InterPro : IPR009008

Name  Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain Short Name  Val/Leu/Ile-tRNA-synth_edit
Type  Domain Description  Certain aminoacyl-tRNA synthetases prevent potential errors in protein synthesis through deacylation of mischarged tRNAs. The close homologues isoleucyl-tRNA synthetase (IleRS) and valyl-tRNA synthetase (ValRS) deacylate Val-tRNAIle and Thr-tRNAVal, respectively. These reactions strictly require the presence of the cognate tRNA. In the absence of tRNA, the enzymatically generated misactivated adenylates remain in the active site, sequestered from hydrolysis. Upon addition of cognate tRNA the misactivated amino acids are hydrolysed, regenerating the free tRNA and amino acid, while converting 1 equivalent of ATP to AMP. A prominent mechanism for editing misactivated amino acids is the rapid hydrolysis of transiently mischarged tRNA. This reaction is catalysed at a second active site on IleRS and ValRS. This site is located within a large insertion (termed CP1) into the canonical class I aminoacyl-tRNA synthetase active-site fold [, ]. The CP1 domain as an isolated polypeptide hydrolyses its cognate mischarged tRNA [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR025709 Leucyl-tRNA synthetase, editing domain Leu_tRNA-synth_edit Domain

0 Contains

7 Found In

Id Name Short Name Type
IPR002300 Aminoacyl-tRNA synthetase, class Ia aa-tRNA-synth_Ia Domain
IPR002303 Valine-tRNA ligase Valyl-tRNA_ligase Family
IPR002302 Leucine-tRNA ligase Leu-tRNA-ligase Family
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold Rossmann-like_a/b/a_fold Domain
IPR002301 Isoleucine-tRNA ligase Ile-tRNA-ligase Family
IPR004493 Leucyl-tRNA synthetase, class Ia, archaeal/eukaryotic cytosolic Leu-tRNA-synth_Ia_arc/euk Family
IPR020791 Leucine-tRNA ligase, archaeal Leu-tRNA-lgase_arc Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Nordin BE Plasticity of recognition of the 3'-end of mischarged tRNA by class I aminoacyl-tRNA synthetases. 2002 J Biol Chem 277 20510-7
Fukunaga R Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase. 2006 J Mol Biol 359 901-12
Li L Leucyl-tRNA synthetase editing domain functions as a molecular rheostat to control codon ambiguity in Mycoplasma pathogens. 2013 Proc Natl Acad Sci U S A 110 3817-22



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)