tRNA-ribosyltransferase family protein such as the catalytic and accessory subunits of TGT, which catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 in tRNAs with GU(N) anticodons resulting in the hypermodified nucleoside queuosine
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2. ...
26-287
4.71e-166
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2.29, also known as tRNA-guanine transglycosylase and guanine insertion enzyme. Queuine tRNA-ribosyltransferase modifies tRNAs for asparagine, aspartic acid, histidine and tyrosine with queuine. It catalyzes the exchange of guanine-34 at the wobble position with 7-aminomethyl-7-deazaguanine, and the addition of a cyclopentenediol moiety to 7-aminomethyl-7-deazaguanine-34 tRNA; giving a hypermodified base queuine in the wobble position. The aligned region contains a zinc binding motif C-x-C-x2-C-x29-H, and important tRNA and 7-aminomethyl-7deazaguanine binding residues.
:
Pssm-ID: 460299 Cd Length: 358 Bit Score: 465.03 E-value: 4.71e-166
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2. ...
26-287
4.71e-166
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2.29, also known as tRNA-guanine transglycosylase and guanine insertion enzyme. Queuine tRNA-ribosyltransferase modifies tRNAs for asparagine, aspartic acid, histidine and tyrosine with queuine. It catalyzes the exchange of guanine-34 at the wobble position with 7-aminomethyl-7-deazaguanine, and the addition of a cyclopentenediol moiety to 7-aminomethyl-7-deazaguanine-34 tRNA; giving a hypermodified base queuine in the wobble position. The aligned region contains a zinc binding motif C-x-C-x2-C-x29-H, and important tRNA and 7-aminomethyl-7deazaguanine binding residues.
Pssm-ID: 460299 Cd Length: 358 Bit Score: 465.03 E-value: 4.71e-166
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; ...
18-287
3.87e-156
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; Queuine/archaeosine tRNA-ribosyltransferase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440112 Cd Length: 370 Bit Score: 440.25 E-value: 3.87e-156
tRNA-guanine transglycosylase; This tRNA-guanine transglycosylase (tgt) catalyzes an exchange ...
18-292
3.34e-121
tRNA-guanine transglycosylase; This tRNA-guanine transglycosylase (tgt) catalyzes an exchange for the guanine base at position 34 of many tRNAs; this nucleotide is subsequently modified to queuosine. The Archaea have a closely related enzyme that catalyzes a base exchange for guanine at position 15 in some tRNAs, a site that is subsequently converted to the archaeal-specific modified base archaeosine (7-formamidino-7-deazaguanosine), while Archaeoglobus fulgidus has both enzymes. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 129522 Cd Length: 368 Bit Score: 351.71 E-value: 3.34e-121
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2. ...
26-287
4.71e-166
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2.29, also known as tRNA-guanine transglycosylase and guanine insertion enzyme. Queuine tRNA-ribosyltransferase modifies tRNAs for asparagine, aspartic acid, histidine and tyrosine with queuine. It catalyzes the exchange of guanine-34 at the wobble position with 7-aminomethyl-7-deazaguanine, and the addition of a cyclopentenediol moiety to 7-aminomethyl-7-deazaguanine-34 tRNA; giving a hypermodified base queuine in the wobble position. The aligned region contains a zinc binding motif C-x-C-x2-C-x29-H, and important tRNA and 7-aminomethyl-7deazaguanine binding residues.
Pssm-ID: 460299 Cd Length: 358 Bit Score: 465.03 E-value: 4.71e-166
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; ...
18-287
3.87e-156
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; Queuine/archaeosine tRNA-ribosyltransferase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440112 Cd Length: 370 Bit Score: 440.25 E-value: 3.87e-156
tRNA-guanine transglycosylase; This tRNA-guanine transglycosylase (tgt) catalyzes an exchange ...
18-292
3.34e-121
tRNA-guanine transglycosylase; This tRNA-guanine transglycosylase (tgt) catalyzes an exchange for the guanine base at position 34 of many tRNAs; this nucleotide is subsequently modified to queuosine. The Archaea have a closely related enzyme that catalyzes a base exchange for guanine at position 15 in some tRNAs, a site that is subsequently converted to the archaeal-specific modified base archaeosine (7-formamidino-7-deazaguanosine), while Archaeoglobus fulgidus has both enzymes. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 129522 Cd Length: 368 Bit Score: 351.71 E-value: 3.34e-121
tRNA-guanine family transglycosylase; Different tRNA-guanine transglycosylases catalyze ...
18-287
2.88e-120
tRNA-guanine family transglycosylase; Different tRNA-guanine transglycosylases catalyze different tRNA base modifications. Two guanine base substitutions by different enzymes described by the model are involved in generating queuosine at position 34 in bacterial tRNAs and archaeosine at position 15 in archaeal tRNAs. This model is designed for fragment searching, so the superfamily is used loosely. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 129541 Cd Length: 367 Bit Score: 349.40 E-value: 2.88e-120
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
