The domain within your query sequence starts at position 1 and ends at position 60; the E-value for the MADS domain shown below is 3.15e-34.
MGRKKIQISRILDQRNRQVTFTKRKFGLMKKAYELSVLCDCDIALIIFNSAQRLFQYASS
MADS |
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SMART accession number: | SM00432 |
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Description: | - |
Interpro abstract (IPR002100): | Human serum response factor (SRF) is a ubiquitous nuclear protein important for cell proliferation and differentiation. SRF function is essential for transcriptional regulation of numerous growth-factor-inducible genes, such as c-fos oncogene and muscle-specific actin genes. A core domain of around 90 amino acids is sufficient for the activities of DNA-binding, dimerisation and interaction with accessory factors. Within the core is a DNA-binding region, designated the MADS box [ (PUBMED:7637780) ], that is highly similar to many eukaryotic regulatory proteins: among these are MCM1, the regulator of cell type-specific genes in fission yeast; DSRF, a Drosophila trachea development factor; the MEF2 family of myocyte-specific enhancer factors; and the Agamous and Deficiens families of plant homeotic proteins. In SRF, the MADS box has been shown to be involved in DNA-binding and dimerisation [ (PUBMED:3203386) ]. Proteins belonging to the MADS family function as dimers, the primary DNA-binding element of which is an anti-parallel coiled coil of two amphipathic alpha-helices, one from each subunit. The DNA wraps around the coiled coil allowing the basic N-termini of the helices to fit into the DNA major groove. The chain extending from the helix N-termini reaches over the DNA backbone and penetrates into the minor groove. A 4-stranded, anti-parallel beta-sheet packs against the coiled-coil face opposite the DNA and is the central element of the dimerisation interface. The MADS-box domain is commonly found associated with K-box region see ( IPR002487 ). |
GO function: | DNA binding (GO:0003677), protein dimerization activity (GO:0046983) |
Family alignment: |
There are 21394 MADS domains in 21348 proteins in SMART's nrdb database.
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