Summary: tRNA ribose 2'-O-methyltransferase, aTrm56
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tRNA ribose 2'-O-methyltransferase, aTrm56 Provide feedback
This family is an aTrm56 that catalyses the 2'-O-methylation of the cytidine residue in archaeal tRNA, using S-adenosyl-L-methionine. Biochemical assays showed that aTrm56 forms a dimer and prefers the L-shaped tRNA to the lambda form as its substrate [1] [2]. aTrm56 consists of the SPOUT domain, which contains the characteristic deep trefoil knot for AdoMet binding, and a unique C-terminal beta-hairpin [3].
Literature references
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Renalier MH, Joseph N, Gaspin C, Thebault P, Mougin A;, RNA. 2005;11:1051-1063.: The Cm56 tRNA modification in archaea is catalyzed either by a specific 2'-O-methylase, or a C/D sRNP. PUBMED:15987815 EPMC:15987815
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Clouet-d'Orval B, Gaspin C, Mougin A;, Biochimie. 2005;87:889-895.: Two different mechanisms for tRNA ribose methylation in Archaea: a short survey. PUBMED:16164996 EPMC:16164996
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Kuratani M, Bessho Y, Nishimoto M, Grosjean H, Yokoyama S;, J Mol Biol. 2008;375:1064-1075.: Crystal structure and mutational study of a unique SpoU family archaeal methylase that forms 2'-O-methylcytidine at position 56 of tRNA. PUBMED:18068186 EPMC:18068186
External database links
| PANDIT: | PF01994 |
| Pseudofam: | PF01994 |
| SYSTERS: | Trm56 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002845
This entry represents tRNA ribose 2'-O-methyltransferase aTrm56, which specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
The crystal structure of Pyrococcus horikoshii aTrm56 complexed with S-adenosyl-L-methionine has been determined to 2.48 A resolution. aTrm56 consists of the SPOUT domain, which contains the characteristic deep trefoil knot, and a unique C-terminal beta-hairpin [PUBMED:18068186].
A conserved cytidine at position 56 of tRNA contributes to the maintenance of the L-shaped tertiary structure. aTrm56 catalyzes the 2'-O-methylation of the cytidine residue in archaeal tRNA, using S-adenosyl-L-methionine. Biochemical assays showed that aTrm56 forms a dimer and prefers the L-shaped tRNA to the lambda form as its substrate [PUBMED:15987815, PUBMED:16164996].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | cytoplasm (GO:0005737) |
| Molecular function | tRNA methyltransferase activity (GO:0008175) |
| Biological process | tRNA nucleoside ribose methylation (GO:0002128) |
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 contains the following 11 members:
DUF2122 Methyltrans_RNA Methyltrn_RNA_2 Methyltrn_RNA_3 Methyltrn_RNA_4 RNA_Me_trans 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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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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 (31) |
Full (143) |
Representative proteomes | NCBI (146) |
Meta (75) |
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| RP15 (21) |
RP35 (53) |
RP55 (73) |
RP75 (88) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
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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 (31) |
Full (143) |
Representative proteomes | NCBI (146) |
Meta (75) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (21) |
RP35 (53) |
RP55 (73) |
RP75 (88) |
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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.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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: | Enright A |
| Previous IDs: | DUF127; |
| Type: | Family |
| Author: | Enright A, Ouzounis C, Bateman A |
| Number in seed: | 31 |
| Number in full: | 143 |
| Average length of the domain: | 121.00 aa |
| Average identity of full alignment: | 48 % |
| Average coverage of the sequence by the domain: | 66.03 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 121 | ||||||||||||
| Family (HMM) version: | 11 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
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 Trm56 domain has been found. There are 4 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 seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence