unnamed protein product [Anisakis simplex]
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 ... |
31-135 | 4.57e-63 | |||
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: 191.42 E-value: 4.57e-63
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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 ... |
31-135 | 4.57e-63 | |||
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: 191.42 E-value: 4.57e-63
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Ski_Sno | pfam02437 | SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ... |
33-134 | 1.97e-27 | |||
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: 100.81 E-value: 1.97e-27
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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 ... |
31-135 | 4.57e-63 | |||
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: 191.42 E-value: 4.57e-63
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Ski_Sno | pfam02437 | SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ... |
33-134 | 1.97e-27 | |||
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: 100.81 E-value: 1.97e-27
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DHD_Ski_Sno_Dac | cd21074 | Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ... |
33-131 | 3.17e-21 | |||
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: 84.27 E-value: 3.17e-21
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DHD_SKIDA1 | cd21082 | Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ... |
37-134 | 5.55e-08 | |||
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: 49.26 E-value: 5.55e-08
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DHD_Sno | cd21084 | Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ... |
26-130 | 3.35e-04 | |||
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: 38.79 E-value: 3.35e-04
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DHD_Ski_Sno | cd21079 | Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ... |
40-132 | 3.78e-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: 38.31 E-value: 3.78e-04
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Blast search parameters | ||||
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