S-adenosylmethionine:tRNA ribosyltransferase-isomerase transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA)
S-adenosylmethionine:tRNA-ribosyltransferase-isomerase (queuine synthetase) [Translation, ribosomal structure and biogenesis]; S-adenosylmethionine:tRNA-ribosyltransferase-isomerase (queuine synthetase) is part of the Pathway/BioSystem: tRNA modification
:
Pssm-ID: 440571 [Multi-domain] Cd Length: 340 Bit Score: 472.19 E-value: 2.17e-167
S-adenosylmethionine:tRNA-ribosyltransferase-isomerase (queuine synthetase) [Translation, ribosomal structure and biogenesis]; S-adenosylmethionine:tRNA-ribosyltransferase-isomerase (queuine synthetase) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440571 [Multi-domain] Cd Length: 340 Bit Score: 472.19 E-value: 2.17e-167
Queuosine biosynthesis protein; Queuosine (Q) biosynthesis protein, or S-adenosylmethionine: ...
11-403
1.45e-136
Queuosine biosynthesis protein; Queuosine (Q) biosynthesis protein, or S-adenosylmethionine:tRNA -ribosyltransferase-isomerase, is required for the synthesis of the queuosine precursor (oQ). It catalyzes the transfer and isomerization of the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to form epoxyqueuosine (oQ-tRNA). Q is a hypermodified nucleoside usually found at the first position of the anticodon of asparagine, aspartate, histidine, and tyrosine tRNAs. In Streptococcus gordonii, QueA has been shown to play a role in the regulation of arginine deiminase genes.
Pssm-ID: 460587 [Multi-domain] Cd Length: 336 Bit Score: 393.67 E-value: 1.45e-136
S-adenosylmethionine:tRNA ribosyltransferase-isomerase; This model describes the enzyme for ...
11-404
1.25e-106
S-adenosylmethionine:tRNA ribosyltransferase-isomerase; This model describes the enzyme for S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA). QueA synthesizes Queuosine which is usually in the first position of the anticodon of tRNAs specific for asparagine, aspartate, histidine, and tyrosine. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 272912 [Multi-domain] Cd Length: 344 Bit Score: 317.86 E-value: 1.25e-106
S-adenosylmethionine:tRNA-ribosyltransferase-isomerase (queuine synthetase) [Translation, ribosomal structure and biogenesis]; S-adenosylmethionine:tRNA-ribosyltransferase-isomerase (queuine synthetase) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440571 [Multi-domain] Cd Length: 340 Bit Score: 472.19 E-value: 2.17e-167
Queuosine biosynthesis protein; Queuosine (Q) biosynthesis protein, or S-adenosylmethionine: ...
11-403
1.45e-136
Queuosine biosynthesis protein; Queuosine (Q) biosynthesis protein, or S-adenosylmethionine:tRNA -ribosyltransferase-isomerase, is required for the synthesis of the queuosine precursor (oQ). It catalyzes the transfer and isomerization of the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to form epoxyqueuosine (oQ-tRNA). Q is a hypermodified nucleoside usually found at the first position of the anticodon of asparagine, aspartate, histidine, and tyrosine tRNAs. In Streptococcus gordonii, QueA has been shown to play a role in the regulation of arginine deiminase genes.
Pssm-ID: 460587 [Multi-domain] Cd Length: 336 Bit Score: 393.67 E-value: 1.45e-136
S-adenosylmethionine:tRNA ribosyltransferase-isomerase; This model describes the enzyme for ...
11-404
1.25e-106
S-adenosylmethionine:tRNA ribosyltransferase-isomerase; This model describes the enzyme for S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA). QueA synthesizes Queuosine which is usually in the first position of the anticodon of tRNAs specific for asparagine, aspartate, histidine, and tyrosine. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 272912 [Multi-domain] Cd Length: 344 Bit Score: 317.86 E-value: 1.25e-106
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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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,
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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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(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
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
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