{PDOC51534} {PS51534; SEFIR} {BEGIN} ************************ * 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 ). 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. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: April 2011 / First entry. [ 1] Novatchkova M., Leibbrandt A., Werzowa J., Neubueser A., Eisenhaber F. "The STIR-domain superfamily in signal transduction, development and immunity." Trends Biochem. Sci. 28:226-229(2003). PubMed=12765832 -------------------------------------------------------------------------------- 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}