InterPro domain: IPR003877

The SPRY domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein interaction module involved in many important signaling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development [ 1 , 2 , 3 ]. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region [ 4 ]. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. The PRY domain consists of three beta-strands tightly packed against ten other beta-strands which form the SPRY component of the B30.2 domain. The beta-strands are linked by loops and form two anti-parallel beta-sheets [ 4 ]. Distant homologues are domains in butyrophilin/marenostrin/pyrin [ 4 ].

1. Structural basis for protein recognition by B30.2/SPRY domains. Mol. Cell 24, 967-76
2. Structure and function of the SPRY/B30.2 domain proteins involved in innate immunity. Protein Sci. 22, 1-10
3. SPRYSEC Effectors: A Versatile Protein-Binding Platform to Disrupt Plant Innate Immunity. Front Plant Sci 7, 1575
4. SPRY domains in ryanodine receptors (Ca(2+)-release channels). Trends Biochem. Sci. 22, 193-4