HMM Summary Page: TIGR03439

Functionprobable methyltransferase domain, EasF family
Trusted Cutoff205.55
Domain Trusted Cutoff205.55
Noise Cutoff205.25
Domain Noise Cutoff205.25
Isology Typesubfamily_domain
EC Number2.1.1.-
HMM Length321
AuthorHaft DH, Fedorova N
Entry DateJun 19 2007 9:33AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis model represents an uncharacterized domain of about 300 amino acids with homology to S-adenosylmethionine-dependent methyltransferases. Proteins with this domain are exclusively fungal. A few, such as EasF from Neotyphodium lolii, are associated with the biosynthesis of ergot alkaloids, a class of fungal secondary metabolites. EasF may, in fact, be the AdoMet:dimethylallyltryptophan N-methyltransferase, the enzyme that follows tryptophan dimethylallyltransferase (DMATS) in ergot alkaloid biosynthesis. Several other members of this family, including mug158 (meiotically up-regulated gene 158 protein) from Schizosaccharomyces pombe, contain an additional uncharacterized domain DUF323 (PF03781).
ReferencesRN [1] RM PMID:1880714 RT Steric course of the N-methylation in the biosynthesis of ergot alkaloids by Claviceps purpurea. RA Groger D, Groger L, D'Amico D, He MX, Floss HG RL J Basic Microbiol. 1991;31(2):121-5.