id: Pfam:PF01877
pfam_id: PF01877
name: RNA binding
short_name: RNA_binding
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01877
counters:
  proteins: 1082
  matches: 1082
  proteomes: 562
  taxa: 1009
  structures: 7
  alphafold_models: 1034
  domain_architectures: 2
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:IPR002739
description: 'PH1010 [swissprot:O58738] is composed of five alpha-helices (1-5) and eight beta-strands
  (1-8) with the following topology: beta-1, alpha-1, beta-2, beta-3, alpha-2, alpha-3, beta-4, beta-5,
  alpha-4, beta-6, alpha-5, beta-7, beta-8. The first six beta-strands (1-6) form a slightly twisted antiparallel
  beta-sheet and face five alpha-helices on one side. The last two beta-strands form an antiparallel beta-sheet
  in the C-terminus. PH1010 forms a characteristic homodimer structure in the crystal. Dimerisation of
  the molecule is crucial for function. The structure resembles that of some ribosomal proteins such as
  the 50S ribosomal protein L5 [[cite:PUB00051274]]. Although the structure resembles that of the RRM-type
  RNA-binding domain of the ribosomal L5 protein, the residues involved in RNA-binding in the L5 protein
  are not conserved in this family [[cite:PUB00048377]]. Despite this, these proteins bind to double-stranded
  RNA in a non-sequence specific manner [[cite:PUB00066786]].'