id: Pfam:PF09418
pfam_id: PF09418
name: Non-canonical E2 ubiquitin-conjugating enzyme, DUF2009 family
short_name: DUF2009
seed_status: KNOWN_HISTORICAL_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF09418
counters:
  proteins: 924
  matches: 1077
  proteomes: 659
  taxa: 1643
  structures: 0
  alphafold_models: 769
  domain_architectures: 37
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:IPR057668
description: This entry represents a novel family of non-canonical E2 ubiquitin-conjugating enzymes that
  lack the typical HPN motif found in other E2 enzymes. The domain contains a highly conserved catalytic
  cysteine (C572 in PF3D7_0811400) that forms a thioester bond with ubiquitin. This was experimentally
  validated through mutational analysis and biochemical assays [[cite:PUB00160741]]. The domain is found
  in the C-terminal region of proteins, while the N-terminal region contains coiled helices involved in
  protein-protein interactions with other ubiquitin pathway components like Rbx1. The domain represents
  a new class of E2 enzymes particularly found in Apicomplexan parasites.