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 [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
1-185
3.58e-112
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: 316.96 E-value: 3.58e-112
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
1-185
3.58e-112
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: 316.96 E-value: 3.58e-112
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
3-173
1.51e-99
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.
Pssm-ID: 238259 Cd Length: 171 Bit Score: 284.75 E-value: 1.51e-99
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that ...
1-185
2.95e-86
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: 251.50 E-value: 2.95e-86
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
1-185
3.58e-112
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: 316.96 E-value: 3.58e-112
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
3-173
1.51e-99
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.
Pssm-ID: 238259 Cd Length: 171 Bit Score: 284.75 E-value: 1.51e-99
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that ...
1-185
2.95e-86
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: 251.50 E-value: 2.95e-86
Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of ...
3-185
1.77e-62
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: 191.54 E-value: 1.77e-62
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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
mapped to the query sequence.
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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
(CDART).
Modify your query to search against a different database and/or use advanced search options
