id: Pfam:PF01995
pfam_id: PF01995
name: NrpR regulatory domains NRD1 and 2
short_name: NRD1_2
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01995
counters:
  proteins: 328
  matches: 398
  proteomes: 222
  taxa: 479
  structures: 1
  alphafold_models: 296
  domain_architectures: 3
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:IPR002846
description: This entry comprises two domains found in the nitrogen regulatory protein NrpR that bind
  DNA and repress transcription of nitrogen assimilation genes. The two NrpR regulatory domains (NRD1
  and NRD2) that sense and bind 2-oxoglutarate (2OG) are both structurally and functionally homologous
  and share a high degree of sequence conservation. Mutational analysis of NrpR from Methanococcus maripaludis
  (MmNrpR) indicated that the two most critical residues for 2OG binding are Cys389 and His435 (Cys395
  and His441, respectively in thermophilic archaeon Methanocaldococcus jannaschii (MjNrpR)). Both the
  Cys395 and His441 are conserved among NrpR proteins from diverse species [[cite:PUB00086621]].