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. ...
42-422
0e+00
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: 574.04 E-value: 0e+00
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2. ...
42-422
0e+00
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: 574.04 E-value: 0e+00
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; ...
34-419
0e+00
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: 536.16 E-value: 0e+00
tRNA-guanine transglycosylase; This tRNA-guanine transglycosylase (tgt) catalyzes an exchange ...
34-421
1.91e-148
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: 426.83 E-value: 1.91e-148
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2. ...
42-422
0e+00
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: 574.04 E-value: 0e+00
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; ...
34-419
0e+00
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: 536.16 E-value: 0e+00
tRNA-guanine transglycosylase; This tRNA-guanine transglycosylase (tgt) catalyzes an exchange ...
34-421
1.91e-148
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: 426.83 E-value: 1.91e-148
tRNA-guanine family transglycosylase; Different tRNA-guanine transglycosylases catalyze ...
42-421
1.85e-145
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: 419.12 E-value: 1.85e-145
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.
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
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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.
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)
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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.
(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,
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specific hits meet or exceed a domain-specific e-value threshold
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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
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the domain superfamily to which the specific and non-specific hits belong
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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