Summary: tRNA (Guanine-1)-methyltransferase
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tRNA (Guanine-1)-methyltransferase Provide feedback
This is a family of tRNA (Guanine-1)-methyltransferases EC:2.1.1.31. In E.coli K12 this enzyme catalyses the conversion of a guanosine residue to N1-methylguanine in position 37, next to the anticodon, in tRNA [1].
Literature references
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Hjalmarsson KJ, Bystrom AS, Bjork GR; , J Biol Chem 1983;258:1343-1351.: Purification and characterization of transfer RNA (guanine- 1)methyltransferase from Escherichia coli. PUBMED:6337136 EPMC:6337136
Internal database links
SCOOP: | SPOUT_MTase SPOUT_MTase_2 |
External database links
SCOP: | 1oy5 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR016009
This domain is found in tRNA methyltransferases including tRNA (guanine-N(1)-)-methyltransferases (TRMD) and mitochondrial ribonuclease P protein 1. Proteins containing this domain also include tRNA (guanine(9)-N1)-methyltransferase (Trm10) from yeasts.
Escherichia coli K12 tRNA (guanine-N(1)-)-methyltransferase catalyses the conversion of a guanosine residue to N1-methylguanine in position 37, next to the anticodon, in tRNA [PUBMED:6337136]. Mitochondrial RNase P (mtRNase P) functions in mitochondrial tRNA maturation [PUBMED:18984158].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan SPOUT (CL0098), which has the following description:
A distinct class of methylases that includes the SpoU and TrmD superfamilies and two superfamilies of predicted methylases defined by the YbeA and MJ0421 proteins in bacteria and archaea, respectively [1] (PFAM:PF00588 PFAM:PF01746). SPOUT is structurally distinct compared to more classical methyltransferases [1]. More specifically, the members of this clan form alpha/beta knots. Knots are extremely rare in protein structures as they pose a folding problem. The mechanism that allow a domain to be folded as a knot are unclear, but are discussed in [2] and reference therein. All members with known structure form homodimers.
The clan contains the following 13 members:
DUF2122 EMG1 Methyltrans_RNA Methyltrn_RNA_2 Methyltrn_RNA_3 Methyltrn_RNA_4 RNA_Me_trans SpoU_methylas_C SpoU_methylase SPOUT_MTase SPOUT_MTase_2 Trm56 tRNA_m1G_MTAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (15) |
Full (8712) |
Representative proteomes | UniProt (37109) |
NCBI (43016) |
Meta (2982) |
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RP15 (1289) |
RP35 (4138) |
RP55 (8217) |
RP75 (13791) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
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Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (15) |
Full (8712) |
Representative proteomes | UniProt (37109) |
NCBI (43016) |
Meta (2982) |
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---|---|---|---|---|---|---|---|---|---|
RP15 (1289) |
RP35 (4138) |
RP55 (8217) |
RP75 (13791) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_2049 (release 4.1) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Bashton M |
Number in seed: | 15 |
Number in full: | 8712 |
Average length of the domain: | 187.40 aa |
Average identity of full alignment: | 32 % |
Average coverage of the sequence by the domain: | 68.34 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 195 | ||||||||||||
Family (HMM) version: | 22 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Selections
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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Interactions
There is 1 interaction for this family. More...
tRNA_m1G_MTStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the tRNA_m1G_MT domain has been found. There are 140 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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