<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>64(1)</volume><submitter>Dunwell JM</submitter><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</pubmed_abstract><journal>Microbiology and molecular biology reviews : MMBR</journal><pagination>153-79</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC98990</full_dataset_link><repository>biostudies-literature</repository><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.</pubmed_title><pmcid>PMC98990</pmcid><pubmed_authors>Khuri S</pubmed_authors><pubmed_authors>Dunwell JM</pubmed_authors><pubmed_authors>Gane PJ</pubmed_authors></additional><is_claimable>false</is_claimable><name>Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamily.</name><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</description><dates><release>2000-01-01T00:00:00Z</release><publication>2000 Mar</publication><modification>2025-05-18T13:41:44.012Z</modification><creation>2025-05-18T13:41:44.012Z</creation></dates><accession>S-EPMC98990</accession><cross_references><pubmed>10704478</pubmed><doi>10.1128/MMBR.64.1.153-179.2000</doi></cross_references></HashMap>