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Conserved domains on  [gi|1720392716|ref|XP_030106230|]
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putative Polycomb group protein ASXL3 isoform X4 [Mus musculus]

Protein Classification

ASXH and PHD_3 domain-containing protein( domain architecture ID 10621621)

ASXH and PHD_3 domain-containing protein

Graphical summary

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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 ...
 179-304 4.55e-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: 4.55e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392716  179 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASFPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 256
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1720392716  257 AYAAQGWKQRLAEGEFTPEMQLRIRQEIEKEK-KTEPWKEKFFERFYGE 304
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 ...
 2147-2202 1.92e-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: 1.92e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720392716 2147 QNTQMPVQNFADNSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2202
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
 
Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
 179-304 4.55e-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: 4.55e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392716  179 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASFPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 256
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1720392716  257 AYAAQGWKQRLAEGEFTPEMQLRIRQEIEKEK-KTEPWKEKFFERFYGE 304
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
 2147-2202 1.92e-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: 1.92e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720392716 2147 QNTQMPVQNFADNSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2202
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
 
Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
 179-304 4.55e-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: 4.55e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392716  179 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASFPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 256
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1720392716  257 AYAAQGWKQRLAEGEFTPEMQLRIRQEIEKEK-KTEPWKEKFFERFYGE 304
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
 2147-2202 1.92e-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: 1.92e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720392716 2147 QNTQMPVQNFADNSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2202
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
 
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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