{PDOC00558} {PS00648; RIBONUCLEASE_P} {BEGIN} ******************************************************** * Bacterial ribonuclease P protein component signature * ******************************************************** Ribonuclease P (EC 3.1.26.5) (RNase P) [1,2,3] is a site specific endonuclease that generates mature tRNAs by cleaving-off the leader sequences at their 5'ends. In bacteria RNase P is known to be composed of two components: a large (about 400 base pairs) RNA (gene rnpB) and a small protein (119 to 133 amino acids) (gene rnpA). The RNA moiety of RNase P carries the catalytic activity; the function of the protein component is not yet clear although it may act as an electrostatic screen allowing the highly negatively charged RNA enzyme- substrate complex to fold into the catalytic conformation. The sequence of rnpA is not highly conserved, however there is, in the central part of the protein, a conserved basic region. We have used this region as a signature pattern. -Consensus pattern: [LIVMFYSNAD]-x(2)-A-x(2)-R-[NH]-[KRQLYAT]-[LIVMFSA]-[KRA]- R-x-[LIVMTA]-[KR] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: 2. -Last update: December 2004 / Pattern and text revised. [ 1] Pace N.R., Smith D. "Ribonuclease P: function and variation." J. Biol. Chem. 265:3587-3590(1990). PubMed=1689306 [ 2] Altman S. "Ribonuclease P. Postscript." J. Biol. Chem. 265:20053-20056(1990). PubMed=1700778 [ 3] Brown J.W., Pace N.R. "Ribonuclease P RNA and protein subunits from bacteria." Nucleic Acids Res. 20:1451-1456(1992). PubMed=1374553 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}