id: Pfam:PF02457
pfam_id: PF02457
name: DisA bacterial checkpoint controller nucleotide-binding
short_name: DAC
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF02457
counters:
  proteins: 11457
  matches: 11457
  proteomes: 9309
  taxa: 14001
  structures: 71
  alphafold_models: 7613
  domain_architectures: 47
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:IPR003390
description: The DisA protein is a bacterial checkpoint protein that dimerises into an octameric complex.
  The protein consists of three distinct domains. This domain is the first and is a globular, nucleotide-binding
  region; the next 146-289 residues constitute the DisA-linker family, [pfam:PF10635], that consists of
  an elongated bundle of three alpha helices (alpha-6, alpha-10, and alpha-11), one side of which carries
  an additional three helices (alpha7-9), which thus forms a spine like-linker between domains 1 and 3.
  The C-terminal residues, of domain 3, are represented by family HHH, [pfam:PF00633], the specific DNA-binding
  domain. The octameric complex thus has structurally linked nucleotide-binding and DNA-binding HhH domains
  and the nucleotide-binding domains are bound to a cyclic di-adenosine phosphate such that DisA is a
  specific di-adenylate cyclase. This N-terminal domain has been identified as a diadenylate cyclase (DAC)
  responsible for producing c-di-AMP from two molecules of ATP [[cite:PUB00109173]]. The di-adenylate
  cyclase activity is strongly suppressed by binding to branched DNA, but not to duplex or single-stranded
  DNA, suggesting a role for DisA as a monitor of the presence of stalled replication forks or recombination
  intermediates via DNA structure-modulated c-di-AMP synthesis [[cite:PUB00044227]].