POP4

A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes and archaeal proteins.
POP4
SMART accession number:SM00538
Description: -
Interpro abstract (IPR002730):

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 [(PUBMED:28971852)].

Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP [(PUBMED: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 [(PUBMED:15916546)]. Despite its name, the vast majority of RNase MRP is localized in the nucleolus [(PUBMED: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) [(PUBMED:21665995)].

This entry includes p29 subunit (also known as Rpp29 or Pop4) of the Ribonuclease P complex [(PUBMED: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 [(PUBMED:14673079)]. Rpp29 (EC 3.1.26.5) catalyses the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits.

GO process:RNA processing (GO:0006396)
GO component:ribonuclease P complex (GO:0030677)
GO function:ribonuclease activity (GO:0004540), RNA binding (GO:0003723)
Family alignment:
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There are 240 POP4 domains in 240 proteins in SMART's nrdb database.

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