Drosophila kelch motif is derived from a common enzyme fold.
A systematic screening of sequence databases with a motif hitherto found only in animal and poxvirus proteins has revealed a trail leading back to prokaryotes. Fortuitously, an X-ray structure is available for one of the identified sequences and shows the fundamental fold to be a set of circularly arranged beta sheets. This structure may be very widely distributed throughout the biological world in sialidases and some other enzymes. In bacteria, a mobile noncatalytic domain is often associated with these same enzymes.
Bork
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European Molecular Biological Laboratory, Heidelberg, Germany.
Doolittle
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RF
D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000201:enzymology; D005075:Biological Evolution; D004330:Drosophila / Q000201:enzymology; D005658:Fungi / Q000201:enzymology; D005692:Galactose Oxidase / Q000737:chemistry*; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012091:Repetitive Sequences, Nucleic Acid; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014780:Viruses / Q000201:enzymology
D000429:Alcohol Oxidoreductases; C052371:glyoxal oxidase; D005692:Galactose Oxidase; D009439:Neuraminidase