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Conserved domains on  [gi|37925570|gb|AAP68443|]
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histone H4, partial [Halteria grandinella]

Protein Classification

histone H4( domain architecture ID 19223581)

histone H4 is one of the four histones, along with H2A, H2B and H3, that form the eukaryotic nucleosome core; along with H3, it plays a central role in nucleosome formation

CATH:  1.10.20.10
Gene Ontology:  GO:0006334|GO:0006355|GO:0006325|GO:0046982|GO:0003677
PubMed:  32556547

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HFD_H4 cd22912
histone-fold domain found in histone H4 and similar proteins; Histone H4 is a core component ...
 1-50 1.17e-23

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: 83.42  E-value: 1.17e-23
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|
gi 37925570  1 RRLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVTSL 50
Cdd:cd22912 15 RRLARRGGVKRISGDIYEEVRGVLKDFLENVIRDAVTYTEHAKRKTVTAM 64
 
Name Accession Description Interval E-value
HFD_H4 cd22912
histone-fold domain found in histone H4 and similar proteins; Histone H4 is a core component ...
 1-50 1.17e-23

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: 83.42  E-value: 1.17e-23
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|
gi 37925570  1 RRLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVTSL 50
Cdd:cd22912 15 RRLARRGGVKRISGDIYEEVRGVLKDFLENVIRDAVTYTEHAKRKTVTAM 64
PTZ00015 PTZ00015
histone H4; Provisional
 1-50 3.30e-21

histone H4; Provisional


Pssm-ID: 185397  Cd Length: 102  Bit Score: 78.24  E-value: 3.30e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37925570    1 RRLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVTSL 50
Cdd:PTZ00015  37 RRLARRGGVKRISGDIYEEVRGVLKAFLENVVRDSTAYTEYARRKTVTAM 86
H4 smart00417
Histone H4;
1-50 4.72e-18

Histone H4;


Pssm-ID: 128694  Cd Length: 74  Bit Score: 69.49  E-value: 4.72e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 37925570     1 RRLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVTSL 50
Cdd:smart00417 20 RRLARRGGVKRISGLIYDETRNVLKSFLENVVRDAVTYTEHARRKTVTAM 69
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
2-48 5.88e-04

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 441639  Cd Length: 67  Bit Score: 33.27  E-value: 5.88e-04
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*..
gi 37925570  2 RLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVT 48
Cdd:COG2036  9 RIIKKAGAERVSEDAVEALAEILEEYAEEIAKEAVELAKHAGRKTVK 55
 
Name Accession Description Interval E-value
HFD_H4 cd22912
histone-fold domain found in histone H4 and similar proteins; Histone H4 is a core component ...
 1-50 1.17e-23

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: 83.42  E-value: 1.17e-23
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|
gi 37925570  1 RRLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVTSL 50
Cdd:cd22912 15 RRLARRGGVKRISGDIYEEVRGVLKDFLENVIRDAVTYTEHAKRKTVTAM 64
PTZ00015 PTZ00015
histone H4; Provisional
 1-50 3.30e-21

histone H4; Provisional


Pssm-ID: 185397  Cd Length: 102  Bit Score: 78.24  E-value: 3.30e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37925570    1 RRLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVTSL 50
Cdd:PTZ00015  37 RRLARRGGVKRISGDIYEEVRGVLKAFLENVVRDSTAYTEYARRKTVTAM 86
PLN00035 PLN00035
histone H4; Provisional
 1-50 1.43e-19

histone H4; Provisional


Pssm-ID: 177669 [Multi-domain]  Cd Length: 103  Bit Score: 74.10  E-value: 1.43e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37925570    1 RRLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVTSL 50
Cdd:PLN00035  36 RRLARRGGVKRISGLIYEETRGVLKIFLENVIRDAVTYTEHARRKTVTAM 85
H4 smart00417
Histone H4;
1-50 4.72e-18

Histone H4;


Pssm-ID: 128694  Cd Length: 74  Bit Score: 69.49  E-value: 4.72e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 37925570     1 RRLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVTSL 50
Cdd:smart00417 20 RRLARRGGVKRISGLIYDETRNVLKSFLENVVRDAVTYTEHARRKTVTAM 69
PLN00163 PLN00163
histone H4; Provisional
 3-24 5.16e-06

histone H4; Provisional


Pssm-ID: 165730  Cd Length: 59  Bit Score: 38.52  E-value: 5.16e-06
                        10        20
                ....*....|....*....|..
gi 37925570   3 LARRGGVKRISALIYEEARGVL 24
Cdd:PLN00163 38 LARRGGVKRISGLIYEETRTVL 59
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 1-48 7.68e-05

histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription regulators and similar proteins; The family includes many archaeal histone-fold proteins and histone-like transcription regulators, which may bind and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. They can increase the resistance of DNA to thermal denaturation.


Pssm-ID: 467034  Cd Length: 64  Bit Score: 35.60  E-value: 7.68e-05
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*...
gi 37925570  1 RRLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVT 48
Cdd:cd22909  8 KRIIKKAGAERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVK 55
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
2-48 5.88e-04

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 441639  Cd Length: 67  Bit Score: 33.27  E-value: 5.88e-04
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*..
gi 37925570  2 RLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVT 48
Cdd:COG2036  9 RIIKKAGAERVSEDAVEALAEILEEYAEEIAKEAVELAKHAGRKTVK 55
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 1-48 2.46e-03

histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also called interphase centromere complex protein 22 (ICEN22), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression, and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENP-T is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Moreover, CENP-T is a component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENP-T has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


Pssm-ID: 467045  Cd Length: 94  Bit Score: 32.14  E-value: 2.46e-03
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*...
gi 37925570  1 RRLARRGGVKRISALIYEEARGVLKGFLETVIKDSVTYCEHSKRKTVT 48
Cdd:cd22920  9 KKLFKHFLKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTIN 56
 
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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