InterPro domain: IPR026904

This entry represents the C-terminal domain of MnmG (also known as GidA). It consists of 4 helices, the last three being rather short and forming small bundle [ 1 , 2 ]. MnmG is a tRNA modification enzyme found in bacteria and mitochondria that forms a complex with MnmE which is involved in the formation of methyluridine derivatives at the wobble uridine base in some tRNAs [ 3 , 4 , 5 ]. Based on mutational analysis this domain has been suggested to be implicated in binding of the D-stem of tRNA [ 6 ] and to be responsible for the interaction with protein MnmE [ 6 ].

1. Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate. J. Mol. Biol. 380, 532-47
2. Conserved cysteine residues of GidA are essential for biogenesis of 5-carboxymethylaminomethyluridine at tRNA anticodon. Structure 17, 713-24
3. Mitochondria-specific RNA-modifying enzymes responsible for the biosynthesis of the wobble base in mitochondrial tRNAs. Implications for the molecular pathogenesis of human mitochondrial diseases. J. Biol. Chem. 280, 1613-24
4. Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift. Genes Dev. 15, 2295-306
5. Evolutionarily conserved proteins MnmE and GidA catalyze the formation of two methyluridine derivatives at tRNA wobble positions. Nucleic Acids Res. 37, 7177-93