id: Pfam:PF02577
pfam_id: PF02577
name: Bifunctional nuclease domain
short_name: BFN_dom
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF02577
counters:
  proteins: 9018
  matches: 9019
  proteomes: 7423
  taxa: 11314
  structures: 2
  alphafold_models: 6182
  domain_architectures: 42
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:IPR003729
description: This entry represents the bifunctional nuclease (BFN) domain which is specific to bacteria
  and plant organisms. It has both RNase and DNase activities [[cite:PUB00057454]]. The dimer of the BFN
  domain forms a wedge, each monomer being a basic triangular shape. The BFN domain is composed of an
  eight-stranded, distorted beta-sheet consisting of a four-stranded antiparallel beta-sheet, and a four-stranded
  mixed beta-sheet. This domain can be found in M. tuberculosis Carbon monoxide resistance (Cor) proteins.
  Cor consists entirely of this domain with homologues in a variety of organisms, including most mycobacteria,
  Bacteroides sp., Chlamydia sp., Streptomyces sp., and Rhodococcussp. One of the homologs from Oryza
  minuta protein OmBBD was reported to exhibit DNase and RNAse activity in vitro [[cite:PUB00057454]].
  OmBBD carries a C-terminal UvrB domain that is absent in the mycobacterial sequences. UvrB is one component
  of the UvrABC endonuclease system. Hence, it was proposed that OmBBD's observed nuclease activity may
  come not from this domain but from an interaction of the C-terminal UvrB with the catalytic UvrC nuclease
  [[cite:PUB00109344]].