PROSITE documentation PDOC51534
SEFIR domain profile


The SEFIR domain (after SEFs and IL17Rs) is a conserved sequence segment identified in transmembrane receptors (including SEFs, IL17Rs) and soluble factors (including CIKS/ACT1) in eukaryotes and bacteria. In addition to the SEFIR sequence homology, SEFs and IL17Rs share the same architecture. Their extracellular regions are sequentially divergent but appear structurally similar to a tandem fibronectin 3 (FN3)-like domain arrangement. A single transmembrane region is followed by a high-complexity sequence region involving the SEFIR domain and a C-terminal tail that is enriched with polar residues and, sometimes, with low complexity regions [1].

The SEFIR domain is related to the TIR domain (see <PDOC50104>). The SEFIR domain is similar to the TIR domain in length and secondary structure. The similarity between the SEFIR and TIR domains involves the conserved boxes 1 and 2 of the TIR domain that are implicated in homotypic dimerization, but there is no sequence similarity between SEFIR domains and the TIR sequence box 3 [1].

The profile we developed covers the entire SEFIR domain.

Last update:

April 2011 / First entry.


Technical section

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

SEFIR, PS51534; SEFIR domain profile  (MATRIX)


1AuthorsNovatchkova M. Leibbrandt A. Werzowa J. Neubueser A. Eisenhaber F.
TitleThe STIR-domain superfamily in signal transduction, development and immunity.
SourceTrends Biochem. Sci. 28:226-229(2003).
PubMed ID12765832

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