tRNA G37 N-methylase TrmD [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase TrmD is part of the Pathway/BioSystem: tRNA modification
:
Pssm-ID: 440105 Cd Length: 242 Bit Score: 443.69 E-value: 2.70e-160
tRNA G37 N-methylase TrmD [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase TrmD is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440105 Cd Length: 242 Bit Score: 443.69 E-value: 2.70e-160
tRNA-M1G37-methyltransferase TrmD; The bacterial tRNA-(N(1)G37) methyltransferase (TrmD) ...
5-223
9.11e-140
tRNA-M1G37-methyltransferase TrmD; The bacterial tRNA-(N(1)G37) methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the N1 position of G37 in the anticodon loop of a subset of tRNA that contains a G at position 36. The presence of the modification prevents Watson-Crick base-pairing of this guanosine with cytosine in mRNA and translational frame-shifting. This family of proteins contains members of the SPOUT methyltransferases. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.
Pssm-ID: 349953 Cd Length: 219 Bit Score: 390.99 E-value: 9.11e-140
tRNA (guanine-N1)-methyltransferase; This model is specfic for the tRNA modification enzyme ...
4-238
4.56e-122
tRNA (guanine-N1)-methyltransferase; This model is specfic for the tRNA modification enzyme tRNA (guanine-N1)-methyltransferase (trmD). This enzyme methylates guanosime-37 in a number of tRNAs.The enzyme's catalytic activity is as follows: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 129196 [Multi-domain] Cd Length: 233 Bit Score: 346.70 E-value: 4.56e-122
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
26-223
2.85e-61
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC:2.1.1.31. In E.coli K12 this enzyme catalyzes the conversion of a guanosine residue to N1-methylguanine in position 37, next to the anticodon, in tRNA.
Pssm-ID: 396350 Cd Length: 182 Bit Score: 190.63 E-value: 2.85e-61
tRNA G37 N-methylase TrmD [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase TrmD is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440105 Cd Length: 242 Bit Score: 443.69 E-value: 2.70e-160
tRNA-M1G37-methyltransferase TrmD; The bacterial tRNA-(N(1)G37) methyltransferase (TrmD) ...
5-223
9.11e-140
tRNA-M1G37-methyltransferase TrmD; The bacterial tRNA-(N(1)G37) methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the N1 position of G37 in the anticodon loop of a subset of tRNA that contains a G at position 36. The presence of the modification prevents Watson-Crick base-pairing of this guanosine with cytosine in mRNA and translational frame-shifting. This family of proteins contains members of the SPOUT methyltransferases. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.
Pssm-ID: 349953 Cd Length: 219 Bit Score: 390.99 E-value: 9.11e-140
tRNA (guanine-N1)-methyltransferase; This model is specfic for the tRNA modification enzyme ...
4-238
4.56e-122
tRNA (guanine-N1)-methyltransferase; This model is specfic for the tRNA modification enzyme tRNA (guanine-N1)-methyltransferase (trmD). This enzyme methylates guanosime-37 in a number of tRNAs.The enzyme's catalytic activity is as follows: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 129196 [Multi-domain] Cd Length: 233 Bit Score: 346.70 E-value: 4.56e-122
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
26-223
2.85e-61
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC:2.1.1.31. In E.coli K12 this enzyme catalyzes the conversion of a guanosine residue to N1-methylguanine in position 37, next to the anticodon, in tRNA.
Pssm-ID: 396350 Cd Length: 182 Bit Score: 190.63 E-value: 2.85e-61
SPOUT superfamily of SAM-dependent RNA methyltransferases; The SPOUT (SpoU-TrmD) ...
87-155
1.46e-04
SPOUT superfamily of SAM-dependent RNA methyltransferases; The SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, also known as class IV methyltransferase family, is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot. Members of the SPOUT superfamily that have been characterized functionally are involved in post-transcriptional RNA modification by catalyzing methylation of the 2-OH group of ribose, the N-1 atom of guanosine 37 in tRNA, or the N-3 atom of uridine 1498 in 16S rRNA.
Pssm-ID: 349952 Cd Length: 99 Bit Score: 39.73 E-value: 1.46e-04
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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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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Domains are color coded according to superfamilies
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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,
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
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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
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