SAM domain of Samd7,11 subfamily of Polycomb group.
SAM (sterile alpha motif) domain is a protein-protein interaction domain. Phylogenetic analysis suggests that proteins of this subfamily are most closely related to SAM-Ph1,2,3 subfamily of Polycomb group. They are predicted transcriptional repressors in photoreceptor cells and pinealocytes of vertebrates. SAM domain containing protein 11 is also known as Mr-s (major retinal SAM) protein. In mouse, it is predominantly expressed in developing retinal photoreceptors and in adult pineal gland. The SAM domain is involved in homooligomerization of whole proteins (it was shown based on immunoprecipitation assay and mutagenesis), however its repression activity is not due to SAM/SAM interactions but to the C-terminal region.
Feature 1:putative oligomer interface ML [polypeptide binding site]
Evidence:
Comment:The mid-loop (ML) surface of the SAM domain of Ph protein interacts with the end-helix (EH) surface of the SAM domain of Scm protein forming heterodimers.
Comment:SAM domains of Scm and Ph proteins can form head-to-tail homooligomers via interactions between the mid-loop (ML) and end-helix (EH) surfaces.