Protein Family Models

This domain can be found in Kae1/Qri7/YgjD, products of COG0533 that belong to a small group of 60 proteins that are present in all three domains of life. COG0533 proteins are suggest to play a role in a post translational modification of certain tRNAs. For example, YgjD along with YeaZ, YjeE, and YrdC have been deemed necessary and sufficient for the tRNA modification [1]. This modification involves the formation of N6-threonyl carbamoyl adenosine (t6A) at position 37 in the anti-codon stem loop which is critical for translational speed and accuracy [2]. Structural analysis indicate that YeaZ lacks resemblance to any known protease active site. Together with the absence of a putative zinc-binding motif. Thus the likelyhood of it being a protease, as previously thought, has been negated [1]. EC:2.3.1.234 [1]. 23471679. Crystal structure of the dimer of two essential Salmonella. typhimurium proteins, YgjD & YeaZ and calorimetric evidence for. the formation of a ternary YgjD-YeaZ-YjeE complex.. Nichols CE, Lamb HK, Thompson P, El Omari K, Lockyer M, Charles. I, Hawkins AR, Stammers DK;. Protein Sci. 2013;22:628-640.. [2]. 26798630. Global translational impacts of the loss of the tRNA. modification t(6)A in yeast.. Thiaville PC, Legendre R, Rojas-Benitez D, Baudin-Baillieu A,. Hatin I, Chalancon G, Glavic A, Namy O, de Crecy-Lagard V;. Microb Cell. 2016;3:29-45. (from Pfam)

Date:

2024-08-14

TsaD catalyzes the formation of a threonylcarbamoyl group at position 37 in tRNAs that read codons beginning with adenine.

Gene:

tsaD

Date:

2024-05-16

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD is part of the enzyme complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine

Date:

2017-05-31

This subfamily includes the well-studied secreted O-sialoglycoprotein endopeptidase (glycoprotease, EC 3.4.24.57) of Pasteurella haemolytica, a pathogen. A member from Riemerella anatipestifer, associated with cohemolysin activity, likewise is exported without benefit of a classical signal peptide and shows glycoprotease activity on the test substrate glycophorin. However, archaeal members of this subfamily show unrelated activities as demonstrated in Pyrococcus abyssi: DNA binding, iron binding, apurinic endonuclease activity, genomic association with a kinase domain, and no glycoprotease activity. This family thus pulls together a set of proteins as a homology group that appears to be near-universal in life, yet heterogeneous in assayed function between bacteria and archaea.

Gene:

tsaD

Date:

2019-09-10