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Conserved domains on  [gi|2462519159|ref|XP_054221824|]
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SKI/DACH domain-containing protein 1 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EPOP pfam15223
Elongin BC and Polycomb repressive complex 2-associated protein; This family of proteins is ...
 534-965 0e+00

Elongin BC and Polycomb repressive complex 2-associated protein; This family of proteins is found in eukaryotes. Family members are approximately 835 amino acids in length and include the polycomb repressive complex 2-associated factor EPOP (Elongin BC and Polycomb Repressive Complex 2 (PRC2) Associated Protein, also termed C17orf96, esPRC2p48, E130012A19Rik), a scaffold protein expressed in the inner cell mass of the mouse blastocyst serving as a bridging partner between the PRC2/EED-EZH2 complex and the elongin BC complex, and fine-tuning the transcriptional status of Polycomb group (PcG) target genes in embryonic stem cells. Both EPOP and Elongin BC are required to maintain low levels of expression at PRC2 genomic targets. EPOP interacts with the H2B deubiquitinase USP7 to modulate transcriptional processes in mESCs similar to MYC. Functional studies found that the C-terminal region of EPOP directly interacts with PRC2 and that this region associates with the VEFS-box of the PRC2 core member SUZ12. Thus, suggesting that EPOP may directly affect PRC2 chromatin binding by altering the functionality of Suz12. This region is proposed to have evolved in early vertebrates and is also present in the paralog SKIDA1 (C10orf140) another novel PRC2-interacting protein, supporting the idea that proteins possessing this sequence are PRC2 regulators in the entire vertebrate branch. The family is found in association with pfam02437.


:

Pssm-ID: 434546  Cd Length: 426  Bit Score: 586.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 534 PSVQAQANFLYHLASAAAATK--PAAFEDAGRLPDLKSSVKAESPAEWNLQSWAPKASPVYCPASLGSCFAEIRNDRVSE 611
Cdd:pfam15223   1 PPLLAQPSFQYNLVANGHNQGvgTALEGAIAGLKDPKSDVKSESHEKPSDQSCLPKPPSVPQSASLGSCFPEIKRDRTSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 612 ITFPHSEISNaVKRTDLTINCLAEGASSPSPKTNNAFPQQRILREARKCLQTTPTTHCADNNTIAARFLNNdssgAEANS 691
Cdd:pfam15223  81 IAFPHSEIDD-VKRTDPTINVLVERESSPGPKENKEFSQQRILREAPKCGSGPGASHCAENEVIKKPGLND----AILNS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 692 EKYSKILHCPEFATDLPSSQTDPEvNAAGAAATKAENpctDTGDKTLPFLHNIKIKVEDSSANEEYEPHL--FTNKLKCE 769
Cdd:pfam15223 156 KKESKIPNQSKLAPPFKKVKSESE-DTSLSAKRHANN---TSGVKTPPFLHNVKIKVEESSDNEEYSSELskIPPKLKYK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 770 CNDTKGEFYSVTESKEEDALlTTAKEGFACPEKETPSLNPLAQSQGLSCTLGSPKPEDGEYKFGARVRKNYRTLVLGKRP 849
Cdd:pfam15223 232 CKVDENELTNKTEAISSEAG-ALRREDFNSKEKKTTSLNPLTQSQEPQCTLKTPKPELGEYKKGARVRKNYRTLVLGKRS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 850 VLQTPPVKPNLKSARSPRPTGKTETNEGTLDDFTVINRRKKVASNVASAVKRPFHFMANFPCPPSLIIGRDGDLWPAYSL 929
Cdd:pfam15223 311 EKKDPPLKKNLKSDRSPRSTGKTEPHEGTLEDFTVLSRRKRVASNVASPVKKPFNFMANFPSPPSLIIGNDGDLAPAYSL 390

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2462519159 930 NTTKDSQTPHKAHPIWKWQLGGSAIPLPPSHKFRKF 965
Cdd:pfam15223 391 NSEKDPQPPHKSHPVWKWQLGGSAIPLPPSHKFRKF 426
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 63-153 1.11e-49

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: 170.22  E-value: 1.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  63 SGFEEVDGVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISR 142
Cdd:cd21082     1 CGREEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISR 80

                          90
                  ....*....|.
gi 2462519159 143 EDVEALYTSCK 153
Cdd:cd21082    81 EDVERLYSSYK 91
 
Name Accession Description Interval E-value
EPOP pfam15223
Elongin BC and Polycomb repressive complex 2-associated protein; This family of proteins is ...
 534-965 0e+00

Elongin BC and Polycomb repressive complex 2-associated protein; This family of proteins is found in eukaryotes. Family members are approximately 835 amino acids in length and include the polycomb repressive complex 2-associated factor EPOP (Elongin BC and Polycomb Repressive Complex 2 (PRC2) Associated Protein, also termed C17orf96, esPRC2p48, E130012A19Rik), a scaffold protein expressed in the inner cell mass of the mouse blastocyst serving as a bridging partner between the PRC2/EED-EZH2 complex and the elongin BC complex, and fine-tuning the transcriptional status of Polycomb group (PcG) target genes in embryonic stem cells. Both EPOP and Elongin BC are required to maintain low levels of expression at PRC2 genomic targets. EPOP interacts with the H2B deubiquitinase USP7 to modulate transcriptional processes in mESCs similar to MYC. Functional studies found that the C-terminal region of EPOP directly interacts with PRC2 and that this region associates with the VEFS-box of the PRC2 core member SUZ12. Thus, suggesting that EPOP may directly affect PRC2 chromatin binding by altering the functionality of Suz12. This region is proposed to have evolved in early vertebrates and is also present in the paralog SKIDA1 (C10orf140) another novel PRC2-interacting protein, supporting the idea that proteins possessing this sequence are PRC2 regulators in the entire vertebrate branch. The family is found in association with pfam02437.


Pssm-ID: 434546  Cd Length: 426  Bit Score: 586.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 534 PSVQAQANFLYHLASAAAATK--PAAFEDAGRLPDLKSSVKAESPAEWNLQSWAPKASPVYCPASLGSCFAEIRNDRVSE 611
Cdd:pfam15223   1 PPLLAQPSFQYNLVANGHNQGvgTALEGAIAGLKDPKSDVKSESHEKPSDQSCLPKPPSVPQSASLGSCFPEIKRDRTSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 612 ITFPHSEISNaVKRTDLTINCLAEGASSPSPKTNNAFPQQRILREARKCLQTTPTTHCADNNTIAARFLNNdssgAEANS 691
Cdd:pfam15223  81 IAFPHSEIDD-VKRTDPTINVLVERESSPGPKENKEFSQQRILREAPKCGSGPGASHCAENEVIKKPGLND----AILNS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 692 EKYSKILHCPEFATDLPSSQTDPEvNAAGAAATKAENpctDTGDKTLPFLHNIKIKVEDSSANEEYEPHL--FTNKLKCE 769
Cdd:pfam15223 156 KKESKIPNQSKLAPPFKKVKSESE-DTSLSAKRHANN---TSGVKTPPFLHNVKIKVEESSDNEEYSSELskIPPKLKYK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 770 CNDTKGEFYSVTESKEEDALlTTAKEGFACPEKETPSLNPLAQSQGLSCTLGSPKPEDGEYKFGARVRKNYRTLVLGKRP 849
Cdd:pfam15223 232 CKVDENELTNKTEAISSEAG-ALRREDFNSKEKKTTSLNPLTQSQEPQCTLKTPKPELGEYKKGARVRKNYRTLVLGKRS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 850 VLQTPPVKPNLKSARSPRPTGKTETNEGTLDDFTVINRRKKVASNVASAVKRPFHFMANFPCPPSLIIGRDGDLWPAYSL 929
Cdd:pfam15223 311 EKKDPPLKKNLKSDRSPRSTGKTEPHEGTLEDFTVLSRRKRVASNVASPVKKPFNFMANFPSPPSLIIGNDGDLAPAYSL 390

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2462519159 930 NTTKDSQTPHKAHPIWKWQLGGSAIPLPPSHKFRKF 965
Cdd:pfam15223 391 NSEKDPQPPHKSHPVWKWQLGGSAIPLPPSHKFRKF 426
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 63-153 1.11e-49

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: 170.22  E-value: 1.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  63 SGFEEVDGVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISR 142
Cdd:cd21082     1 CGREEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISR 80

                          90
                  ....*....|.
gi 2462519159 143 EDVEALYTSCK 153
Cdd:cd21082    81 EDVERLYSSYK 91
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 70-152 9.68e-07

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: 48.04  E-value: 9.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  70 GVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISREDVEALY 149
Cdd:pfam02437  16 GEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSVRRCGLITKTDAERLC 95


                  ...
gi 2462519159 150 TSC 152
Cdd:pfam02437  96 DAL 98
 
Name Accession Description Interval E-value
EPOP pfam15223
Elongin BC and Polycomb repressive complex 2-associated protein; This family of proteins is ...
 534-965 0e+00

Elongin BC and Polycomb repressive complex 2-associated protein; This family of proteins is found in eukaryotes. Family members are approximately 835 amino acids in length and include the polycomb repressive complex 2-associated factor EPOP (Elongin BC and Polycomb Repressive Complex 2 (PRC2) Associated Protein, also termed C17orf96, esPRC2p48, E130012A19Rik), a scaffold protein expressed in the inner cell mass of the mouse blastocyst serving as a bridging partner between the PRC2/EED-EZH2 complex and the elongin BC complex, and fine-tuning the transcriptional status of Polycomb group (PcG) target genes in embryonic stem cells. Both EPOP and Elongin BC are required to maintain low levels of expression at PRC2 genomic targets. EPOP interacts with the H2B deubiquitinase USP7 to modulate transcriptional processes in mESCs similar to MYC. Functional studies found that the C-terminal region of EPOP directly interacts with PRC2 and that this region associates with the VEFS-box of the PRC2 core member SUZ12. Thus, suggesting that EPOP may directly affect PRC2 chromatin binding by altering the functionality of Suz12. This region is proposed to have evolved in early vertebrates and is also present in the paralog SKIDA1 (C10orf140) another novel PRC2-interacting protein, supporting the idea that proteins possessing this sequence are PRC2 regulators in the entire vertebrate branch. The family is found in association with pfam02437.


Pssm-ID: 434546  Cd Length: 426  Bit Score: 586.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 534 PSVQAQANFLYHLASAAAATK--PAAFEDAGRLPDLKSSVKAESPAEWNLQSWAPKASPVYCPASLGSCFAEIRNDRVSE 611
Cdd:pfam15223   1 PPLLAQPSFQYNLVANGHNQGvgTALEGAIAGLKDPKSDVKSESHEKPSDQSCLPKPPSVPQSASLGSCFPEIKRDRTSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 612 ITFPHSEISNaVKRTDLTINCLAEGASSPSPKTNNAFPQQRILREARKCLQTTPTTHCADNNTIAARFLNNdssgAEANS 691
Cdd:pfam15223  81 IAFPHSEIDD-VKRTDPTINVLVERESSPGPKENKEFSQQRILREAPKCGSGPGASHCAENEVIKKPGLND----AILNS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 692 EKYSKILHCPEFATDLPSSQTDPEvNAAGAAATKAENpctDTGDKTLPFLHNIKIKVEDSSANEEYEPHL--FTNKLKCE 769
Cdd:pfam15223 156 KKESKIPNQSKLAPPFKKVKSESE-DTSLSAKRHANN---TSGVKTPPFLHNVKIKVEESSDNEEYSSELskIPPKLKYK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 770 CNDTKGEFYSVTESKEEDALlTTAKEGFACPEKETPSLNPLAQSQGLSCTLGSPKPEDGEYKFGARVRKNYRTLVLGKRP 849
Cdd:pfam15223 232 CKVDENELTNKTEAISSEAG-ALRREDFNSKEKKTTSLNPLTQSQEPQCTLKTPKPELGEYKKGARVRKNYRTLVLGKRS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159 850 VLQTPPVKPNLKSARSPRPTGKTETNEGTLDDFTVINRRKKVASNVASAVKRPFHFMANFPCPPSLIIGRDGDLWPAYSL 929
Cdd:pfam15223 311 EKKDPPLKKNLKSDRSPRSTGKTEPHEGTLEDFTVLSRRKRVASNVASPVKKPFNFMANFPSPPSLIIGNDGDLAPAYSL 390

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2462519159 930 NTTKDSQTPHKAHPIWKWQLGGSAIPLPPSHKFRKF 965
Cdd:pfam15223 391 NSEKDPQPPHKSHPVWKWQLGGSAIPLPPSHKFRKF 426
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 63-153 1.11e-49

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: 170.22  E-value: 1.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  63 SGFEEVDGVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISR 142
Cdd:cd21082     1 CGREEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISR 80

                          90
                  ....*....|.
gi 2462519159 143 EDVEALYTSCK 153
Cdd:cd21082    81 EDVERLYSSYK 91
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 63-150 3.09e-29

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: 111.62  E-value: 3.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  63 SGFEEVDGVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISR 142
Cdd:cd21074     1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLISK 80


                  ....*...
gi 2462519159 143 EDVEALYT 150
Cdd:cd21074    81 SDAERLLN 88
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 67-152 3.07e-08

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: 51.98  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  67 EVDGVRLGYLIIKGKQMFALSQVFTDLLKNI--PRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISRED 144
Cdd:cd21081     7 EYRGAKVAAFTVDGEELICLPQAFELFLKHLvgGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLISRKD 86


                  ....*...
gi 2462519159 145 VEALYTSC 152
Cdd:cd21081    87 FDTLYNDC 94
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 70-152 9.68e-07

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: 48.04  E-value: 9.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  70 GVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISREDVEALY 149
Cdd:pfam02437  16 GEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSVRRCGLITKTDAERLC 95


                  ...
gi 2462519159 150 TSC 152
Cdd:pfam02437  96 DAL 98
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 67-149 2.06e-03

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: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  67 EVDGVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISREDVE 146
Cdd:cd21079     5 LLEGETIACFVVGGEKRLCLPQILNTVLRDFSLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITKTDAE 84


                  ...
gi 2462519159 147 ALY 149
Cdd:cd21079    85 RLC 87
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 68-148 2.51e-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: 38.51  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  68 VDGVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISREDVEA 147
Cdd:cd21083    15 LEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDAER 94


                  .
gi 2462519159 148 L 148
Cdd:cd21083    95 L 95
DHD_Skor cd21080
Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...
 70-151 5.99e-03

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: 37.04  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  70 GVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISREDVEALY 149
Cdd:cd21080     8 GVPIVSLVIDGQERLCLAQISNTLLKDYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITKREAERLC 87


                  ..
gi 2462519159 150 TS 151
Cdd:cd21080    88 KS 89
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 68-148 9.90e-03

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: 36.48  E-value: 9.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519159  68 VDGVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISREDVEA 147
Cdd:cd21084    13 LEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQR 92


                  .
gi 2462519159 148 L 148
Cdd:cd21084    93 L 93
 
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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