id: Pfam:PF16473
pfam_id: PF16473
name: 3'-5' exoribonuclease Rv2179c-like domain
short_name: Rv2179c-like
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF16473
counters:
  proteins: 2547
  matches: 2547
  proteomes: 2444
  taxa: 4185
  structures: 8
  alphafold_models: 1296
  domain_architectures: 18
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:IPR033390
description: This is a highly divergent 3' exoribonuclease family. The proteins constitute a typical RNase
  fold, where the active site residues form a magnesium catalytic centre. The protein of the solved structure
  readily cleaves 3' overhangs in a time-dependent manner. It is similar to DEDD-type RNases and is an
  unusual ATP-binding protein that binds ATP and dATP. It forms a dimer in solution and both protomers
  in the asymmetric unit bind a magnesium ion through Asp-6 in SwissProt:P9WJ73 [[cite:PUB00074134]].
  Proteins containing this domain also include 3'-5' exonuclease dexA from bacteriophage T4. It may play
  a role in the final step of host DNA degradation, by scavenging DNA into mononucleotides [[cite:PUB00078716],[cite:PUB00078717]].