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Conserved domains on  [gi|24586029|ref|NP_724482|]
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Adh transcription factor 1, isoform B [Drosophila melanogaster]

Protein Classification

Myb/SANT-like transcription factor( domain architecture ID 10651957)

Myb/SANT-like transcription factor with an N-terminal MADF domain, which resembles the 3 alpha-helix bundle of the DNA-binding Myb domains

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MADF smart00595
subfamily of SANT domain;
15-95 4.86e-27

subfamily of SANT domain;


:

Pssm-ID: 214738  Cd Length: 89  Bit Score: 99.74  E-value: 4.86e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586029     15 NLIEAVKLNPVIYDRSHYNYKHFVRKAQTWKQIAETLGVPEQKCTKRWKSLRDKFAREMKLCQ--------ESRWRYFKQ 86
Cdd:smart00595   1 RLIELVRERPCLWDRRHPDYRNKEEKRKAWEEIAEELGLSVEECKKRWKNLRDRYRRELKRLQngksgggkKSKWEYFDR 80

                   ....*....
gi 24586029     87 MQFLVDSIR 95
Cdd:smart00595  81 LSFLRPVIR 89
 
Name Accession Description Interval E-value
MADF smart00595
subfamily of SANT domain;
15-95 4.86e-27

subfamily of SANT domain;


Pssm-ID: 214738  Cd Length: 89  Bit Score: 99.74  E-value: 4.86e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586029     15 NLIEAVKLNPVIYDRSHYNYKHFVRKAQTWKQIAETLGVPEQKCTKRWKSLRDKFAREMKLCQ--------ESRWRYFKQ 86
Cdd:smart00595   1 RLIELVRERPCLWDRRHPDYRNKEEKRKAWEEIAEELGLSVEECKKRWKNLRDRYRRELKRLQngksgggkKSKWEYFDR 80

                   ....*....
gi 24586029     87 MQFLVDSIR 95
Cdd:smart00595  81 LSFLRPVIR 89
MADF_DNA_bdg pfam10545
Alcohol dehydrogenase transcription factor Myb/SANT-like; The myb/SANT-like domain in Adf-1 ...
16-90 1.20e-23

Alcohol dehydrogenase transcription factor Myb/SANT-like; The myb/SANT-like domain in Adf-1 (MADF) is an approximately 80-amino-acid module that directs sequence specific DNA binding to a site consisting of multiple tri-nucleotide repeats. The MADF domain is found in one or more copies in eukaryotic and viral proteins and is often associated with the BESS domain. It is likely that the MADF domain is more closely related to the myb/SANT domain than it is to other HTH domains.


Pssm-ID: 463144  Cd Length: 84  Bit Score: 90.81  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586029    16 LIEAVKLNPVIYDRSHYNYKHFVRKAQTWKQIAETLG--VPEQKCTKRWKSLRDKFAREMKLCQ-------ESRWRYFKQ 86
Cdd:pfam10545   1 LIELVREHPCLWDRSHPDYRNRDARERAWEEIAEELGsdVPVEDCKKRWKNLRDQYRRELRRKRtnsgelyKSRWYYYEE 80

                  ....
gi 24586029    87 MQFL 90
Cdd:pfam10545  81 LSFL 84
 
Name Accession Description Interval E-value
MADF smart00595
subfamily of SANT domain;
15-95 4.86e-27

subfamily of SANT domain;


Pssm-ID: 214738  Cd Length: 89  Bit Score: 99.74  E-value: 4.86e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586029     15 NLIEAVKLNPVIYDRSHYNYKHFVRKAQTWKQIAETLGVPEQKCTKRWKSLRDKFAREMKLCQ--------ESRWRYFKQ 86
Cdd:smart00595   1 RLIELVRERPCLWDRRHPDYRNKEEKRKAWEEIAEELGLSVEECKKRWKNLRDRYRRELKRLQngksgggkKSKWEYFDR 80

                   ....*....
gi 24586029     87 MQFLVDSIR 95
Cdd:smart00595  81 LSFLRPVIR 89
MADF_DNA_bdg pfam10545
Alcohol dehydrogenase transcription factor Myb/SANT-like; The myb/SANT-like domain in Adf-1 ...
16-90 1.20e-23

Alcohol dehydrogenase transcription factor Myb/SANT-like; The myb/SANT-like domain in Adf-1 (MADF) is an approximately 80-amino-acid module that directs sequence specific DNA binding to a site consisting of multiple tri-nucleotide repeats. The MADF domain is found in one or more copies in eukaryotic and viral proteins and is often associated with the BESS domain. It is likely that the MADF domain is more closely related to the myb/SANT domain than it is to other HTH domains.


Pssm-ID: 463144  Cd Length: 84  Bit Score: 90.81  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586029    16 LIEAVKLNPVIYDRSHYNYKHFVRKAQTWKQIAETLG--VPEQKCTKRWKSLRDKFAREMKLCQ-------ESRWRYFKQ 86
Cdd:pfam10545   1 LIELVREHPCLWDRSHPDYRNRDARERAWEEIAEELGsdVPVEDCKKRWKNLRDQYRRELRRKRtnsgelyKSRWYYYEE 80

                  ....
gi 24586029    87 MQFL 90
Cdd:pfam10545  81 LSFL 84
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
39-86 6.23e-03

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 34.93  E-value: 6.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24586029    39 RKAQTWKQIAE---TLGVP--EQKCTKRWKSLRDKFAREMKLCQESR--WRYFKQ 86
Cdd:pfam13837  30 RNKKLWEEIAEkmaELGYNrsPEQCKEKWENLKKKYRKEKEGNNGSGssWPFFEE 84
 
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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