id: Pfam:PF14574
pfam_id: PF14574
name: C-terminal domain of RACo the ASKHA domain
short_name: RACo_C_ter
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF14574
counters:
  proteins: 2800
  matches: 2825
  proteomes: 1992
  taxa: 3671
  structures: 2
  alphafold_models: 2089
  domain_architectures: 28
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:IPR027980
description: 'This family includes reductive activator of CoFeSP (RACo) proteins, [swissprot:Q3ACS2].
  Structure analysis of RACo indicate that it contains 4 regions: N-terminal region [pfam:PF00111] (residues
  3-94) binding the [2Fe-2S] cluster, a linker region (residues 95-125), the middle region (residues 126-206),
  and the large C-terminal domain (residues 207-630). This entry is specific for the C-terminal domain
  which harbors the ATP-binding site. Structural studies show that the C-terminal domain contains the
  conserved beta-beta-beta-alpha-beta-alpha-beta-alpha topology characteristic of the ASKHA (acetate and
  sugar kinases/heat shock protein 70/actin). Despite the low-sequence identity shared between members
  of the ASKHA super family, they show a common central fold. Members of the ASKHA include proteins that
  catalyze phosphoryl transfers or hydrolysis of ATP in a variety of biological contexts. Asp, Asn, Glu,
  and Gln residues are well conserved in the core of the ASKHA proteins, where they interact with the
  phosphates of ATP and the bound Mg2+ ions.'