|PROSITE documentation PDOC51293|
The myb family can be classified into three groups: the myb-type HTH domain, which binds DNA (see <PDOC00037>), the SANT domain, which is a protein-protein interaction module and the myb-like domain that can be involved in either of these functions.
The SANT domain is a motif of ~50 amino acids present in proteins involved in chromatin-remodelling and transcription regulation. This eukaryotic domain was identified in nuclear receptor co-repressors and named after switching-defective protein 3 (Swi3), adaptor 2 (Ada2), nuclear receptor co-repressor (N-CoR) and transcription factor (TF)IIIB . Although SANT domains show remarkable sequence and structural similarity to the DNA-binding helix-turn-helix (HTH) domain of the myb-like tandem repeat (see <PDOC00037>), their function is not DNA binding. Instead, SANT domains are protein-protein interaction modules and some can bind to histone tails (e.g. in Ada2 and SMRT). SANT domains are found in combination with other domains, such as the SWIRM domain (see <PDOC50934>), the ZZ-type zinc finger (see <PDOC50135>), the C2H2-type zinc finger (see <PDOC00028>), the GATA-type zinc finger (see <PDOC00300>), the MPN-domain (see <QDOC50249>) and DEAH ATP-helicase domain (see <PDOC00039>). The SANT domain was proposed to function as a histone-interaction module that couples histone-tail binding to enzyme catalysis for the remodelling of nucleosomes [2,3].
The 3-dimensional structure of the SANT domain forms three α helices (see <PDB:1OFC>)  similar to the DNA-binding myb-type HTH domain. Because of the strong resemblance, the SANT domain can also be detected as a myb-like "DNA-binding" domain (see <PDOC00037>). Most SANT domains have acidic amino acids at the start of helix 2 and in helix 3, while myb-like DNA-binding domains have more positively charged residues, in particular in their third 'recognition' helix. The bulky aromatic and hydrophobic residues in the center of helix 3 that are incompatible with DNA contacts of myb-like DNA-binding domains form another distinguishing property of SANT domains.
Some proteins known to contain a SANT domain:
The profile we developed covers the entire SANT domain. SANT-specific positions within the profile have been manually adapted.Note:
The SANT domain profile is in competition with profiles of related domains, which include the myb-type HTH DNA-binding domain and myb-like domain (see <PDOC00037>).Last update:
February 2007 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Aasland R. Stewart A.F. Gibson T.|
|Title||The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB.|
|Source||Trends Biochem. Sci. 21:87-88(1996).|
|2||Authors||Gruene T. Brzeski J. Eberharter A. Clapier C.R. Corona D.F.V. Becker P.B. Mueller C.W.|
|Title||Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.|
|Source||Mol. Cell 12:449-460(2003).|
|3||Authors||Boyer L.A. Latek R.R. Peterson C.L.|
|Title||The SANT domain: a unique histone-tail-binding module?|
|Source||Nat. Rev. Mol. Cell Biol. 5:158-163(2004).|
|4||Authors||Yao Y.-L. Yang W.-M.|
|Title||The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity.|
|Source||J. Biol. Chem. 278:42560-42568(2003).|