Member database | Pfam |
Pfam type | family |
Short name | RNase_P_Rpp14 |
Clan | Rpp14-Pop5-like |
Author | Enright A;0000-0002-6090-3100 Ouzounis C;0000-0002-0086-8657 Bateman A;0000-0002-6982-4660 Cerutti L; Dlakic M;0000-0003-4315-1514 |
Sequence Ontology | 0100021 |
Description
tRNA processing enzyme ribonuclease P (RNase P) is a ubiquitous ribozyme that catalyzes a Mg2-dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA). Archaeal and eukaryotic RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins
[1]. Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14- (Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer. This family includes Rnp2 (also known as Pop5) from archaea
[2] and Pop5/Rpp14 from eukaryotes
[3, 4].
References
1.Rpp14 and Rpp29, two protein subunits of human ribonuclease P. Jarrous N, Eder PS, Wesolowski D, Altman S. RNA 5, 153-7, (1999). View articlePMID: 10024167
2.Characterization of the archaeal ribonuclease P proteins from Pyrococcus horikoshii OT3. Terada A, Honda T, Fukuhara H, Hada K, Kimura M. J Biochem 140, 293-8, (2006). PMID: 16829535
Integrated to
Representative structure
2czv: Crystal structure of archeal RNase P protein ph1481p in complex with ph1877p