Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51549DM13 domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51549
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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