Protein Family Models

This domain is found at the C-terminal end of Carbamoyltransferase from Caldanaerobacter subterraneus (HypF, Swiss:Q8RDB0) and similar prokaryotic sequences. HypF is involved in the biosynthesis of the nitrile group as a precursor of the cyano groups of hydrogenases. HypF consists of four domains: the acylphosphatase domain (Pfam:PF00708), the Zn finger-like domain (Pfam:PF07503), the YrdC-like domain (Pfam:PF01300) and the Kae1 (kinase-associated endopeptidase 1)-like domain, which is composed of two alpha-beta subdomains (Pfam:PF17788 and this entry) [5]. Paper describing PDB structure 2ivn. [1]. 17766251. An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro. Hecker A, Leulliot N, Gadelle D, Graille M, Justome A, Dorlet P, Brochier C, Quevillon-Cheruel S, Le Cam E, van Tilbeurgh H, Forterre P;. Nucleic Acids Res. 2007;35:6042-6051. Paper describing PDB structure 2vwb. [2]. 19172740. Structure of the archaeal Kae1/Bud32 fusion protein MJ1130: a model for the eukaryotic EKC/KEOPS subcomplex. Hecker A, Lopreiato R, Graille M, Collinet B, Forterre P, Libri D, van Tilbeurgh H;. EMBO J. 2008;27:2340-2351. Paper describing PDB structure 3en9. [3]. 18951093. Atomic structure of the KEOPS complex: an ancient protein kinase-containing molecular machine. Mao DY, Neculai D, Downey M, Orlicky S, Haffani YZ, Ceccarelli DF, Ho JS, Szilard RK, Zhang W, Ho CS, Wan L, Fares C, Rumpel S, Kurinov I, Arrowsmith CH, Durocher D, Sicheri F;. Mol Cell. 2008;32:259-275. Paper describing PDB structure 3tsp. [4]. 22153500. Structure . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

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:

2024-10-16

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:

2024-05-07

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

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