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Conserved domains on  [gi|37925546|gb|AAP68431|]
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histone H4, partial [Bursaria truncatella]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00015 super family cl29688
histone H4; Provisional
 1-40 2.77e-17

histone H4; Provisional


The actual alignment was detected with superfamily member PTZ00015:

Pssm-ID: 185397  Cd Length: 102  Bit Score: 67.84  E-value: 2.77e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 37925546    1 RRLARRGGVKRISTFIYDDTRAVLKSFLENVVRDATTYTE 40
Cdd:PTZ00015  37 RRLARRGGVKRISGDIYEEVRGVLKAFLENVVRDSTAYTE 76
 
Name Accession Description Interval E-value
PTZ00015 PTZ00015
histone H4; Provisional
 1-40 2.77e-17

histone H4; Provisional


Pssm-ID: 185397  Cd Length: 102  Bit Score: 67.84  E-value: 2.77e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 37925546    1 RRLARRGGVKRISTFIYDDTRAVLKSFLENVVRDATTYTE 40
Cdd:PTZ00015  37 RRLARRGGVKRISGDIYEEVRGVLKAFLENVVRDSTAYTE 76
HFD_H4 cd22912
histone-fold domain found in histone H4 and similar proteins; Histone H4 is a core component ...
 1-40 7.18e-16

histone-fold domain found in histone H4 and similar proteins; Histone H4 is a core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication, and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called the histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.


Pssm-ID: 467037 [Multi-domain]  Cd Length: 79  Bit Score: 63.39  E-value: 7.18e-16
                       10        20        30        40
               ....*....|....*....|....*....|....*....|
gi 37925546  1 RRLARRGGVKRISTFIYDDTRAVLKSFLENVVRDATTYTE 40
Cdd:cd22912 15 RRLARRGGVKRISGDIYEEVRGVLKDFLENVIRDAVTYTE 54
H4 smart00417
Histone H4;
1-40 3.16e-15

Histone H4;


Pssm-ID: 128694  Cd Length: 74  Bit Score: 61.79  E-value: 3.16e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 37925546     1 RRLARRGGVKRISTFIYDDTRAVLKSFLENVVRDATTYTE 40
Cdd:smart00417 20 RRLARRGGVKRISGLIYDETRNVLKSFLENVVRDAVTYTE 59
 
Name Accession Description Interval E-value
PTZ00015 PTZ00015
histone H4; Provisional
 1-40 2.77e-17

histone H4; Provisional


Pssm-ID: 185397  Cd Length: 102  Bit Score: 67.84  E-value: 2.77e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 37925546    1 RRLARRGGVKRISTFIYDDTRAVLKSFLENVVRDATTYTE 40
Cdd:PTZ00015  37 RRLARRGGVKRISGDIYEEVRGVLKAFLENVVRDSTAYTE 76
HFD_H4 cd22912
histone-fold domain found in histone H4 and similar proteins; Histone H4 is a core component ...
 1-40 7.18e-16

histone-fold domain found in histone H4 and similar proteins; Histone H4 is a core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication, and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called the histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.


Pssm-ID: 467037 [Multi-domain]  Cd Length: 79  Bit Score: 63.39  E-value: 7.18e-16
                       10        20        30        40
               ....*....|....*....|....*....|....*....|
gi 37925546  1 RRLARRGGVKRISTFIYDDTRAVLKSFLENVVRDATTYTE 40
Cdd:cd22912 15 RRLARRGGVKRISGDIYEEVRGVLKDFLENVIRDAVTYTE 54
H4 smart00417
Histone H4;
1-40 3.16e-15

Histone H4;


Pssm-ID: 128694  Cd Length: 74  Bit Score: 61.79  E-value: 3.16e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 37925546     1 RRLARRGGVKRISTFIYDDTRAVLKSFLENVVRDATTYTE 40
Cdd:smart00417 20 RRLARRGGVKRISGLIYDETRNVLKSFLENVVRDAVTYTE 59
PLN00035 PLN00035
histone H4; Provisional
 1-40 1.16e-14

histone H4; Provisional


Pssm-ID: 177669 [Multi-domain]  Cd Length: 103  Bit Score: 61.00  E-value: 1.16e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 37925546    1 RRLARRGGVKRISTFIYDDTRAVLKSFLENVVRDATTYTE 40
Cdd:PLN00035  36 RRLARRGGVKRISGLIYEETRGVLKIFLENVIRDAVTYTE 75
 
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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