{"metadata":{"accession":"PF12640","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR063574","hierarchy":null,"name":{"name":"Peptide arginase FlmR/OhkR-like, N-terminal domain","short":"FlmR_OhkR_N"},"description":[{"text":"<p>This entry represents a domain found at the N-terminal end of FlmR from Flagellimonas meridianipacifica (Swiss A0A2T0MFS9), OhkR from Ohtaekwangia koreensis (Swiss A0A1T5M544) and similar uncharacterised proteins found in animals and bacteria. FlmR and OhkR have been reported to be peptide arginases that modify Arg residues to ornithine in bioactive RiPP peptides [[cite:PUB00162570]]. This domain is predicted to adopt an alpha/beta arginase-like fold.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00162570":{"PMID":41201059,"ISBN":null,"volume":null,"issue":null,"year":2025,"title":"Peptide Arginases from Cryptic Pathways Install Ornithine Residues in Uncharacterized Members of Orphan RiPP Families.","URL":null,"raw_pages":"e202500658","medline_journal":"Chembiochem","ISO_journal":"Chembiochem","authors":["Pfeiffer IP","Schroder MP","Koutsandrea PH","Vitale GA","Herrera-Rosero D","Geibel C","Petras D","Piel J","Vagstad AL","Mordhorst S."],"DOI_URL":"https://doi.org/10.1002/cbic.202500658"}},"set_info":{"accession":"CL0302","name":"Arginase"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":33,"interactions":0,"matches":1816,"pathways":0,"proteins":1799,"proteomes":1333,"sets":1,"structural_models":{"alphafold":1530},"structures":1,"taxa":4226},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":11,"alignment:full":1358},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}