| Literature DB >> 7549889 |
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.Entities:
Mesh:
Substances:
Year: 1995 PMID: 7549889 PMCID: PMC2143151 DOI: 10.1002/pro.5560040623
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725