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Conserved domains on  [gi|294979177|ref|NP_001171094|]
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cAMP-regulated phosphoprotein 21 isoform 7 [Mus musculus]

Protein Classification

R3H_encore_like domain-containing protein( domain architecture ID 10119047)

R3H_encore_like domain-containing protein

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 ...
 162-223 5.71e-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: 96.13  E-value: 5.71e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294979177 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
 
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 ...
 162-223 5.71e-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: 96.13  E-value: 5.71e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294979177 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
146-223 2.04e-11

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 58.47  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294979177   146 IDLHGFLINTLKNNSRDRMILLKMEQEMIDFIAdSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINKT 223
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
 164-222 2.59e-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: 57.50  E-value: 2.59e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294979177  164 MILLKMEQEMIDFIADSNNHYKkFPQMSSYQRMLVHRVAAYFGLDHNV--DQTGKSVIINK 222
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 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 ...
 162-223 5.71e-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: 96.13  E-value: 5.71e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294979177 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
146-223 2.04e-11

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 58.47  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294979177   146 IDLHGFLINTLKNNSRDRMILLKMEQEMIDFIAdSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINKT 223
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
 164-222 2.59e-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: 57.50  E-value: 2.59e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294979177  164 MILLKMEQEMIDFIADSNNHYKkFPQMSSYQRMLVHRVAAYFGLDHNV--DQTGKSVIINK 222
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
 166-222 4.48e-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: 56.85  E-value: 4.48e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 294979177 166 LLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINK 222
Cdd:cd02325    1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
R3H_unknown_2 cd06006
R3H domain of a group of fungal proteins with unknown function. The name of the R3H domain ...
 168-208 1.87e-03

R3H domain of a group of fungal proteins with unknown function. 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: 100076  Cd Length: 59  Bit Score: 35.81  E-value: 1.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 294979177 168 KMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLD 208
Cdd:cd06006    3 QIESTLRKFINDKSKRSLRFPPMRSPQRAFIHELAKDYGLY 43
 
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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