The domain within your query sequence starts at position 1238 and ends at position 1337; the E-value for the Methyltransf_12 domain shown below is 2e-9.

AEVLAGEGHLYSRIPALLNTQPMLQLEYTATDRHPQALKDVQTKLQQHDVAQGQWNPSDP
APSSLGALDLLVCNCALATLGDPALALDNMVAALKEGGFL

Methyltransf_12

Methyltransf_12
PFAM accession number:PF08242
Interpro abstract (IPR013217):

Methyl transfer from the ubiquitous donor S-adenosyl-L-methionine (SAM) to either nitrogen, oxygen or carbon atoms is frequently employed in diverse organisms ranging from bacteria to plants and mammals. The reaction is catalyzed by methyltransferases (Mtases) and modifies DNA, RNA, proteins and small molecules, such as catechol for regulatory purposes. The various aspects of the role of DNA methylation in prokaryotic restriction-modification systems and in a number of cellular processes in eukaryotes including gene regulation and differentiation is well documented.

This entry represents a methyltransferase domain found in a large variety of SAM-dependent methyltransferases including, but not limited to:

  • Hexaprenyldihydroxybenzoate methyltransferase (EC 2.1.1.114), a mitochodrial enzyme involved in ubiquinone biosynthesis [(PUBMED:10419476)]
  • Fatty acid synthase (EC 2.3.1.85), a biosynthetic enzyme catalysing the formation of long-chain fatty acids
  • Glycine N-methyltransferase (EC 2.1.1.20) which catalyses the SAM-dependent methylation of glycine to form sarcosine and may play a role in regulating the methylation potential of the cell [(PUBMED:8281755)]
  • Enniatin synthetase, involved in non-ribosomal biosynthesis of cyclohexadepsipeptidase, enniatin [(PUBMED:10887181)]
  • Histamine N-methyltransferase (EC 2.1.1.8), a SAM-dependent histamine-inactivating enzyme [(PUBMED:11243563)]
  • A probable cobalt-precorrin-6Y C(15)-methyltransferase thought to be involved in adenosylcobalamin biosynthesis [(PUBMED:8501034)]
  • A polyketide synthase, important for the synthesis of chaetoviridin A and chaetomugilin A in the fungus Chaetomium [(PUBMED:26172141)].
Structural studies show that this domain forms the Rossman-like alpha-beta fold typical of SAM-dependent methyltransferases [(PUBMED:11746687), (PUBMED:8810903), (PUBMED:15340920)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Methyltransf_12