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Conserved domains on  [gi|628601831|ref|NP_004383|]
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dachshund homolog 1 isoform c [Homo sapiens]

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 ...
 186-280 7.06e-73

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: 225.70  E-value: 7.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 186 NECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVGGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCK 265
Cdd:cd21081    1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                         90
                 ....*....|....*
gi 628601831 266 LISRKDFETLYNDCT 280
Cdd:cd21081   81 LISRKDFDTLYNDCT 95
ATP-synt_Fo_b super family cl21478
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 361-476 5.50e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


The actual alignment was detected with superfamily member CHL00019:

Pssm-ID: 473877 [Multi-domain]  Cd Length: 184  Bit Score: 37.92  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 361 LSSI-----ETLLTNIQ---GLLKVAIDnaRAQEKQVQLEKTELKMDflrerELREtlEKQLAMEQKNRAIVQKRLKKEK 432
Cdd:CHL00019  49 LSDLldnrkQTILNTIRnseERREEAIE--KLEKARARLRQAELEAD-----EIRV--NGYSEIEREKENLINQAKEDLE 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 628601831 433 KAKRKLQEALEFETKR-REQAEQTLKQAASTDSLRVLNDSLTPEI 476
Cdd:CHL00019 120 RLENYKNETIRFEQQRaINQVRQQVFQLALQRALGTLNSCLNNEL 164
 
Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 186-280 7.06e-73

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: 225.70  E-value: 7.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 186 NECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVGGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCK 265
Cdd:cd21081    1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                         90
                 ....*....|....*
gi 628601831 266 LISRKDFETLYNDCT 280
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. ...
 181-281 2.18e-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: 143.57  E-value: 2.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831  181 NTPQNNECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPG 260
Cdd:pfam02437   2 NTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDF--SLTQINTVCDELIITCVRCTPEQLEILKLLGILPPS 79

                          90       100
                  ....*....|....*....|.
gi 628601831  261 VNRCKLISRKDFETLYNDCTN 281
Cdd:pfam02437  80 VRRCGLITKTDAERLCDALLH 100
atpF CHL00019
ATP synthase CF0 B subunit
 361-476 5.50e-03

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 37.92  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 361 LSSI-----ETLLTNIQ---GLLKVAIDnaRAQEKQVQLEKTELKMDflrerELREtlEKQLAMEQKNRAIVQKRLKKEK 432
Cdd:CHL00019  49 LSDLldnrkQTILNTIRnseERREEAIE--KLEKARARLRQAELEAD-----EIRV--NGYSEIEREKENLINQAKEDLE 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 628601831 433 KAKRKLQEALEFETKR-REQAEQTLKQAASTDSLRVLNDSLTPEI 476
Cdd:CHL00019 120 RLENYKNETIRFEQQRaINQVRQQVFQLALQRALGTLNSCLNNEL 164
 
Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 186-280 7.06e-73

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: 225.70  E-value: 7.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 186 NECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVGGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCK 265
Cdd:cd21081    1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                         90
                 ....*....|....*
gi 628601831 266 LISRKDFETLYNDCT 280
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. ...
 181-281 2.18e-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: 143.57  E-value: 2.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831  181 NTPQNNECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPG 260
Cdd:pfam02437   2 NTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDF--SLTQINTVCDELIITCVRCTPEQLEILKLLGILPPS 79

                          90       100
                  ....*....|....*....|.
gi 628601831  261 VNRCKLISRKDFETLYNDCTN 281
Cdd:pfam02437  80 VRRCGLITKTDAERLCDALLH 100
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 188-277 2.00e-30

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: 113.54  E-value: 2.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 188 CKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVggLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLI 267
Cdd:cd21074    1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFV--QTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLI 78

                         90
                 ....*....|
gi 628601831 268 SRKDFETLYN 277
Cdd:cd21074   79 SKSDAERLLN 88
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 188-279 3.48e-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: 56.58  E-value: 3.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 188 CKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVGGlhTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLI 267
Cdd:cd21082    1 CGREEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRT--TVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLI 78

                         90
                 ....*....|..
gi 628601831 268 SRKDFETLYNDC 279
Cdd:cd21082   79 SREDVERLYSSY 90
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 185-277 6.88e-06

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: 44.57  E-value: 6.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 185 NNECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRC 264
Cdd:cd21084    5 STELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDF--SLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSC 82

                         90
                 ....*....|...
gi 628601831 265 KLISRKDFETLYN 277
Cdd:cd21084   83 GLITLTDAQRLCN 95
DHD_Skor cd21080
Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...
 188-275 7.10e-06

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: 44.36  E-value: 7.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 188 CKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLI 267
Cdd:cd21080    1 VGTVILYGVPIVSLVIDGQERLCLAQISNTLLKDY--SYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMI 78


                 ....*...
gi 628601831 268 SRKDFETL 275
Cdd:cd21080   79 TKREAERL 86
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 188-277 4.13e-04

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: 39.47  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 188 CKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLI 267
Cdd:cd21079    1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDF--SLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLI 78

                         90
                 ....*....|
gi 628601831 268 SRKDFETLYN 277
Cdd:cd21079   79 TKTDAERLCS 88
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 188-277 2.53e-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: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 188 CKMVdLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLI 267
Cdd:cd21083   11 CETI-LEGETISCFVVGGEKRLCLPQILNSVLRDF--SLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLI 87

                         90
                 ....*....|
gi 628601831 268 SRKDFETLYN 277
Cdd:cd21083   88 TKTDAERLCN 97
atpF CHL00019
ATP synthase CF0 B subunit
 361-476 5.50e-03

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 37.92  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601831 361 LSSI-----ETLLTNIQ---GLLKVAIDnaRAQEKQVQLEKTELKMDflrerELREtlEKQLAMEQKNRAIVQKRLKKEK 432
Cdd:CHL00019  49 LSDLldnrkQTILNTIRnseERREEAIE--KLEKARARLRQAELEAD-----EIRV--NGYSEIEREKENLINQAKEDLE 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 628601831 433 KAKRKLQEALEFETKR-REQAEQTLKQAASTDSLRVLNDSLTPEI 476
Cdd:CHL00019 120 RLENYKNETIRFEQQRaINQVRQQVFQLALQRALGTLNSCLNNEL 164
 
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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