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Conserved domains on  [gi|61806538|ref|NP_001013502|]
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nucleoplasmin-3 [Danio rerio]

Protein Classification

nucleoplasmin-like domain-containing protein( domain architecture ID 10503565)

nucleoplasmin-like domain-containing protein similar to Homo sapiens nucleoplasmin-2 and nucleoplasmin-3

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 ...
24-124 4.50e-44

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: 140.86  E-value: 4.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61806538    24 FSCELSSGVPFYTFQADEDEDVEHFLELRTICLGDGAKEENNVVEVTAMNHQGKKISVPVANLNITCLPMVSLGEFELMA 103
Cdd:pfam03066   2 WGCELKKEKKTVTFDVEEDEDCEHQLSLKTICLGAKAKDELNVVEVEAMNYKKKPIKVPIASLKVSVLPMVSLDGLEPTP 81
                          90       100
                  ....*....|....*....|.
gi 61806538   104 PVTLRLKSGSGPVTISGLHLV 124
Cdd:pfam03066  82 PVTFRLKSGSGPVHISGQHLV 102
 
Name Accession Description Interval E-value
Nucleoplasmin pfam03066
Nucleoplasmin/nucleophosmin domain; Nucleoplasmins are also known as chromatin decondensation ...
24-124 4.50e-44

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: 140.86  E-value: 4.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61806538    24 FSCELSSGVPFYTFQADEDEDVEHFLELRTICLGDGAKEENNVVEVTAMNHQGKKISVPVANLNITCLPMVSLGEFELMA 103
Cdd:pfam03066   2 WGCELKKEKKTVTFDVEEDEDCEHQLSLKTICLGAKAKDELNVVEVEAMNYKKKPIKVPIASLKVSVLPMVSLDGLEPTP 81
                          90       100
                  ....*....|....*....|.
gi 61806538   104 PVTLRLKSGSGPVTISGLHLV 124
Cdd:pfam03066  82 PVTFRLKSGSGPVHISGQHLV 102
 
Name Accession Description Interval E-value
Nucleoplasmin pfam03066
Nucleoplasmin/nucleophosmin domain; Nucleoplasmins are also known as chromatin decondensation ...
24-124 4.50e-44

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: 140.86  E-value: 4.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61806538    24 FSCELSSGVPFYTFQADEDEDVEHFLELRTICLGDGAKEENNVVEVTAMNHQGKKISVPVANLNITCLPMVSLGEFELMA 103
Cdd:pfam03066   2 WGCELKKEKKTVTFDVEEDEDCEHQLSLKTICLGAKAKDELNVVEVEAMNYKKKPIKVPIASLKVSVLPMVSLDGLEPTP 81
                          90       100
                  ....*....|....*....|.
gi 61806538   104 PVTLRLKSGSGPVTISGLHLV 124
Cdd:pfam03066  82 PVTFRLKSGSGPVHISGQHLV 102
 
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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