The domain within your query sequence starts at position 125 and ends at position 216; the E-value for the POP4 domain shown below is 7.94e-41.

QMIQAKLLKADLHGAIISVTKSKCPSYVGVTGILLQETKHVFKIITREDHLKVIPKLNCV
FTIEIDDFISYIYGSKFQLRASERSAKKFKAK

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 ~120kDa) is aided by a small protein cofactor (~14kDa), 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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