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Bioinformatics Advance Access first published online on September 18, 2007
This version published online on September 19, 2007
Bioinformatics, doi:10.1093/bioinformatics/btm411
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Published by Oxford University Press 2007.
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

The DOMON domains are involved in heme and sugar recognition

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

NCBI, NLM, NIH, Bethesda, MD 20894, USA.

*To whom correspondence should be addressed. Dr. L. Aravind, E-mail: aravind{at}ncbi.nlm.nih.gov


  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.

Associate Editor: Prof. John Quackenbush

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

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