id: Pfam:PF01868
pfam_id: PF01868
name: Ribonuclease P/MRP, subunit p29
short_name: RNase_P-MRP_p29
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01868
counters:
  proteins: 4328
  matches: 4328
  proteomes: 3725
  taxa: 9455
  structures: 19
  alphafold_models: 3775
  domain_architectures: 51
provenance:
  snapshot_id: interpro-pfam-duf-2026-10-10
  path: data/worklists/interpro-pfam-duf-2026-10-10.json
  sha256: 17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383
  generated_at: '2026-10-10T07:44:21.614711Z'
  source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/
interpro_id: InterPro:IPR002730
description: This family consists of several archaeal and eukaryotic proteins. The archaeal proteins are
  found to be expressed within ribosomal operons and several of the sequences are described as ribonuclease
  P protein subunit p29 proteins [[cite:PUB00042726],[cite:PUB00028005]]. 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 [[cite:PUB00028005]]. Rpp29 catalyses the
  endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with
  the Rpp25 and Pop5 subunits.