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Conserved domains on  [gi|71980877|ref|NP_001021129|]
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Dachshund homolog dac-1 [Caenorhabditis elegans]

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 ...
 84-176 6.20e-64

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: 200.28  E-value: 6.20e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980877  84 AKLIKFRGHNVAAFDINGKEMICLPQVYEVFLKNMVGGLHTVYTKLKRLYIHPMVCNVEQVRALRSLGAIQPGVNRCKLL 163
Cdd:cd21081   3 CKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLI 82

                        90
                ....*....|...
gi 71980877 164 KTSDFEKLYDDCT 176
Cdd:cd21081  83 SRKDFDTLYNDCT 95
 
Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 84-176 6.20e-64

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: 200.28  E-value: 6.20e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980877  84 AKLIKFRGHNVAAFDINGKEMICLPQVYEVFLKNMVGGLHTVYTKLKRLYIHPMVCNVEQVRALRSLGAIQPGVNRCKLL 163
Cdd:cd21081   3 CKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLI 82

                        90
                ....*....|...
gi 71980877 164 KTSDFEKLYDDCT 176
Cdd:cd21081  83 SRKDFDTLYNDCT 95
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 85-177 2.71e-33

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: 120.46  E-value: 2.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980877    85 KLIKFRGHNVAAFDINGKEMICLPQVYEVFLKNMvgGLHTVYTKLKRLYIHPMVCNVEQVRALRSLGAIQPGVNRCKLLK 164
Cdd:pfam02437  10 METMLEGEVISCFMVGGEERLCLPQILNTLLKDF--SLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSVRRCGLIT 87

                          90
                  ....*....|...
gi 71980877   165 TSDFEKLYDDCTS 177
Cdd:pfam02437  88 KTDAERLCDALLH 100
 
Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 84-176 6.20e-64

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: 200.28  E-value: 6.20e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980877  84 AKLIKFRGHNVAAFDINGKEMICLPQVYEVFLKNMVGGLHTVYTKLKRLYIHPMVCNVEQVRALRSLGAIQPGVNRCKLL 163
Cdd:cd21081   3 CKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLI 82

                        90
                ....*....|...
gi 71980877 164 KTSDFEKLYDDCT 176
Cdd:cd21081  83 SRKDFDTLYNDCT 95
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 85-177 2.71e-33

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: 120.46  E-value: 2.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980877    85 KLIKFRGHNVAAFDINGKEMICLPQVYEVFLKNMvgGLHTVYTKLKRLYIHPMVCNVEQVRALRSLGAIQPGVNRCKLLK 164
Cdd:pfam02437  10 METMLEGEVISCFMVGGEERLCLPQILNTLLKDF--SLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSVRRCGLIT 87

                          90
                  ....*....|...
gi 71980877   165 TSDFEKLYDDCTS 177
Cdd:pfam02437  88 KTDAERLCDALLH 100
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 88-172 3.35e-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: 84.65  E-value: 3.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980877  88 KFRGHNVAAFDINGKEMICLPQVYEVFLKNMVG-GLHTVYTKLKrlyIHPMVCNVEQVRALRSLGAIQPGVNRCKLLKTS 166
Cdd:cd21074   5 TLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQtQIHNRCTKLK---IICTRCDQEQLKILKRLGILPPKAKSCGLISKS 81


                ....*.
gi 71980877 167 DFEKLY 172
Cdd:cd21074  82 DAERLL 87
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 87-175 5.11e-11

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: 58.89  E-value: 5.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980877  87 IKFRGHNVAAFDINGKEMICLPQVYEVFLKNMVGGlhTVYTKLKRLYIHPMVCNVEQVRALRSLGAIQPGVNRCKLLKTS 166
Cdd:cd21082   4 EEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRT--TVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISRE 81


                ....*....
gi 71980877 167 DFEKLYDDC 175
Cdd:cd21082  82 DVERLYSSY 90
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 91-171 4.88e-08

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: 50.73  E-value: 4.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980877  91 GHNVAAFDINGKEMICLPQVYEVFLKNMvgGLHTVYTKLKRLYIHPMVCNVEQVRALRSLGAIQPGVNRCKLLKTSDFEK 170
Cdd:cd21084  15 GESISCFMVGGEKRLCLPQVLNSVLRDF--SLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQR 92


                .
gi 71980877 171 L 171
Cdd:cd21084  93 L 93
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 91-172 5.62e-08

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: 50.26  E-value: 5.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980877  91 GHNVAAFDINGKEMICLPQVYEVFLKNMvgGLHTVYTKLKRLYIHPMVCNVEQVRALRSLGAIQPGVNRCKLLKTSDFEK 170
Cdd:cd21079   8 GETIACFVVGGEKRLCLPQILNTVLRDF--SLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITKTDAER 85


                ..
gi 71980877 171 LY 172
Cdd:cd21079  86 LC 87
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 89-171 5.77e-04

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: 39.28  E-value: 5.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980877  89 FRGHNVAAFDINGKEMICLPQVYEVFLKNMvgGLHTVYTKLKRLYIHPMVCNVEQVRALRSLGAIQPGVNRCKLLKTSDF 168
Cdd:cd21083  15 LEGETISCFVVGGEKRLCLPQILNSVLRDF--SLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDA 92


                ...
gi 71980877 169 EKL 171
Cdd:cd21083  93 ERL 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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