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Conserved domains on  [gi|1720354832|ref|XP_030109041|]
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R3H domain-containing protein 1 isoform X16 [Mus musculus]

Protein Classification

R3H domain-containing protein( domain architecture ID 11552619)

R3H domain-containing protein with SUZ and Med15 domains, may bind ssDNA or ssRNA in a sequence-specific manner; similar to Mus musculus R3H domain-containing protein 2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
123-184 4.31e-26

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


:

Pssm-ID: 100071  Cd Length: 63  Bit Score: 101.91  E-value: 4.31e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354832 123 DRMMLLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG-KSVIVNKT 184
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
207-258 2.07e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


:

Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 62.72  E-value: 2.07e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720354832 207 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 258
Cdd:pfam12752   3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
493-814 1.51e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.30  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 493 PSPQMPACYCAPGHyhSSQPQYRPIPSVHHSSHLNQPLPQPAQHTGYQVMPNQQQnyQGIVGVQSPQS--QSLMGG---- 566
Cdd:pfam09606 140 PSQMSRVGRMQPGG--QAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQ--QGPMGGQMPPQmgVPGMPGpada 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 567 -------QPNSTGPHIQGVVIPYPSVPSYQV-SLPQGSQGIAHQTYQQPVVFPnQSNQGSLPtTGMPVyYSVIPPGQQSN 638
Cdd:pfam09606 216 gaqmgqqAQANGGMNPQQMGGAPNQVAMQQQqPQQQGQQSQLGMGINQMQQMP-QGVGGGAG-QGGPG-QPMGPPGQQPG 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 639 LSSAVGYLQHPGSEQVQFPRTtspcSSQQLQGHQCAAVPQQPpgggmvmmqlNLPNNPQSRTHSPPQwkQNKHYCDHQRG 718
Cdd:pfam09606 293 AMPNVMSIGDQNNYQQQQTRQ----QQQQQGGNHPAAHQQQM----------NQSVGQGGQVVALGG--LNHLETWNPGN 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 719 QkcmDFSNMDNIVQPSPQ-LSSPilSPVQSPAPAQLSTLKTIRPSGPPlsimsQFARPFVPGQGDARYPlLGQPLQynPP 797
Cdd:pfam09606 357 F---GGLGANPMQRGQPGmMSSP--SPVPGQQVRQVTPNQFMRQSPQP-----SVPSPQGPGSQPPQSH-PGGMIP--SP 423
                         330
                  ....*....|....*...
gi 1720354832 798 TLLHGHIPH-QQGQSGSR 814
Cdd:pfam09606 424 ALIPSPSPQmSQQPAQQR 441
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
123-184 4.31e-26

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 101.91  E-value: 4.31e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354832 123 DRMMLLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG-KSVIVNKT 184
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
107-184 1.76e-17

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 77.73  E-value: 1.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832  107 IDLHEFLVNTLKNNPRDRMMLLKLEQEILDFIgNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG--KSVIVNKT 184
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFV-KSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
207-258 2.07e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 62.72  E-value: 2.07e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720354832 207 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 258
Cdd:pfam12752   3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
125-183 2.24e-11

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 59.81  E-value: 2.24e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354832 125 MMLLKLEQEILDFIGNNESPrKKFPPMTSYHRMLLHRVAAYFGLDHNV--DQSGKSVIVNK 183
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKS-LELPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
493-814 1.51e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.30  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 493 PSPQMPACYCAPGHyhSSQPQYRPIPSVHHSSHLNQPLPQPAQHTGYQVMPNQQQnyQGIVGVQSPQS--QSLMGG---- 566
Cdd:pfam09606 140 PSQMSRVGRMQPGG--QAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQ--QGPMGGQMPPQmgVPGMPGpada 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 567 -------QPNSTGPHIQGVVIPYPSVPSYQV-SLPQGSQGIAHQTYQQPVVFPnQSNQGSLPtTGMPVyYSVIPPGQQSN 638
Cdd:pfam09606 216 gaqmgqqAQANGGMNPQQMGGAPNQVAMQQQqPQQQGQQSQLGMGINQMQQMP-QGVGGGAG-QGGPG-QPMGPPGQQPG 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 639 LSSAVGYLQHPGSEQVQFPRTtspcSSQQLQGHQCAAVPQQPpgggmvmmqlNLPNNPQSRTHSPPQwkQNKHYCDHQRG 718
Cdd:pfam09606 293 AMPNVMSIGDQNNYQQQQTRQ----QQQQQGGNHPAAHQQQM----------NQSVGQGGQVVALGG--LNHLETWNPGN 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 719 QkcmDFSNMDNIVQPSPQ-LSSPilSPVQSPAPAQLSTLKTIRPSGPPlsimsQFARPFVPGQGDARYPlLGQPLQynPP 797
Cdd:pfam09606 357 F---GGLGANPMQRGQPGmMSSP--SPVPGQQVRQVTPNQFMRQSPQP-----SVPSPQGPGSQPPQSH-PGGMIP--SP 423
                         330
                  ....*....|....*...
gi 1720354832 798 TLLHGHIPH-QQGQSGSR 814
Cdd:pfam09606 424 ALIPSPSPQmSQQPAQQR 441
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
123-184 4.31e-26

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 101.91  E-value: 4.31e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354832 123 DRMMLLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG-KSVIVNKT 184
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
107-184 1.76e-17

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 77.73  E-value: 1.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832  107 IDLHEFLVNTLKNNPRDRMMLLKLEQEILDFIgNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG--KSVIVNKT 184
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFV-KSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
207-258 2.07e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 62.72  E-value: 2.07e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720354832 207 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 258
Cdd:pfam12752   3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
125-183 2.24e-11

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 59.81  E-value: 2.24e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354832 125 MMLLKLEQEILDFIGNNESPrKKFPPMTSYHRMLLHRVAAYFGLDHNV--DQSGKSVIVNK 183
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKS-LELPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
127-183 6.17e-11

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 58.39  E-value: 6.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354832 127 LLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG--KSVIVNK 183
Cdd:cd02325     1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
493-814 1.51e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.30  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 493 PSPQMPACYCAPGHyhSSQPQYRPIPSVHHSSHLNQPLPQPAQHTGYQVMPNQQQnyQGIVGVQSPQS--QSLMGG---- 566
Cdd:pfam09606 140 PSQMSRVGRMQPGG--QAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQ--QGPMGGQMPPQmgVPGMPGpada 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 567 -------QPNSTGPHIQGVVIPYPSVPSYQV-SLPQGSQGIAHQTYQQPVVFPnQSNQGSLPtTGMPVyYSVIPPGQQSN 638
Cdd:pfam09606 216 gaqmgqqAQANGGMNPQQMGGAPNQVAMQQQqPQQQGQQSQLGMGINQMQQMP-QGVGGGAG-QGGPG-QPMGPPGQQPG 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 639 LSSAVGYLQHPGSEQVQFPRTtspcSSQQLQGHQCAAVPQQPpgggmvmmqlNLPNNPQSRTHSPPQwkQNKHYCDHQRG 718
Cdd:pfam09606 293 AMPNVMSIGDQNNYQQQQTRQ----QQQQQGGNHPAAHQQQM----------NQSVGQGGQVVALGG--LNHLETWNPGN 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 719 QkcmDFSNMDNIVQPSPQ-LSSPilSPVQSPAPAQLSTLKTIRPSGPPlsimsQFARPFVPGQGDARYPlLGQPLQynPP 797
Cdd:pfam09606 357 F---GGLGANPMQRGQPGmMSSP--SPVPGQQVRQVTPNQFMRQSPQP-----SVPSPQGPGSQPPQSH-PGGMIP--SP 423
                         330
                  ....*....|....*...
gi 1720354832 798 TLLHGHIPH-QQGQSGSR 814
Cdd:pfam09606 424 ALIPSPSPQmSQQPAQQR 441
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
452-681 5.34e-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: 40.91  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 452 PPPPPPPPSLPPGQSVPTASFSASGHPVSQPVLQQQGFLPQPSPQMPacycAPGHYHSSQPQYRPIPSVHHSSHLNQPLP 531
Cdd:pfam03154 251 PMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 532 QPaqhtgyqvmPNQQQNYQGivgvQSPQSQSLMGGqPNSTgPHIQgvviPYPSVPSYQVSLPQGSQGIAHQTYQQPVVFP 611
Cdd:pfam03154 327 TP---------PSQSQLQSQ----QPPREQPLPPA-PLSM-PHIK----PPPTTPIPQLPNPQSHKHPPHLSGPSPFQMN 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 612 NQ-----------SNQGSLPTTGMPVYYSVIPPGQQSNLSSAvgylQHPGSEQVQfprTTSPCSSQQLQGHQCAAVPQQP 680
Cdd:pfam03154 388 SNlppppalkplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPA----QPPVLTQSQ---SLPPPAASHPPTSGLHQVPSQS 460

                  .
gi 1720354832 681 P 681
Cdd:pfam03154 461 P 461
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
530-801 7.00e-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: 40.52  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 530 LPQPAQHTGYQVMPNQQQNYQGIVGVQSPQSQSLMGGQPNSTGPHIQGVVIPYPSVPSY-------------QVSLPQGS 596
Cdd:pfam03154 148 IPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVppqgspatsqppnQTQSTAAP 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 597 QGIAHQTYQ-------------QPVVFPNQSNQGSLPTTGMPVYYSVIPPGQQSnLSSAVGYLQHPG----------SEQ 653
Cdd:pfam03154 228 HTLIQQTPTlhpqrlpsphpplQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHS-LQTGPSHMQHPVppqpfpltpqSSQ 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354832 654 VQFPRTTSPCSSQQLQGHQCAAVPQQPPGGGMVMMQLNLPNNPQSRTH-SPPQWKQNKHYCDHQRGQKCMDFSNmdnivq 732
Cdd:pfam03154 307 SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHiKPPPTTPIPQLPNPQSHKHPPHLSG------ 380
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354832 733 PSP-QLSSPILSPvqsPAPAQLSTLKTIRPSG---PPLSIMSQfARPFVPGQgdARYPLLGQPLQYNPPTLLH 801
Cdd:pfam03154 381 PSPfQMNSNLPPP---PALKPLSSLSTHHPPSahpPPLQLMPQ-SQQLPPPP--AQPPVLTQSQSLPPPAASH 447
 
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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