Aminoacyl-tRNA synthetase, class 1a, anticodon-binding (IPR009080)

Short name: tRNAsynth_1a_anticodon-bd

Domain relationships


Aminoacyl-tRNA synthetase (aaRS) is a key enzyme during protein biosynthesis. Each aaRS contains a catalytic central domain (CCD), responsible for activating amino acid, and an anticodon-binding domain (ABD), necessary for binding the anticodon in cognate tRNA. aaRSs are classified into class I and II (aaRS-I and aaRS-II) based on the topologies of CCDs. Whereas the structure of the CCDs is similar among the members of each of the two different aaRS classes, the ABDs are diverse in structure [PMID: 15733854].

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 []. Both classes of tRNA synthetases have been subdivided into three subclasses, designated Ia, Ib, Ic and IIa, IIb, IIc.

This domain represents the anticodon binding domain (ABD) of class Ia aminoacyl-tRNA synthetases, and also matches the ABD of glycine tRNA synthetases.

GO terms

Biological Process

GO:0006418 tRNA aminoacylation for protein translation

Molecular Function

GO:0005524 ATP binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0000166 nucleotide binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.