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Conserved domains on  [gi|18875430|ref|NP_573514|]
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transcription cofactor vestigial-like protein 1 [Mus musculus]

Protein Classification

vestigial family protein( domain architecture ID 10540330)

vestigial family protein similar to transcription cofactor vestigial-like proteins that may act as specific coactivators for mammalian TEFs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Vg_Tdu pfam07545
Vestigial/Tondu family; The mammalian TEF and the Drosophila scalloped genes belong to a ...
 21-51 3.05e-13

Vestigial/Tondu family; The mammalian TEF and the Drosophila scalloped genes belong to a conserved family of transcriptional factors that possesses a TEA/ATTS DNA-binding domain. Transcriptional activation by these proteins likely requires interactions with specific coactivators. In Drosophila, Scalloped (Sd) interacts with Vestigial (Vg) to form a complex, which binds DNA through the Sd TEA/ATTS domain. The Sd-Vg heterodimer is a key regulator of wing development, which directly controls several target genes and is able to induce wing outgrowth when ectopically expressed. This short conserved region is needed for interaction with Sd.


:

Pssm-ID: 462203  Cd Length: 31  Bit Score: 62.83  E-value: 3.05e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 18875430    21 TEWNAGSVIFTYFEGDINSMVDEHFSRALRN 51
Cdd:pfam07545   1 QYISARCVVFTYFQGDIASVVDEHFSRALSH 31
 
Name Accession Description Interval E-value
Vg_Tdu pfam07545
Vestigial/Tondu family; The mammalian TEF and the Drosophila scalloped genes belong to a ...
 21-51 3.05e-13

Vestigial/Tondu family; The mammalian TEF and the Drosophila scalloped genes belong to a conserved family of transcriptional factors that possesses a TEA/ATTS DNA-binding domain. Transcriptional activation by these proteins likely requires interactions with specific coactivators. In Drosophila, Scalloped (Sd) interacts with Vestigial (Vg) to form a complex, which binds DNA through the Sd TEA/ATTS domain. The Sd-Vg heterodimer is a key regulator of wing development, which directly controls several target genes and is able to induce wing outgrowth when ectopically expressed. This short conserved region is needed for interaction with Sd.


Pssm-ID: 462203  Cd Length: 31  Bit Score: 62.83  E-value: 3.05e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 18875430    21 TEWNAGSVIFTYFEGDINSMVDEHFSRALRN 51
Cdd:pfam07545   1 QYISARCVVFTYFQGDIASVVDEHFSRALSH 31
 
Name Accession Description Interval E-value
Vg_Tdu pfam07545
Vestigial/Tondu family; The mammalian TEF and the Drosophila scalloped genes belong to a ...
 21-51 3.05e-13

Vestigial/Tondu family; The mammalian TEF and the Drosophila scalloped genes belong to a conserved family of transcriptional factors that possesses a TEA/ATTS DNA-binding domain. Transcriptional activation by these proteins likely requires interactions with specific coactivators. In Drosophila, Scalloped (Sd) interacts with Vestigial (Vg) to form a complex, which binds DNA through the Sd TEA/ATTS domain. The Sd-Vg heterodimer is a key regulator of wing development, which directly controls several target genes and is able to induce wing outgrowth when ectopically expressed. This short conserved region is needed for interaction with Sd.


Pssm-ID: 462203  Cd Length: 31  Bit Score: 62.83  E-value: 3.05e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 18875430    21 TEWNAGSVIFTYFEGDINSMVDEHFSRALRN 51
Cdd:pfam07545   1 QYISARCVVFTYFQGDIASVVDEHFSRALSH 31
 
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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