id: Pfam:PF01641
pfam_id: PF01641
name: SelR domain
short_name: SelR
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01641
counters:
  proteins: 30911
  matches: 30990
  proteomes: 19951
  taxa: 31866
  structures: 22
  alphafold_models: 21713
  domain_architectures: 157
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:IPR002579
description: Methionine sulfoxide reduction is an important process, by which cells regulate biological
  processes and cope with oxidative stress. MsrA, a protein involved in the reduction of methionine sulfoxides
  in proteins, has been known for four decades and has been extensively characterised with respect to
  structure and function. However, recent studies revealed that MsrA is only specific for methionine-S-sulfoxides.
  Because oxidised methionines occur in a mixture of R and S isomers in vivo, it was unclear how stereo-specific
  MsrA could be responsible for the reduction of all protein methionine sulfoxides. It appears that a
  second methionine sulfoxide reductase, SelR, evolved that is specific for methionine-R-sulfoxides, the
  activity that is different but complementary to that of MsrA. Thus, these proteins, working together,
  could reduce both stereoisomers of methionine sulfoxide. This domain is found both in SelR proteins
  and fused with the peptide methionine sulfoxide reductase enzymatic domain [pfam:PF01625]. The domain
  has two conserved cysteines and histidines. The domain binds both selenium and zinc [[cite:PUB00020323]].
  The final cysteine is found to be replaced by the rare amino acid selenocysteine in some members of
  the family [[cite:PUB00006463]]. This family has methionine-R-sulfoxide reductase activity [[cite:PUB00020323]].