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Conserved domains on  [gi|568908722|ref|XP_006529483|]
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R3H domain-containing protein 1 isoform X4 [Mus musculus]

Protein Classification

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 1.88e-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: 103.07  E-value: 1.88e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568908722  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 1.66e-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: 63.11  E-value: 1.66e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568908722   207 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 258
Cdd:pfam12752    3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
PTZ00440 super family cl36566
reticulocyte binding protein 2-like protein; Provisional
8-355 2.19e-04

reticulocyte binding protein 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00440:

Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 45.59  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722    8 IIKDETETMKDLEAEMRDTTRVENLIKSE--NYGKISAEKNEHCIDNNIDlqekiqiQLTQSFEKeekpsKDETDKEKAS 85
Cdd:PTZ00440 2347 GKDKNIELNNENNSYIIKTKEKINNLKEEfsKLLKNIKRNNTLCNNNNIK-------DFISNIGK-----SVETIKQRFS 2414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   86 DKLPRKMLSRDSSQEYTDSTGIdlheflVNTLKNNPRDRMMLLKLEQEI------LDFIGNNESPRKKFPPMTSYHRmll 159
Cdd:PTZ00440 2415 SNLPEKEKLHQIEENLNEIKNI------MNETKRISNVDAFTNKILQDIdneknkENNNMNAEKIDDLIENVTSHNE--- 2485
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722  160 hRVAAYFGLDHNVdqsgKSVIVNKTSNTripDQKFNEHIKDDRGEDFQKRYIL-------KRDNSSFDKDDSQMRI---R 229
Cdd:PTZ00440 2486 -KIKSELLIINDA----LRRVKEKKDEM---NKLFNSLTENNNNNNNSAKNIVdnstyiiNELESHVSKLNELLSYidnE 2557
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722  230 LKD--DRRSKSIEEREEEYQRARDRIFSQDSLCSQENYIIDKRIQDEDTIGT--QQRRQIFRVNKDASG-RSTNSHQSST 304
Cdd:PTZ00440 2558 IKEleNEKLKLLEKAKIEESRKERERIESETQEDNTDEEQINRQQQERLQKEeeQKAYSQERLNREVSGtDDTNKNHNTG 2637
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568908722  305 ENElkyseprpwSSTDSDSSLRNLKPAVTKASS-------FSGISVLTRGDSSGSSKS 355
Cdd:PTZ00440 2638 HDE---------SNYGRYSNKRNDYGQVRLAGGviiglsvFSSIIFISFKEKDEEEKD 2686
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
491-816 5.29e-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: 44.37  E-value: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   491 AASHMFSQPVGPLQSSSQPVQCSPAPYPSPLLPVSPTQQYSVDNLGAQFS-HMSLARQPSADGSDPHaTMFQSTVVLQSP 569
Cdd:pfam03154  162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSpATSQPPNQTQSTAAPH-TLIQQTPTLHPQ 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   570 QqsgyivtTAPPHPPPPPPPPPPPPSLPPGQSVPTASFSASGHPVSQPVLQQQGFLPQPSPQMPacycAPGHYHSSQPQY 649
Cdd:pfam03154  241 R-------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQV 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   650 RPIPSVHHSSHLNQPLPQPaqhtgyqvmPNQQQNYQGivgvQSPQSQSLMGGqPNSTgPHIQgvviPYPSVPSYQVSLPQ 729
Cdd:pfam03154  310 PPGPSPAAPGQSQQRIHTP---------PSQSQLQSQ----QPPREQPLPPA-PLSM-PHIK----PPPTTPIPQLPNPQ 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   730 GSQGIAHQTYQQPVVFPNQ-----------SNQGSLPTTGMPVYYSVIPPGQQSNLSSAvgylQHPGSEQVQfprTTSPC 798
Cdd:pfam03154  371 SHKHPPHLSGPSPFQMNSNlppppalkplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPA----QPPVLTQSQ---SLPPP 443
                          330
                   ....*....|....*...
gi 568908722   799 SSQQLQGHQCAAVPQQPP 816
Cdd:pfam03154  444 AASHPPTSGLHQVPSQSP 461
 
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 1.88e-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: 103.07  E-value: 1.88e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568908722  123 DRMMLLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG-KSVIVNKT 184
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
107-184 7.70e-18

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 78.88  E-value: 7.70e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722    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 1.66e-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: 63.11  E-value: 1.66e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568908722   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 1.45e-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: 60.58  E-value: 1.45e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568908722   125 MMLLKLEQEILDFIGNNESPrKKFPPMTSYHRMLLHRVAAYFGLDHNV--DQSGKSVIVNK 183
Cdd:pfam01424    1 EFLEQLAEKLAEFVKDTGKS-LELPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
8-355 2.19e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 45.59  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722    8 IIKDETETMKDLEAEMRDTTRVENLIKSE--NYGKISAEKNEHCIDNNIDlqekiqiQLTQSFEKeekpsKDETDKEKAS 85
Cdd:PTZ00440 2347 GKDKNIELNNENNSYIIKTKEKINNLKEEfsKLLKNIKRNNTLCNNNNIK-------DFISNIGK-----SVETIKQRFS 2414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   86 DKLPRKMLSRDSSQEYTDSTGIdlheflVNTLKNNPRDRMMLLKLEQEI------LDFIGNNESPRKKFPPMTSYHRmll 159
Cdd:PTZ00440 2415 SNLPEKEKLHQIEENLNEIKNI------MNETKRISNVDAFTNKILQDIdneknkENNNMNAEKIDDLIENVTSHNE--- 2485
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722  160 hRVAAYFGLDHNVdqsgKSVIVNKTSNTripDQKFNEHIKDDRGEDFQKRYIL-------KRDNSSFDKDDSQMRI---R 229
Cdd:PTZ00440 2486 -KIKSELLIINDA----LRRVKEKKDEM---NKLFNSLTENNNNNNNSAKNIVdnstyiiNELESHVSKLNELLSYidnE 2557
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722  230 LKD--DRRSKSIEEREEEYQRARDRIFSQDSLCSQENYIIDKRIQDEDTIGT--QQRRQIFRVNKDASG-RSTNSHQSST 304
Cdd:PTZ00440 2558 IKEleNEKLKLLEKAKIEESRKERERIESETQEDNTDEEQINRQQQERLQKEeeQKAYSQERLNREVSGtDDTNKNHNTG 2637
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568908722  305 ENElkyseprpwSSTDSDSSLRNLKPAVTKASS-------FSGISVLTRGDSSGSSKS 355
Cdd:PTZ00440 2638 HDE---------SNYGRYSNKRNDYGQVRLAGGviiglsvFSSIIFISFKEKDEEEKD 2686
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
491-816 5.29e-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: 44.37  E-value: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   491 AASHMFSQPVGPLQSSSQPVQCSPAPYPSPLLPVSPTQQYSVDNLGAQFS-HMSLARQPSADGSDPHaTMFQSTVVLQSP 569
Cdd:pfam03154  162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSpATSQPPNQTQSTAAPH-TLIQQTPTLHPQ 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   570 QqsgyivtTAPPHPPPPPPPPPPPPSLPPGQSVPTASFSASGHPVSQPVLQQQGFLPQPSPQMPacycAPGHYHSSQPQY 649
Cdd:pfam03154  241 R-------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQV 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   650 RPIPSVHHSSHLNQPLPQPaqhtgyqvmPNQQQNYQGivgvQSPQSQSLMGGqPNSTgPHIQgvviPYPSVPSYQVSLPQ 729
Cdd:pfam03154  310 PPGPSPAAPGQSQQRIHTP---------PSQSQLQSQ----QPPREQPLPPA-PLSM-PHIK----PPPTTPIPQLPNPQ 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   730 GSQGIAHQTYQQPVVFPNQ-----------SNQGSLPTTGMPVYYSVIPPGQQSNLSSAvgylQHPGSEQVQfprTTSPC 798
Cdd:pfam03154  371 SHKHPPHLSGPSPFQMNSNlppppalkplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPA----QPPVLTQSQ---SLPPP 443
                          330
                   ....*....|....*...
gi 568908722   799 SSQQLQGHQCAAVPQQPP 816
Cdd:pfam03154  444 AASHPPTSGLHQVPSQSP 461
 
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 1.88e-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: 103.07  E-value: 1.88e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568908722  123 DRMMLLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG-KSVIVNKT 184
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
107-184 7.70e-18

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 78.88  E-value: 7.70e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722    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 1.66e-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: 63.11  E-value: 1.66e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568908722   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 1.45e-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: 60.58  E-value: 1.45e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568908722   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 3.59e-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: 59.55  E-value: 3.59e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568908722  127 LLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG--KSVIVNK 183
Cdd:cd02325     1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
8-355 2.19e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 45.59  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722    8 IIKDETETMKDLEAEMRDTTRVENLIKSE--NYGKISAEKNEHCIDNNIDlqekiqiQLTQSFEKeekpsKDETDKEKAS 85
Cdd:PTZ00440 2347 GKDKNIELNNENNSYIIKTKEKINNLKEEfsKLLKNIKRNNTLCNNNNIK-------DFISNIGK-----SVETIKQRFS 2414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   86 DKLPRKMLSRDSSQEYTDSTGIdlheflVNTLKNNPRDRMMLLKLEQEI------LDFIGNNESPRKKFPPMTSYHRmll 159
Cdd:PTZ00440 2415 SNLPEKEKLHQIEENLNEIKNI------MNETKRISNVDAFTNKILQDIdneknkENNNMNAEKIDDLIENVTSHNE--- 2485
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722  160 hRVAAYFGLDHNVdqsgKSVIVNKTSNTripDQKFNEHIKDDRGEDFQKRYIL-------KRDNSSFDKDDSQMRI---R 229
Cdd:PTZ00440 2486 -KIKSELLIINDA----LRRVKEKKDEM---NKLFNSLTENNNNNNNSAKNIVdnstyiiNELESHVSKLNELLSYidnE 2557
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722  230 LKD--DRRSKSIEEREEEYQRARDRIFSQDSLCSQENYIIDKRIQDEDTIGT--QQRRQIFRVNKDASG-RSTNSHQSST 304
Cdd:PTZ00440 2558 IKEleNEKLKLLEKAKIEESRKERERIESETQEDNTDEEQINRQQQERLQKEeeQKAYSQERLNREVSGtDDTNKNHNTG 2637
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568908722  305 ENElkyseprpwSSTDSDSSLRNLKPAVTKASS-------FSGISVLTRGDSSGSSKS 355
Cdd:PTZ00440 2638 HDE---------SNYGRYSNKRNDYGQVRLAGGviiglsvFSSIIFISFKEKDEEEKD 2686
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
491-816 5.29e-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: 44.37  E-value: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   491 AASHMFSQPVGPLQSSSQPVQCSPAPYPSPLLPVSPTQQYSVDNLGAQFS-HMSLARQPSADGSDPHaTMFQSTVVLQSP 569
Cdd:pfam03154  162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSpATSQPPNQTQSTAAPH-TLIQQTPTLHPQ 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   570 QqsgyivtTAPPHPPPPPPPPPPPPSLPPGQSVPTASFSASGHPVSQPVLQQQGFLPQPSPQMPacycAPGHYHSSQPQY 649
Cdd:pfam03154  241 R-------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQV 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   650 RPIPSVHHSSHLNQPLPQPaqhtgyqvmPNQQQNYQGivgvQSPQSQSLMGGqPNSTgPHIQgvviPYPSVPSYQVSLPQ 729
Cdd:pfam03154  310 PPGPSPAAPGQSQQRIHTP---------PSQSQLQSQ----QPPREQPLPPA-PLSM-PHIK----PPPTTPIPQLPNPQ 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   730 GSQGIAHQTYQQPVVFPNQ-----------SNQGSLPTTGMPVYYSVIPPGQQSNLSSAvgylQHPGSEQVQfprTTSPC 798
Cdd:pfam03154  371 SHKHPPHLSGPSPFQMNSNlppppalkplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPA----QPPVLTQSQ---SLPPP 443
                          330
                   ....*....|....*...
gi 568908722   799 SSQQLQGHQCAAVPQQPP 816
Cdd:pfam03154  444 AASHPPTSGLHQVPSQSP 461
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
461-855 5.71e-03

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 40.70  E-value: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   461 YNPPMTQQPVRTQVPGPPQPPLPPPPPQQPAASHMFSQPVGPLQSS--SQPVQCSPAPYPSPLLPVSPTQQYSVDNLGAQ 538
Cdd:pfam03157  144 YYPTSPQQPGQWQQPGQGQQGYYPTSPQQSGQRQQPGQGQQLRQGQqgQQSGQGQPGYYPTSSQQPGQLQQTGQGQQGQQ 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   539 FSHMSLARQPSAD------------GSDPHATMFQSTVVLQSPQQSGYIVTTAPPHPPPPPPPPPPPPSLPPGQSVPTAS 606
Cdd:pfam03157  224 PERGQQGQQPGQGqqpgqgqqgqqpGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSGYYPTSQQ 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   607 FSASGHPVSQPVLQQQGFLP----------------QPSPQMPACYCAPGHYHSSQPQYRPIPSVHHSSHLNQPLPQPAQ 670
Cdd:pfam03157  304 QAGQLQQEQQLGQEQQDQQPgqgrqgqqpgqgqqgqQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQP 383
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   671 HTGYQVMPNQQQNYQGIVGVQSPQSQSLMGGQPNSTGPHIQGVVIPYPSVPSYQVSLPQGSQGIAHQTYQ---------- 740
Cdd:pfam03157  384 EQGQQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQpgqgqqpgqg 463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908722   741 QPVVFPNQSNQGSLPTTGMPVYYSVIPpgQQSNLSSAVGYLQHPGSEQVQFPRTTSPCSSQQLQGHQCAAvPQQpPGGGM 820
Cdd:pfam03157  464 QQGQQPGQPEQGQQPGQGQPGYYPTSP--QQSGQGQQLGQWQQQGQGQPGYYPTSPLQPGQGQPGYYPTS-PQQ-PGQGQ 539
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 568908722   821 VMMQLNLPNNPQSRTHSpPQWKQNKHYCDHQRGQK 855
Cdd:pfam03157  540 QLGQLQQPTQGQQGQQS-GQGQQGQQPGQGQQGQQ 573
 
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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