{"metadata":{"accession":"PF02082","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR000944","hierarchy":null,"name":{"name":"Iron-dependent Transcriptional regulator","short":"Rrf2"},"description":[{"text":"<p>Several proteins in this family form iron-sulfur clusters enabling iron dependent DNA transcription regulation [[cite:PUB00109206]]. The iron binding is mediated by three conserved cysteine residues. Members of this family can also bind O-acetyl-L-serine, [Fe-S] and nitric oxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00109206":{"PMID":23644595,"ISBN":null,"volume":"20","issue":"6","year":2013,"title":"Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity.","URL":null,"raw_pages":"740-7","medline_journal":"Nat Struct Mol Biol","ISO_journal":"Nat Struct Mol Biol","authors":["Rajagopalan S","Teter SJ","Zwart PH","Brennan RG","Phillips KJ","Kiley PJ."],"DOI_URL":null}},"set_info":{"accession":"CL0123","name":"HTH"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":34,"interactions":0,"matches":39881,"pathways":0,"proteins":39881,"proteomes":15706,"sets":1,"structural_models":{"alphafold":25715},"structures":21,"taxa":22367},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":93,"alignment:full":19625},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"2y75","name":"The Structure of CymR (YrzC) the Global Cysteine Regulator of B. subtilis"}}}