Protein Family Models

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, in particular the small bundle, 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, Pfam:PF12631. This entry represents the first helices of the GidA associated domain. The last three helices are covered in Pfam:PF13932. [1]. 18565343. Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate. Meyer S, Scrima A, Versees W, Wittinghofer A;. J Mol Biol. 2008;380:532-547. [2]. 19446527. Conserved cysteine residues of GidA are essential for biogenesis of 5-carboxymethylaminomethyluridine at tRNA anticodon. Osawa T, Ito K, Inanaga H, Nureki O, Tomita K, Numata T;. Structure. 2009;17:713-724. [3]. 19801413. Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme. Shi R, Villarroya M, Ruiz-Partida R, Li Y, Proteau A, Prado S, Moukadiri I, Benitez-Paez A, Lomas R, Wagner J, Matte A, Velazquez-Campoy A, Armengod ME, Cygler M;. J Bacteriol. 2009;191:7614-7619. (from Pfam)

Date:

2024-10-16

The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, last three being rather short and forming small bundle and are represented in this entry. GidA is a tRNA modification enzyme found in bacteria and mitochondrial. Based on mutational analysis the C-terminal helices have been suggested to be implicated in binding of the D-stem of tRNA [2] and, specifically this domain, 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, Pfam:PF12631. [1]. 18565343. Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate. Meyer S, Scrima A, Versees W, Wittinghofer A;. J Mol Biol. 2008;380:532-547. [2]. 19446527. Conserved cysteine residues of GidA are essential for biogenesis of 5-carboxymethylaminomethyluridine at tRNA anticodon. Osawa T, Ito K, Inanaga H, Nureki O, Tomita K, Numata T;. Structure. 2009;17:713-724. [3]. 19801413. Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme. Shi R, Villarroya M, Ruiz-Partida R, Li Y, Proteau A, Prado S, Moukadiri I, Benitez-Paez A, Lomas R, Wagner J, Matte A, Velazquez-Campoy A, Armengod ME, Cygler M;. J Bacteriol. 2009;191:7614-7619. (from Pfam)

Date:

2024-10-16

This family of proteins contains FAD dependent oxidoreductases and related proteins. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

tRNA uridine-5-carboxymethylaminomethyl modification enzyme MnmG/GidA such as tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG, which is involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34

Date:

2024-07-19

MnmG, a tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme, was previously known as GidA (glucose-inhibited division protein A). It partners with MnmE, in an alpha2/beta2 heterotetramer, in the 5-carboxymethylaminomethyl modification of uridine 34 in certain tRNAs.

Gene:

mnmG

Date:

2024-07-09