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Bioinformatics Advance Access originally published online on September 18, 2007
Bioinformatics 2007 23(20):2660-2664; doi:10.1093/bioinformatics/btm411
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

The DOMON domains are involved in heme and sugar recognition

Lakshminarayan M. Iyer , Vivek Anantharaman and L. Aravind *

National Center for Biotechnology Information, National Library of Medicine and National Institute of Health, Bethesda, MD 20894, USA

*To whom correspondence should be addressed.


  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.

Contact: aravind{at}ncbi.nlm.nih.gov or aravind{at}mail.nih.gov

Supplementary information: Supplementary data are available at Bioinformatics online and also at ftp://ftp.ncbi.nih.gov/pub/aravind/domon/.

Associate Editor: John Quackenbush

Received on June 13, 2007; revised on July 19, 2007; accepted on August 8, 2007

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