PF01900

Rpp14/Pop5 family

Pfam entry
Member databasePfam
Pfam typefamily
Short nameRNase_P_Rpp14
ClanRpp14-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 Ontology0100021

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

3.Structural insight into precursor tRNA processing by yeast ribonuclease P. Lan P, Tan M, Zhang Y, Niu S, Chen J, Shi S, Qiu S, Wang X, Peng X, Cai G, Cheng H, Wu J, Li G, Lei M. Science 362, (2018). PMID: 30262633

4.Structural basis for activation of an archaeal ribonuclease P RNA by protein cofactors. Kimura M. Biosci Biotechnol Biochem 81, 1670-1680, (2017). PMID: 28715256

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