We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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.
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 PDOC50828Smr domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC50828
Description
The Smr domain is an around 90-residue domain found in:
- The C-terminal region of the mutS2 proteins from bacteria and plants,
- The small mutS related (smr) proteins from bacteria and eukaryotes.
These proteins could be involved in mismatch repair (MMR) or/and chromosome crossing-over and segregation. It has been proposed that the Smr domain acts as a nicking endonuclease [1,2].
The profile we developed spans the entire Smr domain.
Last update:March 2004 / First entry.
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Technical section
PROSITE method (with tools and information) covered by this documentation:
References
| 1 | Authors | Moreira D. Philippe H. |
| Title | Smr: a bacterial and eukaryotic homologue of the C-terminal region of the MutS2 family. | |
| Source | Trends Biochem. Sci. 24:298-300(1999). | |
| PubMed ID | 10431172 |
| 2 | Authors | Malik H.S. Henikoff S. |
| Title | Dual recognition-incision enzymes might be involved in mismatch repair and meiosis. | |
| Source | Trends Biochem. Sci. 25:414-418(2000). | |
| PubMed ID | 10973051 |
Copyright
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.