SMART: Pfam domain Methyltransf

The domain within your query sequence starts at position 111 and ends at position 343; the E-value for the Methyltransf_2 domain shown below is 2.8e-82.

LLLYLAGTTYLCWGHLADGVREGRSQYARAVGVDADDPFTAIYRSEAERLLFMRGLQETW
SLCGGRVLTAFDLSPFRVICDLGGGSGALARMAARLYPGSEVTVFETPDVVAAARAHFPP
PADEDGAEPRVCFLSGDFFRSPLPPADLYVLARVLHDWADAACVELLRRVRGALRPGGAV
LLVESVLSPGGAGPTRTLLLSLTMLLQARGRERTEAEYRALTARAGFSRLRLR

Methyltransf_2

PFAM accession number:	PF00891
Interpro abstract (IPR001077):	This domain includes a range of O-methyltransferases some of which utilise S-adenosyl methionine as substrate [ (PUBMED:8434913) ]. In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. In eukaryotes, DNA methylation has been implicated in the control of several cellular processes, including differentiation, gene regulation, and embryonic development. O-methyltransferases have a common catalytic domain structure, which might be universal among S-adenosyl-L-methionine (AdoMet)-dependent methyltransferases [ (PUBMED:7773746) ]. Comparative analysis of the predicted amino acid sequences of a number of plant O-methyltransferase cDNA clones show that they share some 32-71% sequence identity, and can be grouped according to the different compounds they utilise as substrates [ (PUBMED:9484457) ].
GO function:	O-methyltransferase activity (GO:0008171)

PFAM accession number:

PF00891

Interpro abstract (IPR001077):

This domain includes a range of O-methyltransferases some of which utilise S-adenosyl methionine as substrate [ (PUBMED:8434913) ]. In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. In eukaryotes, DNA methylation has been implicated in the control of several cellular processes, including differentiation, gene regulation, and embryonic development. O-methyltransferases have a common catalytic domain structure, which might be universal among S-adenosyl-L-methionine (AdoMet)-dependent methyltransferases [ (PUBMED:7773746) ].

Comparative analysis of the predicted amino acid sequences of a number of plant O-methyltransferase cDNA clones show that they share some 32-71% sequence identity, and can be grouped according to the different compounds they utilise as substrates [ (PUBMED:9484457) ].

GO function:

O-methyltransferase activity (GO:0008171)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Methyltransf_2