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Conserved domains on  [gi|1622890314|ref|XP_014977283|]
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putative Polycomb group protein ASXL3 isoform X4 [Macaca mulatta]

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 1.25e-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: 143.97  E-value: 1.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  179 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASLPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 256
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622890314  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 ...
2136-2191 3.62e-20

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: 86.11  E-value: 3.62e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622890314 2136 QNAQMPVQNFADSSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2191
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
498-770 1.12e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  498 SDTERKESETAIETSTPKIKTGSSSLEGRF-PNEGISVDMELQSDPEEQLSENACISET--------SFSSESPEGACTS 568
Cdd:pfam03154   89 SDTEEPERATAKKSKTQEISRPNSPSEGEGeSSDGRSVNDEGSSDPKDIDQDNRSTSPSipspqdneSDSDSSAQQQILQ 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  569 LPSPGGETQSTSEESCTPASLETTFCSEVSSTENTdkynqrnstdenlhASLMSEISPISTSPELSEASLMSNLPLTSEA 648
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSA--------------PSVPPQGSPATSQPPNQTQSTAAPHTLIQQT 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  649 SPISNLPLTSETSPMSDLPLTSETSSVSSmlltsettfvSSLPLPSEASPIsnssinERMAHQQRKSPSVSEEPLSPQkd 728
Cdd:pfam03154  235 PTLHPQRLPSPHPPLQPMTQPPPPSQVSP----------QPLPQPSLHGQM------PPMPHSLQTGPSHMQHPVPPQ-- 296
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1622890314  729 essaaakPVGENLTSQQKNLSNTPEPIIMSSSSITPEAFPSE 770
Cdd:pfam03154  297 -------PFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQ 331
 
Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
179-304 1.25e-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: 143.97  E-value: 1.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  179 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASLPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 256
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622890314  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 ...
2136-2191 3.62e-20

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: 86.11  E-value: 3.62e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622890314 2136 QNAQMPVQNFADSSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2191
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
498-770 1.12e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  498 SDTERKESETAIETSTPKIKTGSSSLEGRF-PNEGISVDMELQSDPEEQLSENACISET--------SFSSESPEGACTS 568
Cdd:pfam03154   89 SDTEEPERATAKKSKTQEISRPNSPSEGEGeSSDGRSVNDEGSSDPKDIDQDNRSTSPSipspqdneSDSDSSAQQQILQ 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  569 LPSPGGETQSTSEESCTPASLETTFCSEVSSTENTdkynqrnstdenlhASLMSEISPISTSPELSEASLMSNLPLTSEA 648
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSA--------------PSVPPQGSPATSQPPNQTQSTAAPHTLIQQT 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  649 SPISNLPLTSETSPMSDLPLTSETSSVSSmlltsettfvSSLPLPSEASPIsnssinERMAHQQRKSPSVSEEPLSPQkd 728
Cdd:pfam03154  235 PTLHPQRLPSPHPPLQPMTQPPPPSQVSP----------QPLPQPSLHGQM------PPMPHSLQTGPSHMQHPVPPQ-- 296
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1622890314  729 essaaakPVGENLTSQQKNLSNTPEPIIMSSSSITPEAFPSE 770
Cdd:pfam03154  297 -------PFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQ 331
 
Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
179-304 1.25e-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: 143.97  E-value: 1.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  179 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASLPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 256
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622890314  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 ...
2136-2191 3.62e-20

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: 86.11  E-value: 3.62e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622890314 2136 QNAQMPVQNFADSSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2191
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
498-770 1.12e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  498 SDTERKESETAIETSTPKIKTGSSSLEGRF-PNEGISVDMELQSDPEEQLSENACISET--------SFSSESPEGACTS 568
Cdd:pfam03154   89 SDTEEPERATAKKSKTQEISRPNSPSEGEGeSSDGRSVNDEGSSDPKDIDQDNRSTSPSipspqdneSDSDSSAQQQILQ 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  569 LPSPGGETQSTSEESCTPASLETTFCSEVSSTENTdkynqrnstdenlhASLMSEISPISTSPELSEASLMSNLPLTSEA 648
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSA--------------PSVPPQGSPATSQPPNQTQSTAAPHTLIQQT 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890314  649 SPISNLPLTSETSPMSDLPLTSETSSVSSmlltsettfvSSLPLPSEASPIsnssinERMAHQQRKSPSVSEEPLSPQkd 728
Cdd:pfam03154  235 PTLHPQRLPSPHPPLQPMTQPPPPSQVSP----------QPLPQPSLHGQM------PPMPHSLQTGPSHMQHPVPPQ-- 296
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1622890314  729 essaaakPVGENLTSQQKNLSNTPEPIIMSSSSITPEAFPSE 770
Cdd:pfam03154  297 -------PFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQ 331
 
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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