B30.2/SPRY domain (IPR001870)

Short name: B30.2/SPRY

Overlapping homologous superfamilies

Domain relationships


The B30.2 domain was first identified as a protein domain encoded by an exon (named B30-2) in the Homo sapiens class I major histocompatibility complex region [PMID: 8114113], whereas the SPRY domain was first identified in a Dictyostelium discoideum kinase splA and mammalian calcium-release channels ryanodine receptors [PMID: 9204703]. The SPRY domains (after SPla and the RYanodine Receptor) are shorter at the N terminus than the B30.2 domains and appear as a subdomain of the latter. The ~200-residue B30.2/SPRY (for B30.2 and/or SPRY) domain is present in a large number of proteins with diverse individual functions in different biological processes. The B30.2/SPRY domain in these proteins is likely to function through protein-protein interaction [PMID: 16498413]. The N-terminal ~60 residues of B30.2/SPRY domains are poorly conserved and, as a consequence, a new domain name PRY was coined for a group of similar sequence segments N-terminal to the SPRY domains [PMID: 16498413]. The B30.2/SPRY domain contains three highly conserved motifs (LDP, WEVE and LDYE) [PMID: 9196055]. The B30.2/SPRY domain adopts a highly distorted, compact beta-sandwich fold with two additional short beta helices at the N terminus. The beta sandwich of the B30.2/SPRY domain consists of two layers of beta sheets: sheet A composed of eight strands and sheet B composed of seven strands. All the beta strands are in antiparallel arrangement [PMID: 16498413]. The 5th beta-strand corresponding to WEVE motif [PMID: 10223295]. Both the N- and C-terminal ends of the B30.2/SPRY domains in general are close to each other [PMID: 16498413].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles