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Conserved domains on  [gi|63029935|ref|NP_542451|]
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histone H2A-Bbd type 2/3 [Homo sapiens]

Protein Classification

histone H2A family protein( domain architecture ID 12210400)

histone H2A family protein similar to histone 2A (H2A) that is a core component of nucleosome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
H2A smart00414
Histone 2A;
21-113 1.40e-44

Histone 2A;


:

Pssm-ID: 197711  Cd Length: 106  Bit Score: 140.16  E-value: 1.40e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935     21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLST 100
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90
                   ....*....|....*
gi 63029935    101 LFNTTTISQ--VAPG 113
Cdd:smart00414  81 LLKGVTIAQggVLPN 95
 
Name Accession Description Interval E-value
H2A smart00414
Histone 2A;
21-113 1.40e-44

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 140.16  E-value: 1.40e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935     21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLST 100
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90
                   ....*....|....*
gi 63029935    101 LFNTTTISQ--VAPG 113
Cdd:smart00414  81 LLKGVTIAQggVLPN 95
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 20-108 1.01e-37

histone-fold domain found in histone H2A and similar proteins; Histone H2A is the 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 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: 467020  Cd Length: 89  Bit Score: 122.26  E-value: 1.01e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935  20 CSRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLS 99
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*....
gi 63029935 100 TLFNTTTIS 108
Cdd:cd00074  81 KLFKGVTIA 89
PTZ00017 PTZ00017
histone H2A; Provisional
 21-109 1.35e-28

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 100.59  E-value: 1.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935   21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLST 100
Cdd:PTZ00017  19 SRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEELNK 98


                 ....*....
gi 63029935  101 LFNTTTISQ 109
Cdd:PTZ00017  99 LLAGVTIAS 107
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
21-109 7.05e-25

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 91.08  E-value: 7.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935  21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLST 100
Cdd:COG5262  18 SRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELNK 97


                ....*....
gi 63029935 101 LFNTTTISQ 109
Cdd:COG5262  98 LLGDVTIAQ 106
 
Name Accession Description Interval E-value
H2A smart00414
Histone 2A;
21-113 1.40e-44

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 140.16  E-value: 1.40e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935     21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLST 100
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90
                   ....*....|....*
gi 63029935    101 LFNTTTISQ--VAPG 113
Cdd:smart00414  81 LLKGVTIAQggVLPN 95
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 20-108 1.01e-37

histone-fold domain found in histone H2A and similar proteins; Histone H2A is the 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 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: 467020  Cd Length: 89  Bit Score: 122.26  E-value: 1.01e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935  20 CSRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLS 99
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*....
gi 63029935 100 TLFNTTTIS 108
Cdd:cd00074  81 KLFKGVTIA 89
PTZ00017 PTZ00017
histone H2A; Provisional
 21-109 1.35e-28

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 100.59  E-value: 1.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935   21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLST 100
Cdd:PTZ00017  19 SRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEELNK 98


                 ....*....
gi 63029935  101 LFNTTTISQ 109
Cdd:PTZ00017  99 LLAGVTIAS 107
PLN00157 PLN00157
histone H2A; Provisional
 21-108 1.18e-25

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 92.99  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935   21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLST 100
Cdd:PLN00157  18 SRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVRNDEELSK 97


                 ....*...
gi 63029935  101 LFNTTTIS 108
Cdd:PLN00157  98 LLGGVTIA 105
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
21-109 7.05e-25

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 91.08  E-value: 7.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935  21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLST 100
Cdd:COG5262  18 SRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELNK 97


                ....*....
gi 63029935 101 LFNTTTISQ 109
Cdd:COG5262  98 LLGDVTIAQ 106
PLN00156 PLN00156
histone H2AX; Provisional
 21-108 6.15e-24

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 88.87  E-value: 6.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935   21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLST 100
Cdd:PLN00156  21 SRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHIQLAVRNDEELSK 100


                 ....*...
gi 63029935  101 LFNTTTIS 108
Cdd:PLN00156 101 LLGSVTIA 108
PLN00153 PLN00153
histone H2A; Provisional
 21-108 1.05e-22

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 85.54  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935   21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLST 100
Cdd:PLN00153  16 SRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVPRHIQLAIRNDEELGK 95


                 ....*...
gi 63029935  101 LFNTTTIS 108
Cdd:PLN00153  96 LLGEVTIA 103
PLN00154 PLN00154
histone H2A; Provisional
 21-105 1.67e-17

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 72.28  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935   21 SRTVRAELSFSVSQVERSLREGHYA-QRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLS 99
Cdd:PLN00154  30 SRSSRAGLQFPVGRIHRQLKQRVSAhGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 109


                 ....*.
gi 63029935  100 TLFNTT 105
Cdd:PLN00154 110 TLIKGT 115
PTZ00252 PTZ00252
histone H2A; Provisional
 21-109 3.79e-16

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 68.84  E-value: 3.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63029935   21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGER--NITPLLLDMVVHNDRLL 98
Cdd:PTZ00252  17 GRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQAKKpkRLTPRTVTLAVRHDDDL 96

                         90
                 ....*....|.
gi 63029935   99 STLFNTTTISQ 109
Cdd:PTZ00252  97 GSLLKNVTLSR 107
PLN00155 PLN00155
histone H2A; Provisional
 21-63 1.29e-10

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 52.79  E-value: 1.29e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 63029935   21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYL 63
Cdd:PLN00155  16 SRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 29-103 2.60e-10

second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; SOS-1 is a guanine nucleotide exchange factor for Ras that binds to GRB2. It promotes the exchange of Ras-bound GDP by GTP. It is a catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac, by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. SOS-1 contains tandem histone folds at the N-terminal region. The model corresponds to the second repeat.


Pssm-ID: 467040  Cd Length: 75  Bit Score: 52.24  E-value: 2.60e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63029935  29 SFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLSTLFN 103
Cdd:cd22915   1 LFPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 21-95 5.55e-08

histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins; ABTB2, also called Bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, which has implications for Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homolog (PTEN). This subfamily also includes BTB/POZ domain-containing protein 11 (BTBD11), also called ankyrin repeat and BTB/POZ domain-containing protein BTBD11. It is a BTB-domain-containing Kelch-like protein with unknown function.


Pssm-ID: 467038  Cd Length: 105  Bit Score: 46.91  E-value: 5.55e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63029935  21 SRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHND 95
Cdd:cd22913  10 SKSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINND 84
 
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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