Evolution of functional diversity in the cupin superfamily.
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.
Dunwell
J M
JM
School of Plant Sciences, The University of Reading, Whiteknights, RG6 6AS, Reading, UK. J.Dunwell@reading.ac.uk
Culham
A
A
Carter
C E
CE
Sosa-Aguirre
C R
CR
Goodenough
P W
PW
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D001665:Binding Sites; D019143:Evolution, Molecular; D014644:Genetic Variation; D008969:Molecular Sequence Data; D010802:Phylogeny; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000502:physiology
D001426:Bacterial Proteins; D010940:Plant Proteins; D014157:Transcription Factors