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
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
5-124
2.70e-42
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the nascent peptide and tRNA when peptidyl-tRNA is released prematurely from the ribosome. This ensures the recycling of peptidyl-tRNAs into tRNAs produced through abortion of translation and is essential for cell viability.This group also contains chloroplast RNA splicing 2 (CRS2), which is closely related nuclear-encoded protein required for the splicing of nine group II introns in chloroplasts.
The actual alignment was detected with superfamily member cd02406:
Pssm-ID: 469736 Cd Length: 191 Bit Score: 137.61 E-value: 2.70e-42
Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of ...
5-124
2.70e-42
Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of group II introns in the chloroplast. CRS2 forms stable complexes with two CRS2-associated factors, CAF1 and CAF2, which are required for the splicing of distinct subsets of CRS2-dependent introns. CRS2 is closely related to bacterial peptidyl-tRNA hydrolases (PTH).
Pssm-ID: 239090 Cd Length: 191 Bit Score: 137.61 E-value: 2.70e-42
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
1-125
1.05e-21
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA hydrolase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439963 Cd Length: 187 Bit Score: 84.68 E-value: 1.05e-21
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that ...
5-124
1.33e-18
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that drop off the ribosome during protein synthesis. Peptidyl-tRNA hydrolase is a bacterial protein; YHR189W from Saccharomyces cerevisiae appears to be orthologous and likely has the same function. [Protein synthesis, Other]
Pssm-ID: 213531 Cd Length: 188 Bit Score: 77.01 E-value: 1.33e-18
Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of ...
5-124
2.70e-42
Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of group II introns in the chloroplast. CRS2 forms stable complexes with two CRS2-associated factors, CAF1 and CAF2, which are required for the splicing of distinct subsets of CRS2-dependent introns. CRS2 is closely related to bacterial peptidyl-tRNA hydrolases (PTH).
Pssm-ID: 239090 Cd Length: 191 Bit Score: 137.61 E-value: 2.70e-42
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
1-125
1.05e-21
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA hydrolase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439963 Cd Length: 187 Bit Score: 84.68 E-value: 1.05e-21
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that ...
5-124
1.33e-18
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that drop off the ribosome during protein synthesis. Peptidyl-tRNA hydrolase is a bacterial protein; YHR189W from Saccharomyces cerevisiae appears to be orthologous and likely has the same function. [Protein synthesis, Other]
Pssm-ID: 213531 Cd Length: 188 Bit Score: 77.01 E-value: 1.33e-18
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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