id: Pfam:PF06278
pfam_id: PF06278
name: Condensin II complex subunit CAP-H2 or CNDH2, N-terminal
short_name: CNDH2_N
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF06278
counters:
  proteins: 2090
  matches: 2104
  proteomes: 1328
  taxa: 4310
  structures: 1
  alphafold_models: 1748
  domain_architectures: 41
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:IPR009378
description: CNDH2_N is the N-terminal domain of the H2 subunit of the condensing II complex, found in
  eukaryotes but not in fungi. Eukaryotes carry at least two condensin complexes, I and II, each made
  up of five subunits. The functions of the two complexes are collaborative but non-overlapping. CI appears
  to be functional in G2 phase in the cytoplasm beginning the process of chromosomal lateral compaction
  while the CII is concentrated in the nucleus, possibly to counteract the activity of cohesion at this
  stage. In prophase, CII contributes to axial shortening of chromatids while CI continues to bring about
  lateral chromatid compaction, during which time the sister chromatids are joined centrally by cohesins.
  There appears to be just one condensin complex in fungi. CI and CII each contain SMC2 and SMC4 (structural
  maintenance of chromosomes) subunits, then CI has non-SMC CAP-D2 (CND1), CAP-G (CND3), and CAP-H (CND2).
  CII has, in addition to the two SMCs, CAP-D3, CAPG2 and CAP-H2. All four of the CAP-D and CAP-G subunits
  have degenerate HEAT repeats, whereas the CAP-H are kleisins or SMC-interacting proteins (ie they bind
  directly to the SMC subunits in the complex). The SMC molecules are each long with a small hinge-like
  knob at the free end of a longish strand, articulating with each other at the hinge. Each strand ends
  in a knob-like head that binds to one or other end of the CAP-H subunit. The HEAT-repeat containing
  D and G subunits bind side-by-side between the ends of the H subunit. Activity of the various parts
  of the complex seem to be triggered by extensive phosphorylations, eg, entry of the complex, in Sch.pombe,
  into the nucleus during mitosis is promoted by Cdk1 phosphorylation of SMC4/Cut3; and it has been shown
  that Cdk1 phosphorylates CAP-D3 at Thr1415 in He-La cells thus promoting early stage chromosomal condensation
  by CII.