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A putative FAD-binding domain in a distinct group of oxidases including a protein involved in plant development

✍ Scribed by Arcady R. Mushegian; Eugene V. Koonin

Publisher
Cold Spring Harbor Laboratory Press
Year
1995
Tongue
English
Weight
248 KB
Volume
4
Category
Article
ISSN
0961-8368

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✦ Synopsis

Abstract

Using methods for database screening with individual protein sequences and alignment blocks, a conserved domain is delineated in a group of proteins including several FAD‐dependent oxidases. Two motifs within this domain resemble phosphate‐binding loops and may be directly involved in FAD binding. These motifs can be readily distinguished from previously described nucleotide‐binding sites using a method for database screening with position‐dependent weight matrices derived from alignment blocks. Unexpectedly, this group of known and predicted FAD‐dependent oxidases includes the product of the DIMINUTO gene, which is involved in Arabidopsis development, and its homologues from man and Mycobacterium leprae.

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