PROSITE documentation PDOC51549DM13 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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Iyer L.M. Anantharaman V. Aravind L. |
| Title | The DOMON domains are involved in heme and sugar recognition. | |
| Source | Bioinformatics 23:2660-2664(2007). | |
| PubMed ID | 17878204 | |
| DOI | 10.1093/bioinformatics/btm411 |
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