1-60 8.55e-19

Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA from the premature translation termination product peptidyl-tRNA. Two structurally different enzymes have been reported to encode such activity, Pth present in bacteria and eukaryotes and Pth2 present in archaea and eukaryotes.


Pssm-ID: 239091  Cd Length: 115  Bit Score: 72.57  E-value: 8.55e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831512479   1 MHKVTLGVDSEEEIKKVADKLTARNVDHKVW-------IEDGFPVCIALKPYPKEEVKNALKGLKLF 60
Cdd:cd02407    49 QKKVVLKVPSEEELLELAKKAKELGLPHSLIqdagrtqIPPGTPTVLAIGPAPKEKVDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
 1-60 1.86e-16

Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from peptidyl-tRNA during translation.


Pssm-ID: 460403  Cd Length: 115  Bit Score: 66.70  E-value: 1.86e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831512479   1 MHKVTLGVDSEEEIKKVADKLTARNVDHKVWIEDGF-------PVCIALKPYPKEEVKNALKGLKLF 60
Cdd:pfam01981  49 QKKVVLKVPSEEELLELAEKAKSLGLPHALIRDAGRtqiapgtPTVLAIGPAPKELVDKITGHLKLL 115
 
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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