SAM domain of Scm-like-4MBT proteins of Polycomb group
SAM (sterile alpha motif) domain of Scm-like-4MBT (Sex comb on midleg like, Malignant Brain Tumor) subfamily proteins of the polycomb group is a putative protein-protein interaction domain. Additionally to the SAM domain, most of the proteins of this subfamily have 4 MBT repeats. In Drosophila SAM-Scm-like-4MBT protein (known as dSfmbt) is a member of Pho repressive complex (PhoRC). Additionally to dSfmbt, the PhoRC complex includes Pho or Pho-like proteins. This complex is responsible for HOX (Homeobox) gene silencing: Pho or Pho-like proteins bind DNA and dSmbt binds methylated histones. dSmbt can interact with mono- and di-methylated histones H3 and H4 (however this activity has been shown for the MBT repeats, while exact function of the SAM domain is unclear). Besides interaction with histones, dSmbt can interact with Scm (a member of PRC complex), but this interaction also seems to be SAM domain independent.
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.