{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["64(1)"],"submitter":["Dunwell JM"],"pubmed_abstract":["This review summarizes the recent discovery of the cupin superfamily (from the Latin term \"cupa,\" a small barrel) of functionally diverse proteins that initially were limited to several higher plant proteins such as seed storage proteins, germin (an oxalate oxidase), germin-like proteins, and auxin-binding protein. Knowledge of the three-dimensional structure of two vicilins, seed proteins with a characteristic beta-barrel core, led to the identification of a small number of conserved residues and thence to the discovery of several microbial proteins which share these key amino acids. In particular, there is a highly conserved pattern of two histidine-containing motifs with a varied intermotif spacing. This cupin signature is found as a central component of many microbial proteins includin"],"journal":["Microbiology and molecular biology reviews : MMBR"],"pagination":["153-79"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC98990"],"repository":["biostudies-literature"],"pubmed_title":["Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamily."],"pmcid":["PMC98990"],"pubmed_authors":["Khuri S","Dunwell JM","Gane PJ"],"additional_accession":[]},"is_claimable":false,"name":"Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamily.","description":"This review summarizes the recent discovery of the cupin superfamily (from the Latin term \"cupa,\" a small barrel) of functionally diverse proteins that initially were limited to several higher plant proteins such as seed storage proteins, germin (an oxalate oxidase), germin-like proteins, and auxin-binding protein. Knowledge of the three-dimensional structure of two vicilins, seed proteins with a characteristic beta-barrel core, led to the identification of a small number of conserved residues and thence to the discovery of several microbial proteins which share these key amino acids. In particular, there is a highly conserved pattern of two histidine-containing motifs with a varied intermotif spacing. This cupin signature is found as a central component of many microbial proteins includin","dates":{"release":"2000-01-01T00:00:00Z","publication":"2000 Mar","modification":"2025-05-18T13:41:44.012Z","creation":"2025-05-18T13:41:44.012Z"},"accession":"S-EPMC98990","cross_references":{"pubmed":["10704478"],"doi":["10.1128/MMBR.64.1.153-179.2000"]}}