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Conserved domains on  [gi|24582233|ref|NP_609035|]
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Daxx-like protein, isoform A [Drosophila melanogaster]

Protein Classification

Atrophin-1 and DAXX_histone_binding domain-containing protein( domain architecture ID 10192128)

protein containing domains PTZ00449, Atrophin-1, and DAXX_histone_binding

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAXX_histone_binding cd13150
Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear ...
 1276-1462 1.61e-85

Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. DAXX is also a histone chaperone conserved in Metazoa that acts specifically on histone H3.3. This alignment models a functional domain of DAXX that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer.


:

Pssm-ID: 240523  Cd Length: 198  Bit Score: 277.58  E-value: 1.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233 1276 HFYRTLHAITKRIKMLEEAEVDLND-EDSSYLQLERFKKRACQIYEKICDLKGESKSVRRQLKKPIHFKDSDYPHFNNSL 1354
Cdd:cd13150    8 RLEKLLKKLSKEIRKLEEKEVDLLDdEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGTRYPEVNRKI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233 1355 SAFVNRMQDFPDYHDVLQILEKCNKEKELGLAKYEMKRIAYDAFNKVGRMLQSRRKNDLYETV-THYTANGKDPASSDPE 1433
Cdd:cd13150   88 EKFVNRNKTFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFgSHLTDDEKDPALEDPE 167

                        170       180       190
                 ....*....|....*....|....*....|
gi 24582233 1434 LLAKLKENNKK-QTKISDILEKYALEQDLN 1462
Cdd:cd13150  168 LKRKLEENRKIgDKRLNEVIEKYVNKQDDL 197
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 706-902 1.65e-04

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: 46.68  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233    706 QQQQMPQKKIVMQPQLPKTSVVLPRPQQLPKNPLLVAQQQSPKTPLVNSVMGPQFPSQ-QPSLPVVNQITHK-SMTIQRL 783
Cdd:pfam03154  163 QQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQtQSTAAPHTLIQQTpTLHPQRL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233    784 P-----MLQTVQKILPKQIAPQQTPPPAHIVQKQTMPNAAMQNPPFAHRPPIVRPMTVAKISP---VPTNNKVCIPMKPQ 855
Cdd:pfam03154  243 PsphppLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSqsqVPPGPSPAAPGQSQ 322

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 24582233    856 MASYVSPTDPTMTAARtlPFRssQRKTSEAPMTSTHVQGFTASATPP 902
Cdd:pfam03154  323 QRIHTPPSQSQLQSQQ--PPR--EQPLPPAPLSMPHIKPPPTTPIPQ 365
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 278-379 3.20e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.37  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233   278 PGKQQKPLECPVPAQQEKLPRGPL-PTKPAEPLSgplptePDEPLGGPLPTRPKPPVRSLQQPVNKNTAIGVQIQQSQEP 356
Cdd:PTZ00449  563 PAKEHKPSKIPTLSKKPEFPKDPKhPKDPEEPKK------PKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRP 636

                          90       100
                  ....*....|....*....|....
gi 24582233   357 LGGTLPTR-QKPLGGQLLTQQKPP 379
Cdd:PTZ00449  637 PPPQRPSSpERPEGPKIIKSPKPP 660
 
Name Accession Description Interval E-value
DAXX_histone_binding cd13150
Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear ...
 1276-1462 1.61e-85

Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. DAXX is also a histone chaperone conserved in Metazoa that acts specifically on histone H3.3. This alignment models a functional domain of DAXX that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer.


Pssm-ID: 240523  Cd Length: 198  Bit Score: 277.58  E-value: 1.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233 1276 HFYRTLHAITKRIKMLEEAEVDLND-EDSSYLQLERFKKRACQIYEKICDLKGESKSVRRQLKKPIHFKDSDYPHFNNSL 1354
Cdd:cd13150    8 RLEKLLKKLSKEIRKLEEKEVDLLDdEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGTRYPEVNRKI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233 1355 SAFVNRMQDFPDYHDVLQILEKCNKEKELGLAKYEMKRIAYDAFNKVGRMLQSRRKNDLYETV-THYTANGKDPASSDPE 1433
Cdd:cd13150   88 EKFVNRNKTFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFgSHLTDDEKDPALEDPE 167

                        170       180       190
                 ....*....|....*....|....*....|
gi 24582233 1434 LLAKLKENNKK-QTKISDILEKYALEQDLN 1462
Cdd:cd13150  168 LKRKLEENRKIgDKRLNEVIEKYVNKQDDL 197
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 706-902 1.65e-04

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: 46.68  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233    706 QQQQMPQKKIVMQPQLPKTSVVLPRPQQLPKNPLLVAQQQSPKTPLVNSVMGPQFPSQ-QPSLPVVNQITHK-SMTIQRL 783
Cdd:pfam03154  163 QQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQtQSTAAPHTLIQQTpTLHPQRL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233    784 P-----MLQTVQKILPKQIAPQQTPPPAHIVQKQTMPNAAMQNPPFAHRPPIVRPMTVAKISP---VPTNNKVCIPMKPQ 855
Cdd:pfam03154  243 PsphppLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSqsqVPPGPSPAAPGQSQ 322

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 24582233    856 MASYVSPTDPTMTAARtlPFRssQRKTSEAPMTSTHVQGFTASATPP 902
Cdd:pfam03154  323 QRIHTPPSQSQLQSQQ--PPR--EQPLPPAPLSMPHIKPPPTTPIPQ 365
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 278-379 3.20e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.37  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233   278 PGKQQKPLECPVPAQQEKLPRGPL-PTKPAEPLSgplptePDEPLGGPLPTRPKPPVRSLQQPVNKNTAIGVQIQQSQEP 356
Cdd:PTZ00449  563 PAKEHKPSKIPTLSKKPEFPKDPKhPKDPEEPKK------PKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRP 636

                          90       100
                  ....*....|....*....|....
gi 24582233   357 LGGTLPTR-QKPLGGQLLTQQKPP 379
Cdd:PTZ00449  637 PPPQRPSSpERPEGPKIIKSPKPP 660
 
Name Accession Description Interval E-value
DAXX_histone_binding cd13150
Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear ...
 1276-1462 1.61e-85

Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. DAXX is also a histone chaperone conserved in Metazoa that acts specifically on histone H3.3. This alignment models a functional domain of DAXX that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer.


Pssm-ID: 240523  Cd Length: 198  Bit Score: 277.58  E-value: 1.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233 1276 HFYRTLHAITKRIKMLEEAEVDLND-EDSSYLQLERFKKRACQIYEKICDLKGESKSVRRQLKKPIHFKDSDYPHFNNSL 1354
Cdd:cd13150    8 RLEKLLKKLSKEIRKLEEKEVDLLDdEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGTRYPEVNRKI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233 1355 SAFVNRMQDFPDYHDVLQILEKCNKEKELGLAKYEMKRIAYDAFNKVGRMLQSRRKNDLYETV-THYTANGKDPASSDPE 1433
Cdd:cd13150   88 EKFVNRNKTFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFgSHLTDDEKDPALEDPE 167

                        170       180       190
                 ....*....|....*....|....*....|
gi 24582233 1434 LLAKLKENNKK-QTKISDILEKYALEQDLN 1462
Cdd:cd13150  168 LKRKLEENRKIgDKRLNEVIEKYVNKQDDL 197
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 706-902 1.65e-04

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: 46.68  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233    706 QQQQMPQKKIVMQPQLPKTSVVLPRPQQLPKNPLLVAQQQSPKTPLVNSVMGPQFPSQ-QPSLPVVNQITHK-SMTIQRL 783
Cdd:pfam03154  163 QQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQtQSTAAPHTLIQQTpTLHPQRL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233    784 P-----MLQTVQKILPKQIAPQQTPPPAHIVQKQTMPNAAMQNPPFAHRPPIVRPMTVAKISP---VPTNNKVCIPMKPQ 855
Cdd:pfam03154  243 PsphppLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSqsqVPPGPSPAAPGQSQ 322

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 24582233    856 MASYVSPTDPTMTAARtlPFRssQRKTSEAPMTSTHVQGFTASATPP 902
Cdd:pfam03154  323 QRIHTPPSQSQLQSQQ--PPR--EQPLPPAPLSMPHIKPPPTTPIPQ 365
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 278-379 3.20e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.37  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582233   278 PGKQQKPLECPVPAQQEKLPRGPL-PTKPAEPLSgplptePDEPLGGPLPTRPKPPVRSLQQPVNKNTAIGVQIQQSQEP 356
Cdd:PTZ00449  563 PAKEHKPSKIPTLSKKPEFPKDPKhPKDPEEPKK------PKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRP 636

                          90       100
                  ....*....|....*....|....
gi 24582233   357 LGGTLPTR-QKPLGGQLLTQQKPP 379
Cdd:PTZ00449  637 PPPQRPSSpERPEGPKIIKSPKPP 660
 
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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