PROSITE documentation PDOC52032

MarR-like, BRCT and chromo domains module profile

Mammalian SWI/SNF (mSWI/SNF) of BAF complexes are a subfamily of SWI/SNF ATP-dependent chromatin remodelers that dynamically modulate chromatin structure to regulate fundamental cellular processes including gene transcription, cell cycle control, and DNA damage response [1]. The BAF155/SMARCC1 subunit is a component of all complexes identified to date, incorporated either as a homodimer or as a heterodimer with its paralog BAF170/SMARCC2. The BAF155 subunit predominates in stem cells, while the BAF170 subunit is incorporated during differentiation. The N-terminus of the BAF155/SMARCC1 and BAF170/ SMARCC2 subunits contain a putative DNA-binding MarR-like domain, a chromo domain (see <PDOC00517>) and a BRCT domain that are interconnected to each other to form a distinct module. This N-terminal module could participate in an interaction involving both protein and nucleic acid components [2].

The MarR-like domain forms a four-helix-bundle that resembles the MarR-like helix-turn-helix domain (see <PDOC00861>). The BRCT domain contains an inserted chromo domain between the second and third strands of the canonical fold. The chromo domain consists of the curved antiparallel three-stranded β-sheet characteristic of this domain. The individual domains are linked via a network of hydrogen bonds to form a single structural unit (see <PDB:6YXO>. The architecture of the fold produces a cleft containing two deep pockets at the interface between the domains [2].

The profile we developed covers the entire MarR-like, BRCT and chromo domains module.