{"metadata":{"accession":"PF12102","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR021961","hierarchy":null,"name":{"name":"MrcB-like, N-terminal domain","short":"MrcB_N"},"description":[{"text":"<p>This model describes the N-terminal domain of a group of mostly uncharacterised proteins, including 5-methylcytosine-specific restriction enzyme B (also known as MrcB) from E. coli. MrcB recognises N4- and C5-methylcytosine (and 5-hydroxy-methylcytosines)  produced by a broad range of DNA methylases and appears to act  against 5-methylcytosine preceded by a purine residue [[cite:PUB00070724]]. The  N-terminal domain of MrcB has been shown to be a DNA-binding domain,  and the crystal structure has been solved [[cite:PUB00100346]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00100346":{"PMID":22570415,"ISBN":null,"volume":"40","issue":"15","year":2012,"title":"The recognition domain of the methyl-specific endonuclease McrBC flips out 5-methylcytosine.","URL":null,"raw_pages":"7552-62","medline_journal":"Nucleic Acids Res","ISO_journal":"Nucleic Acids Res","authors":["Sukackaite R","Grazulis S","Tamulaitis G","Siksnys V."],"DOI_URL":null},"PUB00070724":{"PMID":7781618,"ISBN":null,"volume":"14","issue":"11","year":1995,"title":"McrB: a prokaryotic protein specifically recognizing DNA containing modified cytosine residues.","URL":null,"raw_pages":"2661-9","medline_journal":"EMBO J","ISO_journal":"EMBO J.","authors":["Kruger T","Wild C","Noyer-Weidner M."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":38,"interactions":0,"matches":790,"pathways":0,"proteins":787,"proteomes":748,"sets":0,"structural_models":{"alphafold":479},"structures":13,"taxa":1530},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":18,"alignment:full":341},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}