| Ensembl ID | Symbol | Entrez ID | RBD | RBPome | PRI | Expresion | Pathway | Phenotype | Paralog | Ortholog | GO |
|---|---|---|---|---|---|---|---|---|---|---|---|
The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, the last three being rather short and forming small bundle. GidA is an tRNA modification enzyme found in bacteria and mitochondrial. Based on mutational analysis this domain has been suggested to be implicated in binding of the D-stem of tRNA [2] and to be responsible for the interaction with protein MnmE [1]. Structures of GidA in complex with either tRNA or MnmE are missing. Reported to bind to Pfam family MnmE, PF12631.
The GidA associated domain 3 is a motif that has been identified at the C terminus of protein GidA. It consists of 4 helices, the last three being rather short and forming small bundle at the top end of the first longer one. It is here named helical domain 3 because in GidA it is preceded by two other C-terminal helical domain (based on crystal structures [PUBMED:18565343, PUBMED:19446527]). GidA is an tRNA modification enzyme found in bacteria and mitochondria. Based on mutational analysis this domain has been suggested to be implicated in binding of the D-stem of tRNA [PUBMED:19446527] and to be responsible for the interaction with protein MnmE [PUBMED:18565343].
Meyer S, Scrima A, Versees W, Wittinghofer A;, J Mol Biol. 2008;380:532-547.: Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate. PUBMED:18565343 EPMC:18565343 .
Osawa T, Ito K, Inanaga H, Nureki O, Tomita K, Numata T;, Structure. 2009;17:713-724.: Conserved cysteine residues of GidA are essential for biogenesis of 5-carboxymethylaminomethyluridine at tRNA anticodon. PUBMED:19446527 EPMC:19446527.
