{PDOC50966} {PS50966; ZF_SWIM} {BEGIN} ********************************* * 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 beta-beta-alpha structure suggesting that it might adopt a fold similar to that of the classic C2H2 zinc-finger (see ). 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 alpha-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. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: March 2004 / First entry. [ 1] Makarova K.S., Aravind L., Koonin E.V. "SWIM, a novel Zn-chelating domain present in bacteria, archaea and eukaryotes." Trends Biochem. Sci. 27:384-386(2002). PubMed=12151216 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}