Description

IPR004526 is a Glutamyl-tRNA synthetase, archaeal/eukaryotic cytosolic.

This entry are mostly eukaryotic cytosolic and archaeal forms of the glutamyl-tRNA synthetase. The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. In many species, the charging of tRNA (gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes may act on both tRNA (gln) and tRNA (glu). Glutamate-tRNA ligase (also known as glutamyl-tRNA synthetase; [ec:6.1.1.17]) is a class I aminoacyl-tRNA synthetase. This enzyme shares similarities with glutaminyl-tRNA synthetase in terms of structure and catalytic properties. Glutamyl-tRNA synthetase (GluRS) and glutaminyl-tRNA synthetase (GlnRS) are grouped in the GlxRS subclass because of the shared evolutionary pathway of their catalytic domains. The catalytic domain of Glx subfamily is believed to be more ancient, having evolved from a common GluRS ancestor that contained only the catalytic domain. Anticodon binding domains of extant bacterial and eukaryotic/archeal GlxRS appeared independently at a later stage, with the anticodon-binding domain of bacterial GlnRS being acquired by an unique horizontal gene transfer event from the eukaryotic kingdom [[PMID:8078941], [PMID:9746349]]. Bacterial GluRS are divided into two groups -discriminatory GluRS (D-GluRS) and non-discriminatory GluRS (ND-GluRS). While D-GluRS exclusively catalyses the transfer of Glu to tRNA(Glu), the ND-GluRS can also glutamylate tRNA(Gln) forming Glu-tRNAGln. The misacylated product is then transformed to Gln-tRNA(Gln) by an enzyme known as glutamyl-tRNA(Gln) amidotransferase. The bacterial GluRS structure consists of four domains. The N-terminal half (domains 1 and 2) contains the 'Rossman fold' typical for class I aminoacyl-tRNA synthetases and resembles the corresponding part of GlnRS, whereas the C-terminal half exhibits a GluRS-specific structural features [[PMID:9426192]]. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [[PMID:10704480], [PMID:12458790]]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [[PMID:2203971]]. The 20 aminoacyl-tRNA synthetases are divided into two classes. Class I synthetases contain a characteristic Rossmann fold catalytic domain and are predominantly monomeric [[PMID:10673435]]. Class II synthetases feature an antiparallel β-sheet fold flanked by α-helices [[PMID:8364025]] and are mostly dimeric or multimeric, with at least three conserved regions [[PMID:8274143], [PMID:2053131], [PMID:1852601]]. Despite these structural differences, both classes share a conserved α-helical structure involved in tRNA binding. The two classes also differ in their catalytic mechanisms: class I synthetases couple the aminoacyl group to the 2'-hydroxyl of the tRNA, whereas class II synthetases preferentially use the 3'-hydroxyl site. Class I includes synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic). Class II includes those specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal). Based on their mode of binding to the tRNA acceptor stem, each class has been further subdivided into three subclasses: 1a, 1b, 1c and 2a, 2b, 2c [[PMID:10447505]].

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 3

Co-occuring domains 1

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