dachshund homolog 1 isoform b [Homo sapiens]
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 | 2.63e-72 | |||
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: 2.63e-72
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ATP-synt_Fo_b super family | cl21478 | F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
415-530 | 5.67e-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: 38.31 E-value: 5.67e-03
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Name | Accession | Description | Interval | E-value | |||
DHD_Dac | cd21081 | Dachshund-homology domain found in the retinal determination protein Dachshund and similar ... |
186-280 | 2.63e-72 | |||
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: 2.63e-72
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Ski_Sno | pfam02437 | SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ... |
181-281 | 8.84e-42 | |||
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: 145.50 E-value: 8.84e-42
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atpF | CHL00019 | ATP synthase CF0 B subunit |
415-530 | 5.67e-03 | |||
ATP synthase CF0 B subunit Pssm-ID: 176962 [Multi-domain] Cd Length: 184 Bit Score: 38.31 E-value: 5.67e-03
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Name | Accession | Description | Interval | E-value | |||
DHD_Dac | cd21081 | Dachshund-homology domain found in the retinal determination protein Dachshund and similar ... |
186-280 | 2.63e-72 | |||
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: 2.63e-72
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Ski_Sno | pfam02437 | SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ... |
181-281 | 8.84e-42 | |||
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: 145.50 E-value: 8.84e-42
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DHD_Ski_Sno_Dac | cd21074 | Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ... |
188-277 | 2.69e-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: 2.69e-30
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DHD_SKIDA1 | cd21082 | Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ... |
188-279 | 3.89e-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: 3.89e-10
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DHD_Sno | cd21084 | Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ... |
185-277 | 4.82e-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: 45.34 E-value: 4.82e-06
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DHD_Skor | cd21080 | Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ... |
188-275 | 5.41e-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: 44.74 E-value: 5.41e-06
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DHD_Ski_Sno | cd21079 | Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ... |
188-277 | 3.24e-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: 39.86 E-value: 3.24e-04
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DHD_Ski | cd21083 | Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ... |
188-277 | 1.84e-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: 38.13 E-value: 1.84e-03
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atpF | CHL00019 | ATP synthase CF0 B subunit |
415-530 | 5.67e-03 | |||
ATP synthase CF0 B subunit Pssm-ID: 176962 [Multi-domain] Cd Length: 184 Bit Score: 38.31 E-value: 5.67e-03
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Blast search parameters | ||||
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