PROSITE documentation PDOC51549
DM13 domain profile


The DM13 domain has been identified in animal proteins containing a DOMON domain (see <PDOC50836>) likely to function as cytochromes involved in as yet unidentified redox reactions potentially related to protein hydroxylation or oxidative cross-linking. However, it is also found in bacteria. The DM13 domain contains a nearly absolutely conserved cysteine, which can be potentially involved in a redox reaction either as a nacked thiol group or by binding a prosthetic group like heme [1].

The DM13 domain is predicted to have a β-strand-rich fold [1].

The profile we developed covers the entire DM13 domain.

Last update:

October 2011 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

DM13, PS51549; DM13 domain profile  (MATRIX)


1AuthorsIyer L.M. Anantharaman V. Aravind L.
TitleThe DOMON domains are involved in heme and sugar recognition.
SourceBioinformatics 23:2660-2664(2007).
PubMed ID17878204

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