id: Pfam:PF01936
pfam_id: PF01936
name: NYN domain
short_name: NYN
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01936
counters:
  proteins: 25419
  matches: 25756
  proteomes: 13584
  taxa: 22386
  structures: 3
  alphafold_models: 16110
  domain_architectures: 329
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:IPR021139
description: These domains are found in the eukaryotic proteins typified by the Nedd4-binding protein
  1 and the bacterial YacP-like proteins (Nedd4-BP1, YacP nucleases; NYN domains). The NYN domain shares
  a common protein fold with two other previously characterized groups of nucleases, namely the PIN (PilT
  N-terminal) and FLAP/5' --> 3' exonuclease superfamilies. These proteins share a common set of 4 acidic
  conserved residues that are predicted to constitute their active site. Based on the conservation of
  the acidic residues and structural elements Aravind and colleagues suggest that PIN and NYN domains
  are likely to bind only a single metal ion, unlike the FLAP/5' --> 3' exonuclease superfamily, which
  binds two metal ions. Based on conserved gene neighborhoods Aravind and colleagues infer that the bacterial
  members are likely to be components of the processome/degradsome that process tRNAs or ribosomal RNAs.