title: DOMON: an ancient extracellular domain in dopamine beta-monooxygenase and other proteins.
abstract: A previously uncharacterized 110-125 residue-long domain was identified both in the physiologically important enzyme dopamine beta-monooxygenase and in several other secreted and transmembrane proteins such as SDR2 and CG-6. This domain was predicted to adopt an all-beta fold with seven or eight strands and might function as a module mediating a range of extracellular adhesive interactions.
authors.affiliation: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda MD 20894, USA.
authors.forename: L
authors.initials: L
authors.lastname: Aravind
mesh_terms: D000465:Algorithms; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D004299:Dopamine beta-Hydroxylase / Q000737:chemistry* / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
chemical_list: D010940:Plant Proteins; D004299:Dopamine beta-Hydroxylase