NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|10946942|ref|NP_067494|]
View 

endothelial differentiation-related factor 1 [Mus musculus]

Protein Classification

MBF1 and HTH_XRE domain-containing protein( domain architecture ID 12094462)

MBF1 and HTH_XRE domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 5-71 3.86e-26

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: 93.46  E-value: 3.86e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10946942     5 DWDTVTVLRKKGPTAAQAKSKQAILAAQRRGEDVETSKKWAAGQNKQ-HSITKNTAKLDRETEELHHD 71
Cdd:pfam08523   1 DWDSVTVIGKKAPRATVARSESALNAARRSGAVVETEKKFYAGTNKAhHGEGQNTAKLDRETEELKHE 68
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 76-132 7.77e-14

Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 441418 [Multi-domain]  Cd Length: 70  Bit Score: 62.26  E-value: 7.77e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 10946942  76 EVGKVIQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKL 132
Cdd:COG1813  12 DYGERIREAREARGLSQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALGISL 68
 
Name Accession Description Interval E-value
MBF1 pfam08523
Multiprotein bridging factor 1; This domain is found in the multiprotein bridging factor 1 ...
 5-71 3.86e-26

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: 93.46  E-value: 3.86e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10946942     5 DWDTVTVLRKKGPTAAQAKSKQAILAAQRRGEDVETSKKWAAGQNKQ-HSITKNTAKLDRETEELHHD 71
Cdd:pfam08523   1 DWDSVTVIGKKAPRATVARSESALNAARRSGAVVETEKKFYAGTNKAhHGEGQNTAKLDRETEELKHE 68
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 76-132 7.77e-14

Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441418 [Multi-domain]  Cd Length: 70  Bit Score: 62.26  E-value: 7.77e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 10946942  76 EVGKVIQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKL 132
Cdd:COG1813  12 DYGERIREAREARGLSQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALGISL 68
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
81-133 2.66e-10

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 52.52  E-value: 2.66e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 10946942     81 IQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKLR 133
Cdd:smart00530   2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLD 54
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 78-132 1.65e-09

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 50.63  E-value: 1.65e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 10946942  78 GKVIQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKL 132
Cdd:cd00093   1 GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSL 55
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 81-133 2.67e-09

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 50.23  E-value: 2.67e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 10946942    81 IQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKLR 133
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLD 53
 
Name Accession Description Interval E-value
MBF1 pfam08523
Multiprotein bridging factor 1; This domain is found in the multiprotein bridging factor 1 ...
 5-71 3.86e-26

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: 93.46  E-value: 3.86e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10946942     5 DWDTVTVLRKKGPTAAQAKSKQAILAAQRRGEDVETSKKWAAGQNKQ-HSITKNTAKLDRETEELHHD 71
Cdd:pfam08523   1 DWDSVTVIGKKAPRATVARSESALNAARRSGAVVETEKKFYAGTNKAhHGEGQNTAKLDRETEELKHE 68
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 76-132 7.77e-14

Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441418 [Multi-domain]  Cd Length: 70  Bit Score: 62.26  E-value: 7.77e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 10946942  76 EVGKVIQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKL 132
Cdd:COG1813  12 DYGERIREAREARGLSQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALGISL 68
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
81-133 2.66e-10

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 52.52  E-value: 2.66e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 10946942     81 IQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKLR 133
Cdd:smart00530   2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLD 54
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 78-132 1.65e-09

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 50.63  E-value: 1.65e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 10946942  78 GKVIQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKL 132
Cdd:cd00093   1 GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSL 55
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 81-133 2.67e-09

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 50.23  E-value: 2.67e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 10946942    81 IQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKLR 133
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLD 53
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
71-132 2.79e-08

Transcriptional regulator, contains XRE-family HTH domain [Transcription];


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 48.07  E-value: 2.79e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10946942  71 DRVTLEVGKVIQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKL 132
Cdd:COG1396   2 STLKKALGERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSL 63
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
76-132 8.65e-07

DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];


Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 43.68  E-value: 8.65e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 10946942  76 EVGKVIQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKL 132
Cdd:COG1476   4 KLGNRLKELRKERGLTQEELAELLGVSRQTISAIENGKYNPSLELALKIARALGVSL 60
COG1709 COG1709
Predicted transcriptional regulator,contains XRE-type HTH domain [Transcription];
78-128 2.17e-05

Predicted transcriptional regulator,contains XRE-type HTH domain [Transcription];


Pssm-ID: 441315  Cd Length: 234  Bit Score: 42.47  E-value: 2.17e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 10946942  78 GKVIQRGRQSKGLTQKDLATKINEKPQVIADYESG-RAIPNNQVLGKIERAI 128
Cdd:COG1709  24 GETLRKWREDFGISQTELARELGVSPSVISDYESGrRKSPGIAFVKKFVEAL 75
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 65-134 1.00e-04

Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];


Pssm-ID: 442838 [Multi-domain]  Cd Length: 95  Bit Score: 38.85  E-value: 1.00e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946942  65 TEELHHDRVTLEVGKVIQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKLRG 134
Cdd:COG3620   6 SRDVVTVSPDDTLGEALRLMRKELGLSQLPVAELVGVSQSDILRIESGKRDPTVSTLEKIAEALGKELSA 75
RodZ COG1426
Cytoskeletal protein RodZ, contains Xre-like HTH and DUF4115 domains [Cell cycle control, cell ...
 75-113 2.80e-03

Cytoskeletal protein RodZ, contains Xre-like HTH and DUF4115 domains [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441035 [Multi-domain]  Cd Length: 71  Bit Score: 34.39  E-value: 2.80e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 10946942  75 LEVGKVIQRGRQSKGLTQKDLATKINEKPQVIADYESGR 113
Cdd:COG1426   4 ETIGELLRQAREAKGLSLEDVAERTKISVSYLEAIEEGD 42
YiaG COG2944
DNA-binding transcriptional regulator YiaG, XRE-type HTH domain [Transcription];
81-117 9.81e-03

DNA-binding transcriptional regulator YiaG, XRE-type HTH domain [Transcription];


Pssm-ID: 442187 [Multi-domain]  Cd Length: 64  Bit Score: 32.98  E-value: 9.81e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 10946942  81 IQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPN 117
Cdd:COG2944  11 IRALRERLGLSQAEFAALLGVSVSTVRRWEQGRRKPS 47
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH