id: Pfam:PF06565
pfam_id: PF06565
name: DM10 domain
short_name: DM10_dom
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF06565
counters:
  proteins: 4090
  matches: 11385
  proteomes: 1456
  taxa: 4653
  structures: 25
  alphafold_models: 3629
  domain_architectures: 80
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:IPR006602
description: This entry represents the DM10 domain, which consists of approximately 105 residues whose
  function is unknown. It has been identified in nucleoside diphosphate kinases, namely Nucleoside diphosphate
  kinase 7 (NDK7), which contain a single copy of the DM10 domain [[cite:PUB00085676],[cite:PUB00087484]],
  and in uncharacterised proteins including Rib72 from Chlamydomonas and EF-hand domain-containing protein
  1/EF-hand domain-containing family member C2 (EFHC1/2) from mammals, which contain multiple copies of
  DM10 domains. In Chlamydomonas, and possibly mammals, DM10 domain-containing proteins are tightly bound
  to the flagellar doublet microtubules. This suggests that DM10 domains might act as flagellar NDK regulatory
  modules or as units specifically involved in axonemal targeting or assembly [[cite:PUB00043716],[cite:PUB00097750]].
  This domain have a PH-like fold which includes seven beta strands, with a short 3-4 residue helix after
  the first strand, and a more extended alpha helical region at the C terminus [[cite:PUB00087484],[cite:PUB00043716]].