| Family: | TYROSYL-TRNA SYNTHETASE (PTHR11766) | ||
| Subfamilies: | 1 | ||
| PANTHER Links: |
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| Abstract: |
The aminoacyl-tRNA synthetases (EC: 6.1.1.-) 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 [PMID:2203971]. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold and are mostly monomeric [PMID:10673435], while class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet formation, flanked by alpha-helices [PMID:8364025], and are mostly dimeric or multimeric. 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 [PUB00015156]. The 10 class I synthetases are considered to have in common the catalytic domain structure based on the Rossmann fold, which is totally different from the class II catalytic domain structure. The class I synthetases are further divided into three subclasses, a, b and c, according to sequence homology. tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. The aminoacyl-tRNA synthetases (EC: 6.1.1.-) 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 [PMID:2203971]. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold and are mostly monomeric [PMID:10673435], while class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet formation, flanked by alpha-helices [PMID:8364025], and are mostly dimeric or multimeric. 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 [PUB00015156]. The 10 class I synthetases are considered to have in common the catalytic domain structure based on the Rossmann fold, which is totally different from the class II catalytic domain structure. The class I synthetases are further divided into three subclasses, a, b and c, according to sequence homology. tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. Tyrosyl-tRNA synthetase (EC: 6.1.1.1) is an alpha2 dimer that belongs to class Ib. Studies on tyrosyl-tRNA synthetase provide the first kinetic evidence that the 'KMSKS' motif plays a role in the initial binding of tRNA(Tyr) to tyrosyl-tRNA synthetase [PMID:10630994]. |
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| InterPro Accession: | IPR002307 | ||
| PANTHER Molecular Function: |
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| PANTHER Biological Process: |
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| Pathway Categories: | No pathway information available | ||
| Training Sequences: |
29
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| HMM Length | 425 | ||
| Downloads: | HMM (HMMER format) |
| Total | Celera | FlyBase | NCBI | |
| H. sapiens | 2 | 1 | 0 | 1 |
| M. musculus | 2 | 1 | 0 | 1 |
| R. norvegicus | 2 | 1 | 0 | 1 |
| D. melanogaster | 1 | 0 | 1 | 0 |




