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Updated: Aug 10, 2026

Dissection and Flat-mounting of the Threespine Stickleback Branchial Skeleton
Published on: May 7, 2016
Evolution of functional diversity in the cupin superfamily
J M Dunwell1, A Culham, C E Carter
1School of Plant Sciences, The University of Reading, Whiteknights, RG6 6AS, Reading, UK. J.Dunwell@reading.ac.uk
Abstract:
The cupin superfamily of proteins is among the most functionally diverse of any described to date. It was named on the basis of the conserved beta-barrel fold ('cupa' is the Latin term for a small barrel), and comprises both enzymatic and non-enzymatic members, which have either one or two cupin domains. Within the conserved tertiary structure, the variety of biochemical function is provided by minor variation of the residues in the active site and the identity of the bound metal ion. This review discusses the advantages of this particular scaffold and provides an evolutionary analysis of 18 different subclasses within the cupin superfamily.
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