Ribonuclease P/MRP, subunit p29 (IPR002730)

Short name: RNase_P/MRP_p29

Overlapping homologous superfamilies

Domain relationships



RNase P is a ubiquitous ribonucleoprotein enzyme primarily responsible for cleaving the 5' leader sequence during maturation of tRNAs in all three domains of life. In bacteria, the catalytic RNA (typically ~120 kDa) is aided by a small protein cofactor (~14 kDa), while eukaryotic RNase P is a large RNP complex containing at least nine protein components [PMID: 28971852].

Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP [PMID: 28971852]. RNase MRP (mitochondrial RNA processing) is an rRNA processing enzyme that cleaves a specific site within precursor rRNA to generate the mature 5'-end of 5.8S rRNA [PMID: 15916546]. Despite its name, the vast majority of RNase MRP is localized in the nucleolus [PMID: 20627997]. RNase MRP has been shown to cleave primers for mitochondrial DNA replication and CLB2 mRNA. In yeast, RNase MRP possesses one putatively catalytic RNA and at least 9 protein subunits (Pop1, Pop3-Pop8, Rpp1, Snm1 and Rmp1) [PMID: 21665995].

This entry includes p29 subunit (also known as Rpp29 or Pop4) of the Ribonuclease P complex [PMID: 10352175]. Its homologues from eukaryotes are also a subunit of the RNase MRP complex. The structure of the RNase P subunit, Rpp29, from Methanobacterium thermoautotrophicum has been determined. Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. It contains a structured beta-barrel core and unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues that could be involved in RNA contacts in the protein-RNA complex [PMID: 14673079]. Rpp29 (EC: catalyses the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits.

GO terms

Biological Process

GO:0006396 RNA processing

Molecular Function

GO:0003723 RNA binding
GO:0004540 ribonuclease activity

Cellular Component

GO:0030677 ribonuclease P complex

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.