nucleophosmin isoform 4 [Homo sapiens]
NPL and NPM1-C domain-containing protein( domain architecture ID 10925240)
NPL and NPM1-C domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||
NPL super family | cl03870 | Nucleoplasmin-like domain; |
1-53 | 1.93e-27 | ||
Nucleoplasmin-like domain; The actual alignment was detected with superfamily member pfam03066: Pssm-ID: 470892 Cd Length: 102 Bit Score: 100.80 E-value: 1.93e-27
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NPM1-C | pfam16276 | Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly ... |
181-229 | 5.89e-25 | ||
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: 92.82 E-value: 5.89e-25
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Name | Accession | Description | Interval | E-value | ||
Nucleoplasmin | pfam03066 | Nucleoplasmin/nucleophosmin domain; Nucleoplasmins are also known as chromatin decondensation ... |
1-53 | 1.93e-27 | ||
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: 100.80 E-value: 1.93e-27
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NPM1-C | pfam16276 | Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly ... |
181-229 | 5.89e-25 | ||
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: 92.82 E-value: 5.89e-25
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Name | Accession | Description | Interval | E-value | ||
Nucleoplasmin | pfam03066 | Nucleoplasmin/nucleophosmin domain; Nucleoplasmins are also known as chromatin decondensation ... |
1-53 | 1.93e-27 | ||
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: 100.80 E-value: 1.93e-27
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NPM1-C | pfam16276 | Nucleophosmin C-terminal domain; This domain, approximately 50 residues in length, is mainly ... |
181-229 | 5.89e-25 | ||
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: 92.82 E-value: 5.89e-25
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Blast search parameters | ||||
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