在包括一种参与植物发育的蛋白质在内的一组独特氧化酶中存在一个假定的黄素腺嘌呤二核苷酸（FAD）结合结构域。
A putative FAD-binding domain in a distinct group of oxidases including a protein involved in plant development.
作者信息
Mushegian A R, Koonin E V
机构信息
Department of Microbiology, University of Washington, Seattle 98195, USA.
出版信息
Protein Sci. 1995 Jun;4(6):1243-4. doi: 10.1002/pro.5560040623.
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.
摘要
利用针对单个蛋白质序列和比对模块进行数据库筛选的方法，在一组包括几种FAD依赖性氧化酶的蛋白质中划定了一个保守结构域。该结构域内的两个基序类似于磷酸结合环，可能直接参与FAD结合。使用针对源自比对模块的位置依赖性权重矩阵进行数据库筛选的方法，可轻松将这些基序与先前描述的核苷酸结合位点区分开来。出乎意料的是，这组已知和预测的FAD依赖性氧化酶包括拟南芥发育相关的DIMINUTO基因的产物及其来自人和麻风分枝杆菌的同源物。
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