PROSITE documentation PDOC50966Zinc finger SWIM-type profile
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 [1].
Some of the proteins containing a SWIM-type zinc finger are listed below:
- Vertebrate MEKK-1. It is part of the mitogen-activated protein kinase cascade. It interacts with the cytoskeletal protein α-actinin, 14-3-3 proteins and c-Jun.
- Plant MuDR transposases. The mutator transposon MuDR is one of the largest families of mobile elements in plants.
- Plant nuclear protein FAR1.
- Bacterial SWI2/SNF2 ATPases.
- Escherichia coli hypothetical protein yehQ.
The profile we developed covers the whole SWIM domain.
Last update:March 2004 / First entry.
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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). | |
| PubMed ID | 12151216 |
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