title: The DOMON domains are involved in heme and sugar recognition.
abstract: We expand the functionally uncharacterized DOMON domain superfamily to identify several novel families, including the first prokaryotic representatives. Using several computational tools we show that it is involved in ligand binding--either as heme- or sugar-binding domains. We present evidence that the DOMON domain along with the DM13 domain comprises a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. Other novel versions might function as sugar sensors of histidine kinases of bacterial two component systems.
  
  
  BACKGROUND
  Supplementary data are available at Bioinformatics online and also at ftp://ftp.ncbi.nih.gov/pub/aravind/domon/.
authors: National Center for Biotechnology Information, National Library of Medicine and National Institute of Health, Bethesda, MD 20894, USA.
authors: Lakshminarayan M
authors: LM
authors: Iyer
authors: Vivek
authors: V
authors: Anantharaman
authors: L
authors: L
authors: Aravind
mesh_terms: D000818:Animals; D050260:Carbohydrate Metabolism / Q000502:physiology*; D002241:Carbohydrates / Q000737:chemistry*; D004299:Dopamine beta-Hydroxylase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006418:Heme / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D005810:Multigene Family / Q000502:physiology; D025941:Protein Interaction Mapping / Q000379:methods*; D017434:Protein Structure, Tertiary; D020539:Sequence Analysis, Protein
chemical_list: D002241:Carbohydrates; D006418:Heme; D004299:Dopamine beta-Hydroxylase