InterPro : IPR029063

Name  S-adenosyl-L-methionine-dependent methyltransferase Short Name  SAM-dependent_MTases
Type  Domain Description  This entry represents a domain found in S-adenosyl-L-methionine-dependent methyltransferases (SAM MTases). Proteins containing this domain include members from the methyltransferase superfamily and the class I-like SAM-binding methyltransferase superfamily. Methyltransferases transfer a methyl group from a donor to an acceptor. SAM-binding methyltransferases utilise the ubiquitous methyl donor SAM as a cofactor to methylate proteins, small molecules, lipids, and nucleic acids. All SAM MTasescontain a structurally conserved SAM-binding domain consisting of a central seven-stranded beta-sheet that is flanked by three alpha-helices per side of the sheet []. A review published in 2003 []divides all methyltransferases into 5 classes based on the structure of their catalytic domain (fold):class I: Rossmann-like alpha/betaclass II: TIM beta/alpha-barrel alpha/betaclass III: tetrapyrrole methylase alpha/betaclass IV: SPOUT alpha/beta class V: SET domain all beta Another paper []based on a study of the Saccharomyces cerevisiae methyltransferome argues for four more folds:class VI: transmembrane all alpha class VII: DNA/RNA-binding 3-helical bundle all alphaclass VIII: SSo0622-like alpha+betaclass IX: thymidylate synthetase alpha+betaThe vast majority of methyltransferases belong to the Rossmann-like fold (Class I) which consists in a seven-stranded beta sheet adjoined by alpha helices. The beta sheet contains a central topological switch-point resulting in a deep cleft in which SAM binds. Class I methyltransferases display two conserved positions, the first one is a GxGxG motif (or at least a GxG motif) at the end of the first beta strand which is characteristic of a nucleotide-binding site and is hence used to bind the adenosyl part of SAM, the second conserved position is an acidic residue at the end of the second beta strand that forms one hydrogen bond to each hydroxyl of the SAM ribose part. The core of these enzymes is composed by about 150 amino acids that show very strong spatial conservation [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



15 Child Features

Id Name Short Name Type
IPR015985 Tellurite resistance methyltransferase TehB-like domain TehB-like_dom Domain
IPR001678 SAM-dependent methyltransferase RsmB/NOP2-type MeTrfase_RsmB/NOP2 Domain
IPR013216 Methyltransferase type 11 Methyltransf_11 Domain
IPR030382 SAM-dependent methyltransferase TRM5/TYW2-type MeTrfase_TRM5/TYW2 Domain
IPR025714 Methyltransferase domain Methyltranfer_dom Domain
IPR002877 Ribosomal RNA methyltransferase FtsJ domain rRNA_MeTrfase_FtsJ_dom Domain
IPR007848 Methyltransferase small domain Small_mtfrase_dom Domain
IPR004971 mRNA (guanine-N(7))-methyltransferase domain mRNA_G-N7_MeTrfase_dom Domain
IPR025789 Histone-lysine N-methyltransferase DOT1 domain DOT1_dom Domain
IPR013110 Histone methylation DOT1 DOT1_dom_Pfam Domain
IPR030374 Polyamine biosynthesis domain PABS Domain
IPR001077 O-methyltransferase, family 2 O_MeTrfase_2 Domain
IPR022642 MCP methyltransferase, CheR-type, SAM-binding domain, C-terminal CheR_C Domain
IPR030380 SAM-dependent methyltransferase DRM SAM_MeTfrase_DRM Domain
IPR030384 SAM-dependent methyltransferase SMT-type MeTrfase_SMT Domain

0 Contains

0 Found In

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Schubert HL Many paths to methyltransfer: a chronicle of convergence. 2003 Trends Biochem Sci 28 329-35
Wlodarski T Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome. 2011 PLoS One 6 e23168
Martin JL SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. 2002 Curr Opin Struct Biol 12 783-93

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)