InterPro domain: IPR014912

SelM and Sep15 consists of one catalytic a-domain that assumes a thioredoxin-like fold composed of a mixed four-stranded beta-sheet and three interspersed alpha-helices. The active-site redox motifs of SelM and Sep15 are located between the C terminus of strand beta1 and the N terminus of helix alpha1. SelM and Sep15 may function as thiol-disulphide isomerases involved in disulphide bond formation in the endoplasmic reticulum [ 1 ].

1. NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. J. Biol. Chem. 281, 3536-43