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PROSITE documentation PDOC51397 |
The WLM (WSS1-like metalloprotease) domain is a globular domain related to the zincin-like superfamily of Zn-dependent peptidase. Since the WLM domain contains all known active site residues of zincins, it is predicted to be a catalytically active peptidase domain. The WLM domain is an eukaryotic domain represented in plants, fungi, Plasmodium, and kinetoplastids. By contrast, it is absent in animals, Cryptosporidium, and Microsporidia, suggesting that it has been lost on multiple occasions during the evolution of eukaryotes. The WLM domain is found either in stand-alone form or in association with other domains such as the RanBP2 zinc finger (see <PDOC50199>), the ubiquitin domain (see <PDOC00271>) or the PUB/PUG domain. The WLM domain could function as a specific de-SUMOylating domain of distinct protein complexes in the nucleus and the cytoplasm [1].
The WLM domain has been suggested to have a segregated α/β structure with eight helices and five strands [1].
Some proteins known to contain a WLM domain are listed below:
The profile we developed covers the entire WLM domain.
Last update:July 2008 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Iyer L.M. Koonin E.V. Aravind L. |
Title | Novel predicted peptidases with a potential role in the ubiquitin signaling pathway. | |
Source | Cell Cycle 3:1440-1450(2004). | |
PubMed ID | 15483401 |