Summary: RNA cap guanine-N2 methyltransferase
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RNA cap guanine-N2 methyltransferase Provide feedback
RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyse methylation of the exocyclic N2 amine of 7-methylguanosine .
Hausmann S, Ramirez A, Schneider S, Schwer B, Shuman S; , Nucleic Acids Res. 2007; [Epub ahead of print]: Biochemical and Genetic Analysis of RNA Cap Guanine-N2 Methyltransferases from Giardia lamblia and Schizosaccharomyces pombe. PUBMED:17284461 EPMC:17284461
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR019012
RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe (Fission yeast) trimethylguanosine synthase (Tgs1) and Giardia lamblia (Giardia intestinalis) Tgs2, catalyse the methylation step(s) for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure [PUBMED:17284461, PUBMED:18840651, PUBMED:15590684]. Trimethylguanosine synthase is specific for guanine, and N7 methylation must precede N2 methylation. This enzyme is required for pre-mRNA splicing, pre-rRNA processing and small ribosomal subunit synthesis. As such, this enzyme plays a role in transcriptional regulation.
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|Molecular function||methyltransferase activity (GO:0008168)|
|Biological process||RNA capping (GO:0009452)|
|RNA methylation (GO:0001510)|
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Curation and family details
|Seed source:||Pfam-B_9480 (Release 21.0)|
|Author:||Wood V, Bateman A|
|Number in seed:||11|
|Number in full:||426|
|Average length of the domain:||156.50 aa|
|Average identity of full alignment:||32 %|
|Average coverage of the sequence by the domain:||33.86 %|
|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:||5|
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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 Methyltransf_15 domain has been found. There are 7 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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