{"metadata":{"accession":"PF12122","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR022732","hierarchy":null,"name":{"name":"Cytoplasmic N-terminal domain of rhomboid serine protease","short":"Rhomboid_N"},"description":[{"text":"<p>Rhomboid_N is the N-terminal cytoplasmic domain of the rhomboid intra-membraneous serine protease, otherwise known as Peptidase_S54, [pfam:PF01694]. This N-terminal domain has similarity to other GlnB-like domains, some of which appear to have a binding role, eg to peptidoglycan.  It is not clear exactly what the function of this domain is in the protease, but its presence is critical for maintaining a catalytically competent state for the protein [[cite:PUB00088222]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00088222":{"PMID":22963263,"ISBN":null,"volume":"51","issue":"39","year":2012,"title":"Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core.","URL":null,"raw_pages":"7794-803","medline_journal":"Biochemistry","ISO_journal":"Biochemistry","authors":["Sherratt AR","Blais DR","Ghasriani H","Pezacki JP","Goto NK."],"DOI_URL":"https://doi.org/10.1021/bi301087c"}},"set_info":{"accession":"CL0089","name":"GlnB-like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":2,"interactions":0,"matches":1303,"pathways":0,"proteins":1303,"proteomes":1267,"sets":1,"structural_models":{"alphafold":811},"structures":3,"taxa":1789},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":12,"alignment:full":414},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4hdd","name":"Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease"}}}