Protein Domain : tRNA N6-adenosine threonylcarbamoyltransferase, TsaD IPR022450

Type  Family
Description  This entry represents the TsaD protein family that is widely distributed. TsaD and its archaeal homologue Kae1 ( ) belong to the Kae1/TsaD family ( ), a conserved protein family with unknown function. This entry includes bacterial TsaD and its homologues, such as Qri7 (localize to the mitochondria) from budding yeast []. TsaD (also known as Gcp or YgjD) was originally described as a glycoprotease essential for cell viability [ ] and a critical mediator involved in the modification of cell wall peptidoglycan synthesis and/or cell division []. Gcp is a member of the Kae1/TsaD family, required for the formation of a threonylcarbamoyl group on adenosine at position 37 in tRNAs that read codons beginning with adenine []. YgjD has been renamed as TsaD, and it has been shown that YgjD and proteins YrdC (TsaC), YjeE (TsaE), and YeaZ (TsaB), are necessary and sufficient for t6A biosynthesis in vitro, and may constitute a complex [].The first characterised member of the Kae1/TsaD family was annotated as Gcp for O-sialoglycoprotein endopeptidase [ ], but this activity could not be confirmed []. Later, its homologue, Kae1 from Pyrococcus abyssi, has been shown to have DNA-binding properties and apurinic-endonuclease activity []. Members of this family have since been studied in yeast, archaea and bacteria resulting in sometimes conflicting data, several proposed functions and annotations but no definitive characterisation. For instance, some members have been linked to DNA maintenance in bacteria and mitochondria [] and transcription regulation and telomere homeostasis in eukaryotes [, ], but their function remained unclear. Recent research indicates that this family is involved in the biosynthesis of N6-threonylcarbamoyl adenosine, a universal modification found at position 37 of tRNAs that read codons beginning with adenine [, ].
Short Name  TsaD

0 Child Features

0 Gene Families

47 Genes

1 Ontology Annotations

1 Parent Features

11 Publications

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