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Conserved domains on  [gi|24584617|ref|NP_723968|]
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dachshund, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 215-309 2.98e-67

Dachshund-homology domain found in the retinal determination protein Dachshund and similar proteins; Dachshund proteins act as transcription factors involved in the regulation of organogenesis. They may be a regulator of SIX1, SIX6 and probably SIX5. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. It has been postulated that Dachshund proteins may bind to chromatin DNA via their DHD domains.


:

Pssm-ID: 410784  Cd Length: 95  Bit Score: 219.92  E-value: 2.98e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584617  215 NECKLVEYRGQKVAAFIISNETMLCLPQAFELFLKHLVGGLHTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQPGVNRCK 294
Cdd:cd21081    1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                         90
                 ....*....|....*
gi 24584617  295 LLCCKDFDILYRDCT 309
Cdd:cd21081   81 LISRKDFDTLYNDCT 95
 
Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 215-309 2.98e-67

Dachshund-homology domain found in the retinal determination protein Dachshund and similar proteins; Dachshund proteins act as transcription factors involved in the regulation of organogenesis. They may be a regulator of SIX1, SIX6 and probably SIX5. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. It has been postulated that Dachshund proteins may bind to chromatin DNA via their DHD domains.


Pssm-ID: 410784  Cd Length: 95  Bit Score: 219.92  E-value: 2.98e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584617  215 NECKLVEYRGQKVAAFIISNETMLCLPQAFELFLKHLVGGLHTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQPGVNRCK 294
Cdd:cd21081    1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                         90
                 ....*....|....*
gi 24584617  295 LLCCKDFDILYRDCT 309
Cdd:cd21081   81 LISRKDFDTLYNDCT 95
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 209-310 1.30e-38

SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. All members of this family contain a conserved CLPQ motif. The c-ski proto-oncogene has been shown to influence proliferation, morphological transformation and myogenic differentiation. Sno, a Ski proto-oncogene homolog, is expressed in two isoforms and plays a role in the response to proliferation stimuli. Dachshund also contains this domain. It is involved in various aspects of development.


Pssm-ID: 460558  Cd Length: 100  Bit Score: 138.95  E-value: 1.30e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584617    209 TSDPSANECKLVEYRGQKVAAFIISNETMLCLPQAFELFLKHLvgGLHTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQP 288
Cdd:pfam02437    1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDF--SLTQINTVCDELIITCVRCTPEQLEILKLLGILPP 78

                           90       100
                   ....*....|....*....|..
gi 24584617    289 GVNRCKLLCCKDFDILYRDCTT 310
Cdd:pfam02437   79 SVRRCGLITKTDAERLCDALLH 100
 
Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 215-309 2.98e-67

Dachshund-homology domain found in the retinal determination protein Dachshund and similar proteins; Dachshund proteins act as transcription factors involved in the regulation of organogenesis. They may be a regulator of SIX1, SIX6 and probably SIX5. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. It has been postulated that Dachshund proteins may bind to chromatin DNA via their DHD domains.


Pssm-ID: 410784  Cd Length: 95  Bit Score: 219.92  E-value: 2.98e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584617  215 NECKLVEYRGQKVAAFIISNETMLCLPQAFELFLKHLVGGLHTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQPGVNRCK 294
Cdd:cd21081    1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                         90
                 ....*....|....*
gi 24584617  295 LLCCKDFDILYRDCT 309
Cdd:cd21081   81 LISRKDFDTLYNDCT 95
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 209-310 1.30e-38

SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. All members of this family contain a conserved CLPQ motif. The c-ski proto-oncogene has been shown to influence proliferation, morphological transformation and myogenic differentiation. Sno, a Ski proto-oncogene homolog, is expressed in two isoforms and plays a role in the response to proliferation stimuli. Dachshund also contains this domain. It is involved in various aspects of development.


Pssm-ID: 460558  Cd Length: 100  Bit Score: 138.95  E-value: 1.30e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584617    209 TSDPSANECKLVEYRGQKVAAFIISNETMLCLPQAFELFLKHLvgGLHTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQP 288
Cdd:pfam02437    1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDF--SLTQINTVCDELIITCVRCTPEQLEILKLLGILPP 78

                           90       100
                   ....*....|....*....|..
gi 24584617    289 GVNRCKLLCCKDFDILYRDCTT 310
Cdd:pfam02437   79 SVRRCGLITKTDAERLCDALLH 100
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 217-305 5.23e-20

Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. Members of this family include the Ski protein, Ski-like protein (Sno), and Dachshund proteins. Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. Ski-like protein, also known as SKIL or Sno, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. Dachshund proteins are essential components of a regulatory network controlling cell fate determination. They have been implicated in eye, limb, brain, and muscle development.


Pssm-ID: 410781  Cd Length: 88  Bit Score: 85.42  E-value: 5.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584617  217 CKLVEYRGQKVAAFIISNETMLCLPQAFELFLKHLVggLHTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQPGVNRCKLL 296
Cdd:cd21074    1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFV--QTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLI 78


                 ....*....
gi 24584617  297 CCKDFDILY 305
Cdd:cd21074   79 SKSDAERLL 87
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 217-308 2.36e-06

Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar proteins; SKIDA1 is also known as protein DLN-1. Its biological function remains unclear. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410785  Cd Length: 91  Bit Score: 46.57  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584617  217 CKLVEYRGQKVAAFIISNETMLCLPQAFELFLKHLVGGlhTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQPGVNRCKLL 296
Cdd:cd21082    1 CGREEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRT--TVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLI 78

                         90
                 ....*....|..
gi 24584617  297 CCKDFDILYRDC 308
Cdd:cd21082   79 SREDVERLYSSY 90
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 205-300 3.09e-05

Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like protein, also known as SKIL, Ski-related oncogene (Sno), or Ski-related protein, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410787  Cd Length: 100  Bit Score: 43.80  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584617  205 PPISTSDPSanECKLveyRGQKVAAFIISNETMLCLPQAFELFLKHLvgGLHTVYTKLKRLDIVPLVCNVEQVRILRGLG 284
Cdd:cd21084    1 PSDSSTELT--QTVL---EGESISCFMVGGEKRLCLPQVLNSVLRDF--SLQQINTVCDELYIYCSRCTSDQLHILKVLG 73

                         90
                 ....*....|....*.
gi 24584617  285 AIQPGVNRCKLLCCKD 300
Cdd:cd21084   74 ILPFNAPSCGLITLTD 89
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 224-296 5.57e-05

Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. Ski-like protein, also known as SKIL or Sno, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410782  Cd Length: 91  Bit Score: 42.94  E-value: 5.57e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584617  224 GQKVAAFIISNETMLCLPQAFELFLKHLvgGLHTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQPGVNRCKLL 296
Cdd:cd21079    8 GETIACFVVGGEKRLCLPQILNTVLRDF--SLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLI 78
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 210-304 6.59e-03

Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410786  Cd Length: 102  Bit Score: 37.36  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584617  210 SDPSANECKLVeYRGQKVAAFIISNETMLCLPQAFELFLKHLvgGLHTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQPG 289
Cdd:cd21083    4 SDRSTERCETI-LEGETISCFVVGGEKRLCLPQILNSVLRDF--SLQQINSVCDELHIYCSRCTADQLEILKVMGILPFS 80

                         90
                 ....*....|....*
gi 24584617  290 VNRCKLLCCKDFDIL 304
Cdd:cd21083   81 APSCGLITKTDAERL 95
 
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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