id: Pfam:PF01595
pfam_id: PF01595
name: Cyclin M transmembrane N-terminal domain
short_name: CNNM
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01595
counters:
  proteins: 56844
  matches: 56920
  proteomes: 21107
  taxa: 33615
  structures: 4
  alphafold_models: 38019
  domain_architectures: 249
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:IPR002550
description: This transmembrane domain is found in metal transporter proteins such as cyclin M 1/2 (CNNM).
  CNNMs are integral membrane proteins that are conserved from bacteria to humans. CNNM family members
  influence metal ion homeostasis through mechanisms that may not involve direct membrane transport of
  the ions. Structurally, CNNMs are complex proteins that contain an extracellular N-terminal domain preceding
  a transmembrane domain, a 'Bateman module', which consists of two cystathionine- beta-synthase (CBS)
  domains [pfam:PF00571], and a C-terminal cNMP (cyclic nucleotide monophosphate) binding domain [[cite:PUB00088668],[cite:PUB00088669],[cite:PUB00088670],[cite:PUB00088671]].
  This entry describes the CNNM transmembrane domain which contains four hydrophobic regions and forms
  a dimer through hydrophobic contacts between TM2 and TM3, in which each chain is composed of three transmembrane
  helices (TM1-3), a pair of short helices exposed on the intracellular side, and a juxtamembrane (JM)
  helix that forms a belt-like structure [[cite:PUB00088669],[cite:PUB00098586]]. The homodimer adopts
  an inward-facing conformation with a negatively charged cavity containing a conserved pi-helical turn
  in TM3 that coordinates a Mg2 ion [[cite:PUB00098586]].