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IPR000924

Description

IPR000924 is a Glutamyl/glutaminyl-tRNA synthetase.

<p>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 [[cite:PUB00103851], [cite:PUB00103850]].</p> <p>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 [[cite:PUB00006397]].</p> <p>The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [[cite:PUB00079872], [cite:PUB00079873]]. These proteins differ widely in size and oligomeric state, and have limited sequence homology [[cite:PUB00007191]]. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric [[cite:PUB00006477]]. Class II aminoacyl-tRNA synthetases share an anti-parallel β-sheet fold flanked by α-helices [[cite:PUB00000386]], and are mostly dimeric or multimeric, containing at least three conserved regions [[cite:PUB00000723], [cite:PUB00005365], [cite:PUB00004391]]. However, tRNA binding involves an α-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [[cite:PUB00007363]].</p>

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 , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Molecular function Nucleotide binding Interacting selectively and non-covalently with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
Molecular function Aminoacyl-tRNA ligase activity Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
Molecular function ATP binding Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
Biological process TRNA aminoacylation The chemical reactions and pathways by which the various amino acids become bonded to their corresponding tRNAs. The most common route for synthesis of aminoacyl tRNA is by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules.

Associated Lotus transcripts 7

Transcript Name Description Predicted domains Domain count
PREDICTED: glutamate--tRNA ligase, chloroplastic/mitochondrial-like [Cicer arietinum] gi|502155737|ref|XP_004510174.1| 23
PREDICTED: glutaminyl-tRNA synthetase-like isoform 1 [Glycine max] gi|356536302|ref|XP_003536678.1| 28
PREDICTED: probable glutamyl-tRNA synthetase, cytoplasmic-like [Glycine max] gi|356534931|ref|XP_003536004.1| 33
Glutamate--tRNA ligase; TAIR: AT5G64050.1 glutamate tRNA synthetase; Swiss-Prot: sp|Q9FEA2|SYEM_ARATH Glutamate--tRNA ligase, chloroplastic/mitochondrial; TrEMBL-Plants: tr|V7ALD7|V7ALD7_PHAVU Uncharacterized protein; Found in the gene: LotjaGi3g1v0075100 25
Glutamine--tRNA ligase; TAIR: AT1G25350.1 glutamine-tRNA ligase, putative / glutaminyl-tRNA synthetase, putative / GlnRS; Swiss-Prot: sp|P52780|SYQ_LUPLU Glutamine--tRNA ligase; TrEMBL-Plants: tr|A0A0B2PPT7|A0A0B2PPT7_GLYSO Glutamine--tRNA ligase; Found in the gene: LotjaGi4g1v0303500 29
Glutamate--tRNA ligase; TAIR: AT5G26710.1 Glutamyl/glutaminyl-tRNA synthetase, class Ic; Swiss-Prot: sp|O82462|SYEC_ARATH Glutamate--tRNA ligase, cytoplasmic; TrEMBL-Plants: tr|A0A0L9TZ06|A0A0L9TZ06_PHAAN Uncharacterized protein; Found in the gene: LotjaGi5g1v0005200 27
Glutamate--tRNA ligase; TAIR: AT5G26710.1 Glutamyl/glutaminyl-tRNA synthetase, class Ic; Swiss-Prot: sp|O82462|SYEC_ARATH Glutamate--tRNA ligase, cytoplasmic; TrEMBL-Plants: tr|A0A0L9TZ06|A0A0L9TZ06_PHAAN Uncharacterized protein; Found in the gene: LotjaGi5g1v0235000 31

Co-occuring domains 1

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

Predicted domain Source Observations Saturation (%)
cd10289 CDD 1 14.29