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Conserved domains on  [gi|334185590|ref|NP_001189962|]
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multiprotein bridging factor 1C [Arabidopsis thaliana]

Protein Classification

MBF1 domain-containing protein( domain architecture ID 10553810)

MBF1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MBF1 pfam08523
Multiprotein bridging factor 1; This domain is found in the multiprotein bridging factor 1 ...
 12-81 1.49e-20

Multiprotein bridging factor 1; 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. 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. The domain is found in a wide range of eukaryotic proteins including metazoans, fungi and plants. A helix-turn-helix motif (pfam01381) is found to its C-terminus.


:

Pssm-ID: 462508  Cd Length: 68  Bit Score: 77.67  E-value: 1.49e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185590  12 DWEPVV-LHKSKQKSQDLRDPKAVNAALRNGVAVQTVKKFDAGSNKKGKSTAVpviNTKKLEEETEPAAMD 81
Cdd:pfam08523  1 DWDSVTvIGKKAPRATVARSESALNAARRSGAVVETEKKFYAGTNKAHHGEGQ---NTAKLDRETEELKHE 68
 
Name Accession Description Interval E-value
MBF1 pfam08523
Multiprotein bridging factor 1; This domain is found in the multiprotein bridging factor 1 ...
 12-81 1.49e-20

Multiprotein bridging factor 1; 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. 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. The domain is found in a wide range of eukaryotic proteins including metazoans, fungi and plants. A helix-turn-helix motif (pfam01381) is found to its C-terminus.


Pssm-ID: 462508  Cd Length: 68  Bit Score: 77.67  E-value: 1.49e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185590  12 DWEPVV-LHKSKQKSQDLRDPKAVNAALRNGVAVQTVKKFDAGSNKKGKSTAVpviNTKKLEEETEPAAMD 81
Cdd:pfam08523  1 DWDSVTvIGKKAPRATVARSESALNAARRSGAVVETEKKFYAGTNKAHHGEGQ---NTAKLDRETEELKHE 68
 
Name Accession Description Interval E-value
MBF1 pfam08523
Multiprotein bridging factor 1; This domain is found in the multiprotein bridging factor 1 ...
 12-81 1.49e-20

Multiprotein bridging factor 1; 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. 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. The domain is found in a wide range of eukaryotic proteins including metazoans, fungi and plants. A helix-turn-helix motif (pfam01381) is found to its C-terminus.


Pssm-ID: 462508  Cd Length: 68  Bit Score: 77.67  E-value: 1.49e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185590  12 DWEPVV-LHKSKQKSQDLRDPKAVNAALRNGVAVQTVKKFDAGSNKKGKSTAVpviNTKKLEEETEPAAMD 81
Cdd:pfam08523  1 DWDSVTvIGKKAPRATVARSESALNAARRSGAVVETEKKFYAGTNKAHHGEGQ---NTAKLDRETEELKHE 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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