Description

IPR010280 is a (Uracil-5)-methyltransferase family.

<p>This family consists of (uracil-5-)-methyltransferases [ec:2.1.1.35] from bacteria, archaea and eukaryotes. They are class I-like SAM-binding methyltransferases.</p> <p>Methyltransferases (MTs) (EC 2.1.1.-) constitute an important class of enzymes present in every life form. They transfer a methyl group most frequently from S-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such as nitrogen, oxygen, sulfur or carbon leading to S-adenosyl-L-homocysteine (AdoHcy) and a methylated molecule. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids. MTs are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing [[cite:PUB00057957], [cite:PUB00054125], [cite:PUB00057958]].</p> <p>More than 230 different enzymatic reactions of MTs have been described so far, of which more than 220 use SAM as the methyl donor. A review published in 2003 [[cite:PUB00054125]] divides all MTs into 5 classes based on the structure of their catalytic domain (fold):</p> <ul> <li>class I: Rossmann-like α/β</li> <li>class II: TIM β/α-barrel α/β</li> <li>class III: tetrapyrrole methylase α/β</li> <li>class IV: SPOUT α/β</li> <li>class V: SET domain all β</li> </ul> <p>A more recent paper [[cite:PUB00057958]] based on a study of the Saccharomyces cerevisiae methyltransferome argues for four more folds:</p> <ul> <li>class VI: transmembrane all α</li> <li>class VII: DNA/RNA-binding 3-helical bundle all α</li> <li>class VIII: SSo0622-like α+β</li> <li>class IX: thymidylate synthetase α+β</li> </ul> <p>The vast majority of MTs belong to the Rossmann-like fold (Class I) which consists in a seven-stranded β-sheet adjoined by α-helices. The β-sheet contains a central topological switch-point resulting in a deep cleft in which SAM binds. Class I MTs display two conserved positions, the first one is a GxGxG motif (or at least a GxG motif) at the end of the first β-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 β-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. Catechol O-MT (EC 2.1.1.6) is the canonical Class I MT considering that it consists in the exact consensus structural core with no extra domain [[cite:PUB00054125]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 12

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: