id: Pfam:PF20208
pfam_id: PF20208
name: ARG and Rhodanese-Phosphatase-superfamily-associated Protein domain
short_name: ARPP-1
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF20208
counters:
  proteins: 313
  matches: 315
  proteomes: 283
  taxa: 687
  structures: 0
  alphafold_models: 230
  domain_architectures: 6
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:IPR046699
description: ARPP-1 shows a distinguishing group of absolutely conserved residues, including a cysteine
  and a glutamine, suggestive of enzymatic activity. Structural predictions reveal a core beta-sheet comprised
  of a duplicated four-stranded beta-meander with a beta-barrel domain bearing the absolutely conserved
  residues inserted into the first repeat. The unifying biochemical theme across its conserved contextual
  genome linkages is the presence of molecules with sugar moieties (ADPr, nucleotides, and polysaccharides).
  In genome contexts linking ARPP-1 with ARG and other counter viral ribosylation domains, ARPP is predicted
  to act on ribose moieties coming from ADPr. The presence of the conserved cysteine suggests that it
  could function analogous to the recently characterized SRAP domain by forming covalent cross-links with
  sugars [[cite:PUB00153825],[cite:PUB00153826]].