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Conserved domains on  [gi|442629238|ref|NP_001261216|]
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uncharacterized protein Dmel_CG3386, isoform B [Drosophila melanogaster]

Protein Classification

MADF domain-containing protein( domain architecture ID 10565669)

MADF (Myb/SANT-like domain in Adf-1) domain-containing protein 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_DNA_bdg pfam10545
Alcohol dehydrogenase transcription factor Myb/SANT-like; The myb/SANT-like domain in Adf-1 ...
 20-111 3.59e-18

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: 77.33  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629238   20 FLALYQGMPELWDVHHLNYRNKELRNRAYELLERKLREiqpNATRTEVGRRINIFRTNYRREqmrilKQKELGLHSDLCK 99
Cdd:pfam10545   1 LIELVREHPCLWDRSHPDYRNRDARERAWEEIAEELGS---DVPVEDCKKRWKNLRDQYRRE-----LRRKRTNSGELYK 72

                          90
                  ....*....|..
gi 442629238  100 PTLWFYDYMGFL 111
Cdd:pfam10545  73 SRWYYYEELSFL 84
 
Name Accession Description Interval E-value
MADF_DNA_bdg pfam10545
Alcohol dehydrogenase transcription factor Myb/SANT-like; The myb/SANT-like domain in Adf-1 ...
 20-111 3.59e-18

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: 77.33  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629238   20 FLALYQGMPELWDVHHLNYRNKELRNRAYELLERKLREiqpNATRTEVGRRINIFRTNYRREqmrilKQKELGLHSDLCK 99
Cdd:pfam10545   1 LIELVREHPCLWDRSHPDYRNRDARERAWEEIAEELGS---DVPVEDCKKRWKNLRDQYRRE-----LRRKRTNSGELYK 72

                          90
                  ....*....|..
gi 442629238  100 PTLWFYDYMGFL 111
Cdd:pfam10545  73 SRWYYYEELSFL 84
MADF smart00595
subfamily of SANT domain;
19-111 7.82e-11

subfamily of SANT domain;


Pssm-ID: 214738  Cd Length: 89  Bit Score: 57.37  E-value: 7.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629238    19 EFLALYQGMPELWDVHHLNYRNKELRNRAYELLERKLreiqpNATRTEVGRRINIFRTNYRREqmriLKQKELGLHSDLC 98
Cdd:smart00595   1 RLIELVRERPCLWDRRHPDYRNKEEKRKAWEEIAEEL-----GLSVEECKKRWKNLRDRYRRE----LKRLQNGKSGGGK 71

                           90
                   ....*....|...
gi 442629238    99 KPTLWFYDYMGFL 111
Cdd:smart00595  72 KSKWEYFDRLSFL 84
 
Name Accession Description Interval E-value
MADF_DNA_bdg pfam10545
Alcohol dehydrogenase transcription factor Myb/SANT-like; The myb/SANT-like domain in Adf-1 ...
 20-111 3.59e-18

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: 77.33  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629238   20 FLALYQGMPELWDVHHLNYRNKELRNRAYELLERKLREiqpNATRTEVGRRINIFRTNYRREqmrilKQKELGLHSDLCK 99
Cdd:pfam10545   1 LIELVREHPCLWDRSHPDYRNRDARERAWEEIAEELGS---DVPVEDCKKRWKNLRDQYRRE-----LRRKRTNSGELYK 72

                          90
                  ....*....|..
gi 442629238  100 PTLWFYDYMGFL 111
Cdd:pfam10545  73 SRWYYYEELSFL 84
MADF smart00595
subfamily of SANT domain;
19-111 7.82e-11

subfamily of SANT domain;


Pssm-ID: 214738  Cd Length: 89  Bit Score: 57.37  E-value: 7.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629238    19 EFLALYQGMPELWDVHHLNYRNKELRNRAYELLERKLreiqpNATRTEVGRRINIFRTNYRREqmriLKQKELGLHSDLC 98
Cdd:smart00595   1 RLIELVRERPCLWDRRHPDYRNKEEKRKAWEEIAEEL-----GLSVEECKKRWKNLRDRYRRE----LKRLQNGKSGGGK 71

                           90
                   ....*....|...
gi 442629238    99 KPTLWFYDYMGFL 111
Cdd:smart00595  72 KSKWEYFDRLSFL 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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