Summary: tRNA (Guanine-1)-methyltransferase
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This is a family of tRNA (Guanine-1)-methyltransferases EC:184.108.40.206. 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 .
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
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR016009
In transfer RNA many different modified nucleosides are found, especially in the anticodon region.
tRNA (guanine-N1-)-methyltransferase EC is one of several nucleases operating together with the tRNA-modifying enzymes before the formation of the mature tRNA. It catalyses the reaction:
The mechanism of the trmD3-induced frameshift involving mutant tRNA(Pro) and tRNA(Leu) species has been investigated [PUBMED:7689113]. It has been suggested that the conformation of the anticodon loop may be a major determining element for the formation of m1G37 in vivo [PUBMED:9047363].
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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  (PFAM:PF00588 PFAM:PF01746). SPOUT is structurally distinct compared to more classical methyltransferases . 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  and reference therein. All members with known structure form homodimers.
The clan 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_MT
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_2049 (release 4.1)|
|Author:||Bashton M, Bateman A|
|Number in seed:||23|
|Number in full:||5148|
|Average length of the domain:||190.20 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||74.76 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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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 18 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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