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Conserved domains on  [gi|1239469436|ref|NP_001341939|]
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nucleophosmin isoform 6 [Homo sapiens]

Protein Classification

NPM1-C domain-containing protein( domain architecture ID 11242140)

NPM1-C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NPM1-C pfam16276
Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly ...
 118-166 5.62e-24

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: 88.20  E-value: 5.62e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1239469436 118 EDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKS 166
Cdd:pfam16276   1 EEIKAKMQESVEKGVSLPKVEAKFENFVKNCFKMTDQKVIQDLWQWRQS 49
 
Name Accession Description Interval E-value
NPM1-C pfam16276
Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly ...
 118-166 5.62e-24

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: 88.20  E-value: 5.62e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1239469436 118 EDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKS 166
Cdd:pfam16276   1 EEIKAKMQESVEKGVSLPKVEAKFENFVKNCFKMTDQKVIQDLWQWRQS 49
 
Name Accession Description Interval E-value
NPM1-C pfam16276
Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly ...
 118-166 5.62e-24

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: 88.20  E-value: 5.62e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1239469436 118 EDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKS 166
Cdd:pfam16276   1 EEIKAKMQESVEKGVSLPKVEAKFENFVKNCFKMTDQKVIQDLWQWRQS 49
 
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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