The DOMON domains are involved in heme and sugar recognition.
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/.
Iyer
Lakshminarayan M
LM
National Center for Biotechnology Information, National Library of Medicine and National Institute of Health, Bethesda, MD 20894, USA.
Anantharaman
Vivek
V
Aravind
L
L
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
D002241:Carbohydrates; D006418:Heme; D004299:Dopamine beta-Hydroxylase