SMART: Pfam domain MBF1

The domain within your query sequence starts at position 4 and ends at position 73; the E-value for the MBF1 domain shown below is 4.6e-29.

SDWDTVTVLRKKGPTAAQAKSKQAILAAQRRGEDVETSKKWAAGQNKQHSITKNTAKLDR
ETEELHHDRV

MBF1

PFAM accession number:	PF08523
Interpro abstract (IPR013729):	This domain is found in the multiprotein bridging factor 1 (MBF1) which forms a heterodimer with MBF2. It has been shown to make direct contact with the TATA-box binding protein (TBP) and interacts with Ftz-F1, stabilising the Ftz-F1-DNA complex [ (PUBMED:9207077) ]. It is also found in the endothelial differentiation-related factor (EDF-1). Human EDF-1 is involved in the repression of endothelial differentiation, interacts with CaM and is phosphorylated by PKC [ (PUBMED:11587857) ]. The domain is found in a wide range of eukaryotic proteins including metazoans, fungi and plants. A helix-turn-helix motif ( IPR001387 ) is found to its C terminus.

PFAM accession number:

PF08523

Interpro abstract (IPR013729):

This domain is found in the multiprotein bridging factor 1 (MBF1) which forms a heterodimer with MBF2. It has been shown to make direct contact with the TATA-box binding protein (TBP) and interacts with Ftz-F1, stabilising the Ftz-F1-DNA complex [ (PUBMED:9207077) ]. It is also found in the endothelial differentiation-related factor (EDF-1). Human EDF-1 is involved in the repression of endothelial differentiation, interacts with CaM and is phosphorylated by PKC [ (PUBMED:11587857) ]. The domain is found in a wide range of eukaryotic proteins including metazoans, fungi and plants. A helix-turn-helix motif ( IPR001387 ) is found to its C terminus.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry MBF1