InterPro domain: IPR013536

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 a 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 , the ubiquitin domain, or the PUB/PUG domain. This domain could function as a specific de-SUMOylating domain of distinct protein complexes in the nucleus and the cytoplasm [ 1 ].

It has been suggested to form a segregated alpha/beta structure with eight helices and five strands. Proteins containing this domain include yeast WSS1 (also known as weak suppressor of SMT3) which is involved in the repair of toxic DNA-protein cross-links (DPCs) such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesions or DPCs induced by reactive compounds [ 2 ], WSS1 homologues and various putative metalloproteases from plant and fungal species. This domain is also found in an uncharacterised protein from Acanthamoeba polyphaga mimivirus.

1. Novel predicted peptidases with a potential role in the ubiquitin signaling pathway. Cell Cycle 3, 1440-50
2. A DNA-dependent protease involved in DNA-protein crosslink repair. Cell 158, 327-338