| Primary Identifier | IPR002999 | Type | Domain |
| Short Name | Tudor |
| description | The drosophila Tudor protein, the founder of the Tudor domain family, is encoded by a 'posterior group' gene, which when mutated disrupt normal abdominal segmentation and pole cell formation. Another drosophila gene, homeless, is required for RNA localization during oogenesis. The tudor protein contains multiple repeats of a domain which is also found in homeless [, ].The tudor domain is found in many proteins that colocalise with ribonucleoprotein or single-strand DNA-associated complexes in the nucleus, in the mitochondrial membrane, or at kinetochores. At first it was not clear if the domain binds directly to RNA and ssDNA, or controls interactions with the nucleoprotein complexes but it is now known that this domain recognises and binds to methyl-arginine-lysine residues, playing important roles in diverse epigenetics, gene expression and the regulation of various small RNAs [, , ]. The tudor-containing protein homeless, also contains a zinc finger typical of RNA-binding proteins [].This domain has been implicated in protein-protein interactions in which methylated protein substrates bind to these domains. One example is the Tudor domain of Survival of Motor Neuron (SMN), linked to spinal muscular atrophy, which binds to symmetrically dimethylated arginines of arginine-glycine (RG) rich sequences found in the C-terminal tails of Sm proteins. The resolution of the solution structure of the Tudor domain of human SMN revealed that the Tudor domain forms a strongly bent antiparallel β-sheet with five strands forming a barrel-like fold. The structure exhibits a conserved negatively charged surface that interacts with the C-terminal Arg and Gly-rich tails of the spliceosomal Sm D1 and D3 proteins [, ]. |
