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Conserved domains on  [gi|1907206449|ref|XP_036018016|]
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dachshund homolog 2 isoform X5 [Mus musculus]

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 ...
 73-167 6.12e-68

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: 216.46  E-value: 6.12e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  73 NECRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLVGGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCK 152
Cdd:cd21081     1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                          90
                  ....*....|....*
gi 1907206449 153 LITRKDFETLFTDCT 167
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 ...
 73-167 6.12e-68

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: 216.46  E-value: 6.12e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  73 NECRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLVGGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCK 152
Cdd:cd21081     1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                          90
                  ....*....|....*
gi 1907206449 153 LITRKDFETLFTDCT 167
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. ...
 69-168 1.71e-41

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: 145.88  E-value: 1.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  69 NTNTNECRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLVGgLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGV 148
Cdd:pfam02437   2 NTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFS-LTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 1907206449 149 NRCKLITRKDFETLFTDCTN 168
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
 
Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 73-167 6.12e-68

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: 216.46  E-value: 6.12e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  73 NECRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLVGGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCK 152
Cdd:cd21081     1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                          90
                  ....*....|....*
gi 1907206449 153 LITRKDFETLFTDCT 167
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. ...
 69-168 1.71e-41

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: 145.88  E-value: 1.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  69 NTNTNECRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLVGgLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGV 148
Cdd:pfam02437   2 NTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFS-LTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 1907206449 149 NRCKLITRKDFETLFTDCTN 168
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 75-162 1.12e-27

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: 106.61  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  75 CRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLVggLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCKLI 154
Cdd:cd21074     1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFV--QTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLI 78


                  ....*...
gi 1907206449 155 TRKDFETL 162
Cdd:cd21074    79 SKSDAERL 86
DHD_Skor cd21080
Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...
 75-162 7.98e-11

Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and similar proteins; Skor1, also known as functional Smad-suppressing element on chromosome 15 (Fussel-15), LBX1 corepressor 1, or ladybird homeobox corepressor 1, acts as a transcriptional corepressor of LBX1 and inhibits BMP signaling. Skor2, also known as functional Smad-suppressing element on chromosome 18 (Fussel-18), LBX1 corepressor 1-like protein, or ladybird homeobox corepressor 1-like protein, exhibits transcriptional repressor activity. It acts as a transforming growth factor-beta (TGF-beta) antagonist in the nervous system. 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: 410783  Cd Length: 91  Bit Score: 59.00  E-value: 7.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  75 CRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLvgGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCKLI 154
Cdd:cd21080     1 VGTVILYGVPIVSLVIDGQERLCLAQISNTLLKDY--SYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMI 78


                  ....*...
gi 1907206449 155 TRKDFETL 162
Cdd:cd21080    79 TKREAERL 86
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 75-166 1.15e-10

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: 58.51  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  75 CRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLVGGlhTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCKLI 154
Cdd:cd21082     1 CGREEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRT--TVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLI 78

                          90
                  ....*....|..
gi 1907206449 155 TRKDFETLFTDC 166
Cdd:cd21082    79 SREDVERLYSSY 90
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 71-173 1.21e-07

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: 49.96  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  71 NTNECRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLvgGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNR 150
Cdd:cd21084     4 SSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDF--SLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPS 81

                          90       100
                  ....*....|....*....|...
gi 1907206449 151 CKLITRKDFETLftdcTNASSRP 173
Cdd:cd21084    82 CGLITLTDAQRL----CNALLRP 100
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 81-162 3.58e-06

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: 45.63  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  81 HGVKVASFLMDGQELICLPQVFDLFLKHLvgGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCKLITRKDFE 160
Cdd:cd21079     7 EGETIACFVVGGEKRLCLPQILNTVLRDF--SLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITKTDAE 84


                  ..
gi 1907206449 161 TL 162
Cdd:cd21079    85 RL 86
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 69-162 1.27e-05

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: 44.29  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907206449  69 NTNTNECRMVdMHGVKVASFLMDGQELICLPQVFDLFLKHLvgGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGV 148
Cdd:cd21083     5 DRSTERCETI-LEGETISCFVVGGEKRLCLPQILNSVLRDF--SLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSA 81

                          90
                  ....*....|....
gi 1907206449 149 NRCKLITRKDFETL 162
Cdd:cd21083    82 PSCGLITKTDAERL 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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