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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC51673
SUZ domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51673

Description

The SUZ domain is found in a wide range of eukaryotes including animals, fungi, Dictyostelium, plants, and the apicomplexan Plasmodium falciparum. The SUZ domain shows a strong association with known RNA-binding domains: it is fused with R3H (see <PDOC51061>) and RRM domains and RGG repeats in previously characterized multidomain RNA-binding proteins:

  • Caenorhabditis elegans SZY-20, a putative RNA-binding protein that plays a critical role in limiting centrosome size.
  • Drosophila Encore protein, required for the regulation of germline mitosis, karyosome formation, and establishment of dorsoventral (DS) polarity of the egg and embryo.
  • Maize Dip1 protein.
  • Mammalian R3H domain-containing protein 1 (R3HDM1).

Based on the "syntax" of the domain architecture, the SUZ domain has been predicted to function in connection to RNA-protein complexes. The SUZ domain enrichment in positively charged residues, including four universally conserved positively charged positions, supports a role in direct RNA-binding [1].

The profile we developed covers the entire SUZ domain.

Last update:

April 2013 / First entry.

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Technical section

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

SUZ, PS51673; SUZ domain profile  (MATRIX)


Reference

1AuthorsSong M.H. Aravind L. Mueller-Reichert T. O'Connell K.F.
TitleThe conserved protein SZY-20 opposes the Plk4-related kinase ZYG-1 to limit centrosome size.
SourceDev. Cell 15:901-912(2008).
PubMed ID19081077
DOI10.1016/j.devcel.2008.09.018



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