Aminoacyl-tRNA synthetase, class I, conserved site
IPR001412
Definition
This entry represents a conserved sequence in their N-terminal section of class I aminoacyl-tRNA synthetases. 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 [[cite:PMID:10704480], [cite: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 [[cite:PMID:8274143], [cite:PMID:2053131], [cite: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.
15 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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