The domain within your query sequence starts at position 26 and ends at position 101; the E-value for the SWIB domain shown below is 2.5e-17.

QVRPKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLL
GCQSFSVKDPSPLYDM

SWIB

SWIB
PFAM accession number:PF02201
Interpro abstract (IPR003121):

The SWI/SNF family of complexes, which are conserved from yeast to humans, are ATP-dependent chromatin-remodelling proteins that facilitate transcription activation [ (PUBMED:11147808) ]. The mammalian complexes are made up of 9-12 proteins called BAFs (BRG1-associated factors). The BAF60 family have at least three members: BAF60a, which is ubiquitous, BAF60b and BAF60c, which are expressed in muscle and pancreatic tissues, respectively. BAF60b is present in alternative forms of the SWI/SNF complex, including complex B (SWIB), which lacks BAF60a. The SWIB domain is a conserved region found within the BAF60b proteins [ (PUBMED:12016060) ], and can be found fused to the C terminus of DNA topoisomerase in Chlamydia.

MDM2 is an oncoprotein that acts as a cellular inhibitor of the p53 tumour suppressor by binding to the transactivation domain of p53 and suppressing its ability to activate transcription [ (PUBMED:8875929) ]. p53 acts in response to DNA damage, inducing cell cycle arrest and apoptosis. Inactivation of p53 is a common occurrence in neoplastic transformations. The core of MDM2 folds into an open bundle of four helices, which is capped by two small 3-stranded beta-sheets. It consists of a duplication of two structural repeats. MDM2 has a deep hydrophobic cleft on which the p53 alpha-helix binds; p53 residues involved in transactivation are buried deep within the cleft of MDM2, thereby concealing the p53 transactivation domain.

The SWIB and MDM2 domains are homologous and share a common fold.

GO function:protein binding (GO:0005515)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SWIB