The domain within your query sequence starts at position 78 and ends at position 166; the E-value for the Arg_tRNA_synt_N domain shown below is 1.6e-27.



Arginyl tRNA synthetase N terminal dom
SMART accession number:SM01016
Description: This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). It is about 140 residues long and it has been suggested that this domain will be involved in tRNA recognition.
Interpro abstract (IPR005148):

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 [(PUBMED:10704480),(PUBMED:12458790)]. These proteins differ widely in size and oligomeric state, and have limited sequence homology [(PUBMED:2203971)]. 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 [(PUBMED:10673435)]. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [(PUBMED:8364025)], and are mostly dimeric or multimeric, containing at least three conserved regions [(PUBMED:8274143), (PUBMED:2053131), (PUBMED:1852601)]. 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, 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 [(PUBMED:10447505)].

This domain is found at the N terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). It is about 140 residues long and it has been suggested to be involved in tRNA recognition [(PUBMED:9736621)].

GO process:arginyl-tRNA aminoacylation (GO:0006420)
GO component:cytoplasm (GO:0005737)
GO function:ATP binding (GO:0005524), arginine-tRNA ligase activity (GO:0004814), nucleotide binding (GO:0000166)
Family alignment:
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There are 26085 Arg_tRNA_synt_N domains in 26083 proteins in SMART's nrdb database.

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