{"metadata":{"accession":"PF04008","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR007153","hierarchy":null,"name":{"name":"Adenosine specific kinase","short":"Adenosine_kin"},"description":[{"text":"<p>The structure of a member of this family from the hyperthermophilic archaeon Pyrobaculum aerophilum contains a modified histidine residue which is interpreted as stable phosphorylation [[cite:PUB00041095]]. In vitro binding studies confirmed that adenosine and AMP but not ADP or ATP bind to the protein [[cite:PUB00041095]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00041095":{"PMID":16737961,"ISBN":null,"volume":"281","issue":"31","year":2006,"title":"The structure of an ancient conserved domain establishes a structural basis for stable histidine phosphorylation and identifies a new family of adenosine-specific kinases.","URL":null,"raw_pages":"22131-41","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Lott JS","Paget B","Johnston JM","Delbaere LT","Sigrell-Simon JA","Banfield MJ","Baker EN."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M603062200"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":4,"interactions":0,"matches":767,"pathways":0,"proteins":767,"proteomes":756,"sets":0,"structural_models":{"alphafold":562},"structures":7,"taxa":1640},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":83,"alignment:full":388},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"1vgg","name":"Crystal Structure of the Conserved Hypothetical Protein TTHA1091 from Thermus Thermophilus HB8"}}}