PROSITE documentation PDOC50966
Zinc 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.


Technical section

PROSITE method (with tools and information) covered by this documentation:

ZF_SWIM, PS50966; Zinc finger SWIM-type profile  (MATRIX)


1AuthorsMakarova K.S. Aravind L. Koonin E.V.
TitleSWIM, a novel Zn-chelating domain present in bacteria, archaea and eukaryotes.
SourceTrends Biochem. Sci. 27:384-386(2002).
PubMed ID12151216

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