NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907129143|ref|XP_006525802|]
View 

putative Polycomb group protein ASXL3 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
 209-334 4.62e-39

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


:

Pssm-ID: 464041  Cd Length: 129  Bit Score: 142.43  E-value: 4.62e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129143  209 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASFPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 286
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907129143  287 AYAAQGWKQRLAEGEFTPEMQLRIRQEIEKEK-KTEPWKEKFFERFYGE 334
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 super family cl16478
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
 2177-2232 1.97e-19

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


The actual alignment was detected with superfamily member pfam13922:

Pssm-ID: 316444  Cd Length: 68  Bit Score: 84.18  E-value: 1.97e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907129143 2177 QNTQMPVQNFADNSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2232
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 1-55 1.73e-10

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


:

Pssm-ID: 461541  Cd Length: 71  Bit Score: 58.86  E-value: 1.73e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907129143    1 MTAKQILEVIQKEGLKETrNGTSPLACLNAMLHTNTRvGDGTFFKI-PGKSGLYAL 55
Cdd:pfam05066   18 LHFKEIAEEIQEKGLISL-SGKTPEATLAAQLYTDIK-EDSLFVRVgPGTFGLRSW 71
 
Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
 209-334 4.62e-39

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


Pssm-ID: 464041  Cd Length: 129  Bit Score: 142.43  E-value: 4.62e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129143  209 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASFPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 286
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907129143  287 AYAAQGWKQRLAEGEFTPEMQLRIRQEIEKEK-KTEPWKEKFFERFYGE 334
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
 2177-2232 1.97e-19

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


Pssm-ID: 316444  Cd Length: 68  Bit Score: 84.18  E-value: 1.97e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907129143 2177 QNTQMPVQNFADNSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2232
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 1-55 1.73e-10

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


Pssm-ID: 461541  Cd Length: 71  Bit Score: 58.86  E-value: 1.73e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907129143    1 MTAKQILEVIQKEGLKETrNGTSPLACLNAMLHTNTRvGDGTFFKI-PGKSGLYAL 55
Cdd:pfam05066   18 LHFKEIAEEIQEKGLISL-SGKTPEATLAAQLYTDIK-EDSLFVRVgPGTFGLRSW 71
 
Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
 209-334 4.62e-39

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


Pssm-ID: 464041  Cd Length: 129  Bit Score: 142.43  E-value: 4.62e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129143  209 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASFPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 286
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907129143  287 AYAAQGWKQRLAEGEFTPEMQLRIRQEIEKEK-KTEPWKEKFFERFYGE 334
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
 2177-2232 1.97e-19

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


Pssm-ID: 316444  Cd Length: 68  Bit Score: 84.18  E-value: 1.97e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907129143 2177 QNTQMPVQNFADNSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2232
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 1-55 1.73e-10

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


Pssm-ID: 461541  Cd Length: 71  Bit Score: 58.86  E-value: 1.73e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907129143    1 MTAKQILEVIQKEGLKETrNGTSPLACLNAMLHTNTRvGDGTFFKI-PGKSGLYAL 55
Cdd:pfam05066   18 LHFKEIAEEIQEKGLISL-SGKTPEATLAAQLYTDIK-EDSLFVRVgPGTFGLRSW 71
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH