{"metadata":{"accession":"PF01863","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR002725","hierarchy":null,"name":{"name":"YgjP-like, metallopeptidase domain","short":"YgjP-like"},"description":[{"text":"<p>This is a conserved domain containing the catalytic zinc-metallopeptidase (HExxH) catalytic motif. Proteins containing this domain are found in some archaebacteria, as well as Helicobacter pylori. The proteins are 190-240 amino acids long, with the C terminus being the most conserved region, containing three conserved histidines [[cite:PUB00098014],[cite:PUB00098016],[cite:PUB00098015],[cite:PUB00084997]]. This domain is found in YgjP from E. coli [[cite:PUB00084997]], a predicted metal-dependent hydrolase that hydrolyses UTP to UMP and diphosphate in vitro; and in MJ0123 from Methanocaldococcus jannaschii (also referred to as projannalysin) [[cite:PUB00098015]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00098015":{"PMID":23733187,"ISBN":null,"volume":"288","issue":"29","year":2013,"title":"A novel family of soluble minimal scaffolds provides structural insight into the catalytic domains of integral membrane metallopeptidases.","URL":null,"raw_pages":"21279-21294","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Lopez-Pelegrin M","Cerda-Costa N","Martinez-Jimenez F","Cintas-Pedrola A","Canals A","Peinado JR","Marti-Renom MA","Lopez-Otin C","Arolas JL","Gomis-Ruth FX."],"DOI_URL":null},"PUB00098014":{"PMID":25802851,"ISBN":null,"volume":"2015","issue":null,"year":2015,"title":"MALDI-TOF MS and CD spectral analysis for identification and structure prediction of a purified, novel, organic solvent stable, fibrinolytic metalloprotease from Bacillus cereus B80.","URL":null,"raw_pages":"527015","medline_journal":"Biomed Res Int","ISO_journal":"Biomed Res Int","authors":["Saxena R","Singh R."],"DOI_URL":null},"PUB00084997":{"PMID":27941785,"ISBN":null,"volume":"14","issue":"2","year":2017,"title":"Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli.","URL":null,"raw_pages":"187-194","medline_journal":"Nat Methods","ISO_journal":"Nat. Methods","authors":["Sevin DC","Fuhrer T","Zamboni N","Sauer U."],"DOI_URL":"https://doi.org/10.1038/nmeth.4103"},"PUB00098016":{"PMID":26257768,"ISBN":null,"volume":"6","issue":null,"year":2015,"title":"Remote homology and the functions of metagenomic dark matter.","URL":null,"raw_pages":"234","medline_journal":"Front Genet","ISO_journal":"Front Genet","authors":["Lobb B","Kurtz DA","Moreno-Hagelsieb G","Doxey AC."],"DOI_URL":null}},"set_info":{"accession":"CL0126","name":"Peptidase_MA"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":18,"interactions":0,"matches":15593,"pathways":0,"proteins":15247,"proteomes":12259,"sets":1,"structural_models":{"alphafold":9610},"structures":2,"taxa":17503},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":55,"alignment:full":8108},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4jiu","name":"Crystal structure of the metallopeptidase zymogen of Pyrococcus abyssi abylysin"}}}