PROSITE documentation PDOC51534SEFIR 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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Novatchkova M. Leibbrandt A. Werzowa J. Neubueser A. Eisenhaber F. |
| Title | The STIR-domain superfamily in signal transduction, development and immunity. | |
| Source | Trends Biochem. Sci. 28:226-229(2003). | |
| PubMed ID | 12765832 |
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