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Conserved domains on  [gi|50845430|ref|NP_861415|]
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R3H domain-containing protein 1 [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 ...
167-228 1.34e-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: 103.45  E-value: 1.34e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50845430  167 DRMMLLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG-KSVIVNKT 228
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
251-302 2.27e-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: 2.27e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 50845430    251 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 302
Cdd:pfam12752    3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
535-860 1.15e-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: 43.22  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    535 AASHMFSQPVGPLQSSSQPVQCSPAPYPSPLLPVSPTQQYSVDNLGAQFS-HMSLARQPSADGSDPHaTMFQSTVVLQSP 613
Cdd:pfam03154  162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSpATSQPPNQTQSTAAPH-TLIQQTPTLHPQ 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    614 QqsgyivtTAPPHPPPPPPPPPPPPSLPPGQSVPTASFSASGHPVSQPVLQQQGFLPQPSPQMPacycAPGHYHSSQPQY 693
Cdd:pfam03154  241 R-------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQV 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    694 RPIPSVHHSSHLNQPLPQPaqhtgyqvmPNQQQNYQGivgvQSPQSQSLMGGqPNSTgPHIQgvviPYPSVPSYQVSLPQ 773
Cdd:pfam03154  310 PPGPSPAAPGQSQQRIHTP---------PSQSQLQSQ----QPPREQPLPPA-PLSM-PHIK----PPPTTPIPQLPNPQ 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    774 GSQGIAHQTYQQPVVFPNQ-----------SNQGSLPTTGMPVYYSVIPPGQQSNLSSAvgylQHPGSEQVQfprTTSPC 842
Cdd:pfam03154  371 SHKHPPHLSGPSPFQMNSNlppppalkplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPA----QPPVLTQSQ---SLPPP 443
                          330
                   ....*....|....*...
gi 50845430    843 SSQQLQGHQCAAVPQQPP 860
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 ...
167-228 1.34e-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: 103.45  E-value: 1.34e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50845430  167 DRMMLLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG-KSVIVNKT 228
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
151-228 7.13e-18

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 79.27  E-value: 7.13e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430     151 IDLHEFLVNTLKNNPRDRMMLLKLEQEILDFIgNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG--KSVIVNKT 228
Cdd:smart00393    1 ADFLPVTLDALSYRPRRREELIELELEIARFV-KSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
251-302 2.27e-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: 2.27e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 50845430    251 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 302
Cdd:pfam12752    3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
169-227 1.48e-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: 1.48e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50845430    169 MMLLKLEQEILDFIGNNESPrKKFPPMTSYHRMLLHRVAAYFGLDHNV--DQSGKSVIVNK 227
Cdd:pfam01424    1 EFLEQLAEKLAEFVKDTGKS-LELPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
535-860 1.15e-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: 43.22  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    535 AASHMFSQPVGPLQSSSQPVQCSPAPYPSPLLPVSPTQQYSVDNLGAQFS-HMSLARQPSADGSDPHaTMFQSTVVLQSP 613
Cdd:pfam03154  162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSpATSQPPNQTQSTAAPH-TLIQQTPTLHPQ 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    614 QqsgyivtTAPPHPPPPPPPPPPPPSLPPGQSVPTASFSASGHPVSQPVLQQQGFLPQPSPQMPacycAPGHYHSSQPQY 693
Cdd:pfam03154  241 R-------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQV 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    694 RPIPSVHHSSHLNQPLPQPaqhtgyqvmPNQQQNYQGivgvQSPQSQSLMGGqPNSTgPHIQgvviPYPSVPSYQVSLPQ 773
Cdd:pfam03154  310 PPGPSPAAPGQSQQRIHTP---------PSQSQLQSQ----QPPREQPLPPA-PLSM-PHIK----PPPTTPIPQLPNPQ 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    774 GSQGIAHQTYQQPVVFPNQ-----------SNQGSLPTTGMPVYYSVIPPGQQSNLSSAvgylQHPGSEQVQfprTTSPC 842
Cdd:pfam03154  371 SHKHPPHLSGPSPFQMNSNlppppalkplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPA----QPPVLTQSQ---SLPPP 443
                          330
                   ....*....|....*...
gi 50845430    843 SSQQLQGHQCAAVPQQPP 860
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 ...
167-228 1.34e-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: 103.45  E-value: 1.34e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50845430  167 DRMMLLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG-KSVIVNKT 228
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
151-228 7.13e-18

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 79.27  E-value: 7.13e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430     151 IDLHEFLVNTLKNNPRDRMMLLKLEQEILDFIgNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG--KSVIVNKT 228
Cdd:smart00393    1 ADFLPVTLDALSYRPRRREELIELELEIARFV-KSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
251-302 2.27e-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: 2.27e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 50845430    251 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 302
Cdd:pfam12752    3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
169-227 1.48e-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: 1.48e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50845430    169 MMLLKLEQEILDFIGNNESPrKKFPPMTSYHRMLLHRVAAYFGLDHNV--DQSGKSVIVNK 227
Cdd:pfam01424    1 EFLEQLAEKLAEFVKDTGKS-LELPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
171-227 3.66e-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: 3.66e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 50845430  171 LLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG--KSVIVNK 227
Cdd:cd02325    1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
535-860 1.15e-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: 43.22  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    535 AASHMFSQPVGPLQSSSQPVQCSPAPYPSPLLPVSPTQQYSVDNLGAQFS-HMSLARQPSADGSDPHaTMFQSTVVLQSP 613
Cdd:pfam03154  162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSpATSQPPNQTQSTAAPH-TLIQQTPTLHPQ 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    614 QqsgyivtTAPPHPPPPPPPPPPPPSLPPGQSVPTASFSASGHPVSQPVLQQQGFLPQPSPQMPacycAPGHYHSSQPQY 693
Cdd:pfam03154  241 R-------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQV 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    694 RPIPSVHHSSHLNQPLPQPaqhtgyqvmPNQQQNYQGivgvQSPQSQSLMGGqPNSTgPHIQgvviPYPSVPSYQVSLPQ 773
Cdd:pfam03154  310 PPGPSPAAPGQSQQRIHTP---------PSQSQLQSQ----QPPREQPLPPA-PLSM-PHIK----PPPTTPIPQLPNPQ 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845430    774 GSQGIAHQTYQQPVVFPNQ-----------SNQGSLPTTGMPVYYSVIPPGQQSNLSSAvgylQHPGSEQVQfprTTSPC 842
Cdd:pfam03154  371 SHKHPPHLSGPSPFQMNSNlppppalkplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPA----QPPVLTQSQ---SLPPP 443
                          330
                   ....*....|....*...
gi 50845430    843 SSQQLQGHQCAAVPQQPP 860
Cdd:pfam03154  444 AASHPPTSGLHQVPSQSP 461
 
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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