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Conserved domains on  [gi|10835063|ref|NP_002511|]
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nucleophosmin isoform 1 [Homo sapiens]

Protein Classification

Nucleoplasmin and NPM1-C domain-containing protein( domain architecture ID 11140131)

Nucleoplasmin and NPM1-C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nucleoplasmin pfam03066
Nucleoplasmin/nucleophosmin domain; Nucleoplasmins are also known as chromatin decondensation ...
 18-117 1.83e-55

Nucleoplasmin/nucleophosmin domain; Nucleoplasmins are also known as chromatin decondensation proteins. They bind to core histones and transfer DNA to them in a reaction that requires ATP. This is thought to play a role in the assembly of regular nucleosomal arrays.


:

Pssm-ID: 460792  Cd Length: 102  Bit Score: 174.75  E-value: 1.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835063    18 LFGCELKADK-DYHFKVDNDE-NEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEIT 95
Cdd:pfam03066   1 LWGCELKKEKkTVTFDVEEDEdCEHQLSLKTICLGAKAKDELNVVEVEAMNYKKKPIKVPIASLKVSVLPMVSLDGLEPT 80

                          90       100
                  ....*....|....*....|..
gi 10835063    96 PPVVLRLKCGSGPVHISGQHLV 117
Cdd:pfam03066  81 PPVTFRLKSGSGPVHISGQHLV 102
NPM1-C pfam16276
Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly ...
 245-293 7.76e-26

Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly found in Nucleophosmin proteins in mammalia species. Nucleophosmin, a nucleocytoplasmic shuttling protein, is related with cancer and involved in serveral cellluar functions, such as ribosome maturatation and export, centrosome duplication, and response to stress stimuli. This domain has a three-helix bundle which can bind G-quadruplex DNA and the interaction involves helices H1 and H2 of the NPM1-C domain mainly through electrostatic contacts with G-quadruplex phosphates, indicating a crucial role in rescuring its function in leukemia.


:

Pssm-ID: 465081  Cd Length: 49  Bit Score: 96.68  E-value: 7.76e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 10835063   245 EDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKS 293
Cdd:pfam16276   1 EEIKAKMQESVEKGVSLPKVEAKFENFVKNCFKMTDQKVIQDLWQWRQS 49
 
Name Accession Description Interval E-value
Nucleoplasmin pfam03066
Nucleoplasmin/nucleophosmin domain; Nucleoplasmins are also known as chromatin decondensation ...
 18-117 1.83e-55

Nucleoplasmin/nucleophosmin domain; Nucleoplasmins are also known as chromatin decondensation proteins. They bind to core histones and transfer DNA to them in a reaction that requires ATP. This is thought to play a role in the assembly of regular nucleosomal arrays.


Pssm-ID: 460792  Cd Length: 102  Bit Score: 174.75  E-value: 1.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835063    18 LFGCELKADK-DYHFKVDNDE-NEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEIT 95
Cdd:pfam03066   1 LWGCELKKEKkTVTFDVEEDEdCEHQLSLKTICLGAKAKDELNVVEVEAMNYKKKPIKVPIASLKVSVLPMVSLDGLEPT 80

                          90       100
                  ....*....|....*....|..
gi 10835063    96 PPVVLRLKCGSGPVHISGQHLV 117
Cdd:pfam03066  81 PPVTFRLKSGSGPVHISGQHLV 102
NPM1-C pfam16276
Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly ...
 245-293 7.76e-26

Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly found in Nucleophosmin proteins in mammalia species. Nucleophosmin, a nucleocytoplasmic shuttling protein, is related with cancer and involved in serveral cellluar functions, such as ribosome maturatation and export, centrosome duplication, and response to stress stimuli. This domain has a three-helix bundle which can bind G-quadruplex DNA and the interaction involves helices H1 and H2 of the NPM1-C domain mainly through electrostatic contacts with G-quadruplex phosphates, indicating a crucial role in rescuring its function in leukemia.


Pssm-ID: 465081  Cd Length: 49  Bit Score: 96.68  E-value: 7.76e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 10835063   245 EDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKS 293
Cdd:pfam16276   1 EEIKAKMQESVEKGVSLPKVEAKFENFVKNCFKMTDQKVIQDLWQWRQS 49
 
Name Accession Description Interval E-value
Nucleoplasmin pfam03066
Nucleoplasmin/nucleophosmin domain; Nucleoplasmins are also known as chromatin decondensation ...
 18-117 1.83e-55

Nucleoplasmin/nucleophosmin domain; Nucleoplasmins are also known as chromatin decondensation proteins. They bind to core histones and transfer DNA to them in a reaction that requires ATP. This is thought to play a role in the assembly of regular nucleosomal arrays.


Pssm-ID: 460792  Cd Length: 102  Bit Score: 174.75  E-value: 1.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835063    18 LFGCELKADK-DYHFKVDNDE-NEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEIT 95
Cdd:pfam03066   1 LWGCELKKEKkTVTFDVEEDEdCEHQLSLKTICLGAKAKDELNVVEVEAMNYKKKPIKVPIASLKVSVLPMVSLDGLEPT 80

                          90       100
                  ....*....|....*....|..
gi 10835063    96 PPVVLRLKCGSGPVHISGQHLV 117
Cdd:pfam03066  81 PPVTFRLKSGSGPVHISGQHLV 102
NPM1-C pfam16276
Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly ...
 245-293 7.76e-26

Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly found in Nucleophosmin proteins in mammalia species. Nucleophosmin, a nucleocytoplasmic shuttling protein, is related with cancer and involved in serveral cellluar functions, such as ribosome maturatation and export, centrosome duplication, and response to stress stimuli. This domain has a three-helix bundle which can bind G-quadruplex DNA and the interaction involves helices H1 and H2 of the NPM1-C domain mainly through electrostatic contacts with G-quadruplex phosphates, indicating a crucial role in rescuring its function in leukemia.


Pssm-ID: 465081  Cd Length: 49  Bit Score: 96.68  E-value: 7.76e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 10835063   245 EDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKS 293
Cdd:pfam16276   1 EEIKAKMQESVEKGVSLPKVEAKFENFVKNCFKMTDQKVIQDLWQWRQS 49
NPL pfam17800
Nucleoplasmin-like domain;
18-113 7.32e-07

Nucleoplasmin-like domain;


Pssm-ID: 465511  Cd Length: 90  Bit Score: 46.44  E-value: 7.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835063    18 LFGCELKADKDYHFKVDNDenehqLSLRTVSLGAGAKDELHIveaeAMNYEGSPIKVTLATLKMSVQPTVSLGgFEITP- 96
Cdd:pfam17800   1 FWGLEVPPGKPVTLEVPED-----LHITNAALGPSAKPETVV----KVKVDDEEEEFVLCTLTPGKVEQQPLD-LVFSEg 70

                          90
                  ....*....|....*...
gi 10835063    97 -PVVLRLKcGSGPVHISG 113
Cdd:pfam17800  71 eEVTFSVK-GKNTVHLTG 87
 
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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