{"metadata":{"accession":"PF09153","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR015236","hierarchy":null,"name":{"name":"Methylated DNA-protein cysteine methyltransferase, N-terminal","short":"MGMT_N"},"description":[{"text":"<p>This domain is found in the archaeal protein O6-alkylguanine-DNA alkyltransferase (also known as Methylated DNA-protein cysteine methyltransferase MGMT), adopt a secondary structure consisting of a three stranded antiparallel beta-sheet and three alpha helices. This entry represents the N-terminal ribonuclease H-like domain, associated with 6-O-methylguanine DNA methyltransferase activity. The exact function has not, as yet, been defined, though it has been postulated that they confer thermostability to the archaeal protein [[cite:PUB00027330]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00027330":{"PMID":10497033,"ISBN":null,"volume":"292","issue":"3","year":1999,"title":"Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase.","URL":null,"raw_pages":"707-16","medline_journal":"J Mol Biol","ISO_journal":"J. Mol. Biol.","authors":["Hashimoto H","Inoue T","Nishioka M","Fujiwara S","Takagi M","Imanaka T","Kai Y."],"DOI_URL":"http://dx.doi.org/10.1006/jmbi.1999.3100"}},"set_info":{"accession":"CL0219","name":"RNase_H"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":1,"interactions":0,"matches":36,"pathways":0,"proteins":36,"proteomes":35,"sets":1,"structural_models":{"alphafold":35},"structures":1,"taxa":61},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":2,"alignment:full":5},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}