This is a PIN domain found in eukaryotic ribonuclease Nob1 and archaeal ribonuclease VapC1 [1]. Budding yeast Nob1 is involved in proteasomal and 40S ribosomal subunit biogenesis [2]. VapC1 is a toxic component and a ribonuclease of a toxin-antitoxin (TA) module [3]. PIN domains are small protein domains identified by the presence of three strictly conserved acidic residues. Apart from these three residues, there is poor sequence conservation [4]. PIN domains are found in eukaryotes, eubacteria and archaea. In eukaryotes they are ribonucleases involved in nonsense mediated mRNA decay [5] and in processing of 18S ribosomal RNA [6]. In prokaryotes, they are the toxic components of toxin-antitoxin (TA) systems, their toxicity arising by virtue of their ribonuclease activity. The PIN domain TA systems are now called VapBC TAs(virulence associated proteins), where VapB is the inhibitor and VapC, the PIN-domain ribonuclease toxin [4]. [1]. 22156373. Structural and functional analysis of the archaeal endonuclease Nob1. Veith T, Martin R, Wurm JP, Weis BL, Duchardt-Ferner E, Safferthal C, Hennig R, Mirus O, Bohnsack MT, Wohnert J, Schleiff E;. Nucleic Acids Res. 2012;40:3259-3274. [2]. 10675611. Nob1p, a new essential protein, associates with the 26S proteasome of growing saccharomyces cerevisiae cells. Tone Y, Tanahashi N, Tanaka K, Fujimuro M, Yokosawa H, Toh-e A;. Gene. 2000;243:37-45. [3]. 25391136. Analysis of non-typeable Haemophilous influenzae VapC1 mutations reveals structural features required for toxicity and flexibility in the active site. Hamilton B, Manzella A, Schmidt K, DiMarco V, Butler JS;. PLoS One. 2014;9:e1129. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-10-16