InterPro : IPR008909

Name  DALR anticodon binding Short Name  DALR_anticod-bd
Type  Domain Description  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 [].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 all alpha helical domain is the anticodon binding domain (ABD) of arginyl tRNA synthetase, and also matches the ABD of some glycine tRNA synthetases. This domain is known as the DALR domain after characteristic conserved amino acids [].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

3 Found In

Id Name Short Name Type
IPR009080 Aminoacyl-tRNA synthetase, class 1a, anticodon-binding tRNAsynth_1a_anticodon-bd Domain
IPR001278 Arginine-tRNA ligase Arg-tRNA-ligase Family
IPR015944 Glycine-tRNA ligase, beta subunit Gly-tRNA-synth_bsu Family

1 Parent Features

Id Name Short Name Type
IPR009080 Aminoacyl-tRNA synthetase, class 1a, anticodon-binding tRNAsynth_1a_anticodon-bd Domain

2 Publications

First Author Title Year Journal Volume Pages
Wolf YI Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. 1999 Genome Res 9 689-710
Tang SN Evolution of different oligomeric glycyl-tRNA synthetases. 2005 FEBS Lett 579 1441-5



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)