Protein Domain : IPR002904

Type:  Family Name:  Lysine-tRNA ligase
Description:  Lysine-tRNA ligase (also known as Lysyl-tRNA synthetase) () is an alpha 2 homodimer that belong to both class I and class II. In eubacteria and eukaryota lysine-tRNA ligases belong to class II in the same family as aspartyl tRNA ligase. The class Ic lysine-tRNA ligase family is present in archaea and in a number of bacterial groups that include the alphaproteobacteria and spirochaetes[]. A refined crystal structures shows that the active site of LysU is shaped to position the substrates for the nucleophilic attack of the lysine carboxylate on the ATP alpha-phosphate. No residues are directly involved in catalysis, but a number of highly conserved amino acids and three metal ions coordinate the substrates and stabilise the pentavalent transition state. A loop close to the catalytic pocket, disordered in the lysine-bound structure, becomes ordered upon adenine binding [].The aminoacyl-tRNA synthetase (also known as aminoacyl-tRNA ligase) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. 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 []. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [, , ]. However, tRNA binding involves an alpha-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 and valine belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine 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. Short Name:  Lys-tRNA-ligase
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0 Child Features

4 Contains

DB identifier Type Name
IPR014729 Domain Rossmann-like alpha/beta/alpha sandwich fold
IPR020751 Domain Aminoacyl-tRNA synthetase, class I, anticodon-binding domain, subdomain 2
IPR008925 Domain Aminoacyl-tRNA synthetase, class I, anticodon-binding
IPR001412 Conserved_site Aminoacyl-tRNA synthetase, class I, conserved site

2 Cross Referencess

Identifier
TIGR00467
MF_00177

0 Found In

5 GO Annotations

GO Term Gene Name
GO:0000166 IPR002904
GO:0004824 IPR002904
GO:0005524 IPR002904
GO:0006430 IPR002904
GO:0005737 IPR002904

5 Ontology Annotations

GO Term Gene Name
GO:0000166 IPR002904
GO:0004824 IPR002904
GO:0005524 IPR002904
GO:0006430 IPR002904
GO:0005737 IPR002904

0 Parent Features

0 Proteins

8 Publications

First Author Title Year Journal Volume Pages PubMed ID
            8364025
            8274143
            1852601
            2053131
            10673435
            2203971
            9353192
            10913247