{"metadata":{"accession":"PF04174","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR007302","hierarchy":null,"name":{"name":"A circularly permuted ATPgrasp","short":"CP_ATPgrasp_1"},"description":[{"text":"<p>An ATP-grasp family that is present both as catalytically active and inactive versions. Contextual analysis suggests that  it functions in a distinct peptide synthesis/modification system that additionally contains a transglutaminase, an NTN-hydrolase, the Alpha-E domain, and a transglutaminase fused N-terminal to a  circularly permuted COOH-NH2 ligase. The inactive forms are often  fused N-terminal to the Alpha-E domain [[cite:PUB00057486]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00057486":{"PMID":20023723,"ISBN":null,"volume":"5","issue":"12","year":2009,"title":"Amidoligases with ATP-grasp, glutamine synthetase-like and acetyltransferase-like domains: synthesis of novel metabolites and peptide modifications of proteins.","URL":null,"raw_pages":"1636-60","medline_journal":"Mol Biosyst","ISO_journal":"Mol Biosyst","authors":["Iyer LM","Abhiman S","Maxwell Burroughs A","Aravind L."],"DOI_URL":"http://dx.doi.org/10.1039/b917682a"}},"set_info":{"accession":"CL0179","name":"ATP-grasp"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":7,"interactions":0,"matches":412,"pathways":0,"proteins":411,"proteomes":325,"sets":1,"structural_models":{"alphafold":306},"structures":0,"taxa":554},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":7,"alignment:full":178},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}