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Conserved domains on  [gi|568908720|ref|XP_006529482|]
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R3H domain-containing protein 1 isoform X3 [Mus musculus]

Protein Classification

R3H and SUZ domain-containing protein( domain architecture ID 10119061)

R3H and SUZ domain-containing protein may bind single-stranded nucleic acids through its R3H domain and RNA through its SUZ domain, similar to Zea mays DBF1-interactor protein 1 that is a potential regulator of DBF1 activity in stress responses

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 1.77e-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: 1.77e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568908720  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 2.45e-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: 2.45e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568908720   251 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 302
Cdd:pfam12752    3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
 
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 1.77e-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: 1.77e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568908720  167 DRMMLLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG-KSVIVNKT 228
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
151-228 9.63e-18

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 78.88  E-value: 9.63e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908720    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 2.45e-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: 2.45e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568908720   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 1.66e-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: 60.20  E-value: 1.66e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568908720   169 MMLLKLEQEILDFIGNNESPrKKFPPMTSYHRMLLHRVAAYFGLDHNV--DQSGKSVIVNK 227
Cdd:pfam01424    1 EFLEQLAEKLAEFVKDTGKS-LELPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
 
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 1.77e-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: 1.77e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568908720  167 DRMMLLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG-KSVIVNKT 228
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
151-228 9.63e-18

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 78.88  E-value: 9.63e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908720    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 2.45e-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: 2.45e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568908720   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 1.66e-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: 60.20  E-value: 1.66e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568908720   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 4.28e-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: 59.16  E-value: 4.28e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568908720  171 LLKLEQEILDFIGNNESPRKKFPPMTSYHRMLLHRVAAYFGLDHNVDQSG--KSVIVNK 227
Cdd:cd02325     1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
 
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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