id: Pfam:PF04079
pfam_id: PF04079
name: Segregation and condensation complex subunit ScpB
short_name: SMC_ScpB
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF04079
counters:
  proteins: 15280
  matches: 15281
  proteomes: 14360
  taxa: 20342
  structures: 6
  alphafold_models: 9916
  domain_architectures: 15
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:IPR005234
description: This is a family of prokaryotic proteins that form one of the subunits, ScpB, of the segregation
  and condensation complex, condensin, that plays a key role in the maintenance of the chromosome. In
  prokaryotes the complex consists of three proteins, SMC, ScpA (kleisin) and ScpB. ScpB dimerises and
  binds to ScpA. As originally predicted, ScpB is structurally a winged-helix at both its N- and C-terminal
  halves. IN Bacillus subtilis,one Smc dimer is bridged by a single ScpAB to generate asymmetric tripartite
  rings analogous to eukaryotic SMC complex ring-shaped assemblies [[cite:PUB00109191],[cite:PUB00109192]].