Aminoacyl tRNA synthetases, class II
| Aminoacyl-tRNA synthetase, class II (D, K and N) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | aa-tRNA-synt_II | ||||||||
| Pfam | PF00152 | ||||||||
| InterPro | IPR004364 | ||||||||
| CDD | cd00768 | ||||||||
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Aminoacyl-tRNA synthetase, class II (D, K and N) (EC 6.1.1.) is a protein domain that catalyses the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. This protein differs widely in size and oligomeric state, and has a limited sequence homology.[1]
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.[2] Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices,[3] and are mostly dimeric or multimeric, containing at least three conserved regions.[4][5][6] 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; these synthetases are further divided into three subclasses, a, b and c, according to sequence homology. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases.[7]
Human proteins containing this domain
References
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