{"metadata":{"accession":"PF18231","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR040867","hierarchy":null,"name":{"name":"L-serine kinase SerK, C-terminal domain","short":"SerK_C"},"description":[{"text":"<p>This domain is found in the C-terminal region of free serine kinase (SerK) in the hyperthermophilic archaeon Thermococcus kodakarensis. SerK converts ADP and l-serine (Ser) into AMP and O-phospho-l-serine (Sep), which is a precursor of l-cysteine. The domain is not conserved in the ParB/Srx family. The differences between SerK and the other members of the ParB/Srx family is concentrated in the C-terminal region, which may include residues involved in the Sep binding [[cite:PUB00091306]]. Members of this group are mainly found in archaea.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00091306":{"PMID":28358477,"ISBN":null,"volume":"12","issue":"6","year":2017,"title":"Structural Study on the Reaction Mechanism of a Free Serine Kinase Involved in Cysteine Biosynthesis.","URL":null,"raw_pages":"1514-1523","medline_journal":"ACS Chem Biol","ISO_journal":"ACS Chem. Biol.","authors":["Nagata R","Fujihashi M","Kawamura H","Sato T","Fujita T","Atomi H","Miki K."],"DOI_URL":"https://doi.org/10.1021/acschembio.7b00064"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":1,"interactions":0,"matches":39,"pathways":0,"proteins":39,"proteomes":38,"sets":0,"structural_models":{"alphafold":38},"structures":7,"taxa":74},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":2,"alignment:full":9},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}