id: Pfam:PF04424
pfam_id: PF04424
name: MINDY deubiquitinase
short_name: MINDY_DUB
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF04424
counters:
  proteins: 5182
  matches: 5756
  proteomes: 3009
  taxa: 7761
  structures: 11
  alphafold_models: 4396
  domain_architectures: 84
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:IPR033979
description: This entry represents a group of deubiquitinating (DUB) enzymes known as the MINDY family
  (MIU-containing novel DUB). Ubiquitin (Ub) is released one molecule at a time from the distal end of
  proteins with Lys48-linked polyubiquitin chains. Long polyubiquitin chains are preferred. The catalytic
  Cys and His residues have been identified by site-directed mutagenesis, as has the Gln that participates
  in formation of the oxyanion hole during catalysis. Despite the structural similarity to papain-like
  cysteine peptidases, a residue corresponding to the Asn that orientates the imidazolium ring of the
  catalytic His has not been identified. Members of the MINDY family of DUBs contain an MIU (motif interacting
  with Ub) motif, which is a helical motif that binds mono-Ub [[cite:PUB00081935]].