InterPro : IPR007214

Name  YbaK/aminoacyl-tRNA synthetase-associated domain Short Name  YbaK/aa-tRNA-synth-assoc-dom
Type  Domain Description  Bacterial prolyl-tRNA synthetases and some smaller paralogues, YbaK and ProX, can hydrolyse misacylated Cys-tRNA(Pro) or Ala-tRNA(Pro) []. The small bacterial protein Ybak preferentially hydrolyses Cys-tRNA(Pro) and Cys-tRNA(Cys) [, ]. ProX functions in trans to edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro) []. Prolyl-tRNA synthetases main function is to catalyse the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro) [].This entry represents a domain characteristic of Ybak and ProX, that can also be found with other domains in prolyl-tRNA synthetases.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

4 Found In

Id Name Short Name Type
IPR004500 Prolyl-tRNA synthetase, class IIa, bacterial-type Pro-tRNA-synth_IIa_bac-type Family
IPR006195 Aminoacyl-tRNA synthetase, class II aa-tRNA-synth_II Domain
IPR004369 Prolyl-tRNA editing protein, YbaK/EbsC Prolyl-tRNA_editing_YbaK/EbsC Family
IPR014627 Uncharacterised conserved protein UCP036888, signal transduction HD-GYP-like, PA5346 type UCP036888_HDGYP-like Family

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Ruan B The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase. 2005 J Biol Chem 280 25887-91
Kumar S Aminoacyl-tRNA substrate and enzyme backbone atoms contribute to translational quality control by YbaK. 2013 J Phys Chem B 117 4521-7
Ahel I Trans-editing of mischarged tRNAs. 2003 Proc Natl Acad Sci U S A 100 15422-7
Stathopoulos C One polypeptide with two aminoacyl-tRNA synthetase activities. 2000 Science 287 479-82



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)