{"metadata":{"accession":"PF04168","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR007296","hierarchy":null,"name":{"name":"A predicted alpha-helical domain with a conserved ER motif.","short":"Alpha-E"},"description":[{"text":"<p>An uncharacterized alpha helical domain containing a highly conserved ER motif and typically found as a tandem duplication. Contextual analysis suggests that it functions in a distinct peptide  synthesis/modification system comprising of a transglutaminase,  a peptidase of the NTN-hydrolase superfamily, an active and inactive  circularly permuted ATP-grasp domains and a transglutaminase fused  N-terminal to a circularly permuted COOH-NH2 ligase 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":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":17,"interactions":0,"matches":10891,"pathways":0,"proteins":10852,"proteomes":7165,"sets":0,"structural_models":{"alphafold":7027},"structures":0,"taxa":10082},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":279,"alignment:full":5474},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}