|PROSITE documentation PDOC50966|
The zinc finger-like domain SWIM was first identified in the bacterial ATPases of the SWI2/SNF2 family, the plant MuDR transposases and vertebrate MEK kinase-1. It is represented in all major lineages of prokaryotes and eukaryotes. It has the signature of predicted zinc-binding residues C-x-C-x(6,25)-C-x-H surounded by two blocks of conserved residues, an N-terminal aromatic/hydrophobic motif and a C-terminal region enriched in small and hydrophobic residues. The SWIM domain appears to have a β-β-α structure suggesting that it might adopt a fold similar to that of the classic C2H2 zinc-finger (see <PDOC00028>). The function of the SWIM domain is not yet known .
Some of the proteins containing a SWIM-type zinc finger are listed below:
The profile we developed covers the whole SWIM domain.Last update:
March 2004 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Makarova K.S. Aravind L. Koonin E.V.|
|Title||SWIM, a novel Zn-chelating domain present in bacteria, archaea and eukaryotes.|
|Source||Trends Biochem. Sci. 27:384-386(2002).|