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Conserved domains on  [gi|41406069|ref|NP_958924|]
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histone H2A.V isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00154 super family cl30550
histone H2A; Provisional
 6-66 2.06e-24

histone H2A; Provisional


The actual alignment was detected with superfamily member PLN00154:

Pssm-ID: 177756  Cd Length: 136  Bit Score: 88.08  E-value: 2.06e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41406069    6 AGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEV 66
Cdd:PLN00154  17 AAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEV 77
 
Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
 6-66 2.06e-24

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 88.08  E-value: 2.06e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41406069    6 AGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEV 66
Cdd:PLN00154  17 AAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEV 77
H2A smart00414
Histone 2A;
19-66 4.13e-24

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 86.23  E-value: 4.13e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 41406069     19 SRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEV 66
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEV 47
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 18-66 7.64e-22

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: 79.88  E-value: 7.64e-22
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*....
gi 41406069 18 VSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEV 66
Cdd:cd00074  1 QSRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEI 48
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
1-66 2.35e-15

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 64.88  E-value: 2.35e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41406069   1 MAGGKAGKDSGKAKAKavSRSQRAGLQFPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEV 66
Cdd:COG5262   2 VSGGKGGKAADARVSQ--SRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEI 64
Histone pfam00125
Core histone H2A/H2B/H3/H4;
5-66 3.43e-05

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 38.57  E-value: 3.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41406069     5 KAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEV 66
Cdd:pfam00125  37 RPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVEL 98
 
Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
 6-66 2.06e-24

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 88.08  E-value: 2.06e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41406069    6 AGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEV 66
Cdd:PLN00154  17 AAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEV 77
H2A smart00414
Histone 2A;
19-66 4.13e-24

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 86.23  E-value: 4.13e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 41406069     19 SRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEV 66
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEV 47
PTZ00017 PTZ00017
histone H2A; Provisional
 3-66 4.35e-23

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 84.41  E-value: 4.35e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41406069    3 GGKAGKDSGK-AKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEV 66
Cdd:PTZ00017   2 GGKGKTGGGKaGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEV 65
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 18-66 7.64e-22

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: 79.88  E-value: 7.64e-22
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*....
gi 41406069 18 VSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEV 66
Cdd:cd00074  1 QSRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEI 48
PLN00157 PLN00157
histone H2A; Provisional
 3-66 6.38e-16

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 66.41  E-value: 6.38e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41406069    3 GGKAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEV 66
Cdd:PLN00157   2 SGRGKRKGGGGGKKATSRSAKAGLQFPVGRIARYLKAGKYAT-RVGAGAPVYLAAVLEYLAAEV 64
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
1-66 2.35e-15

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 64.88  E-value: 2.35e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41406069   1 MAGGKAGKDSGKAKAKavSRSQRAGLQFPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEV 66
Cdd:COG5262   2 VSGGKGGKAADARVSQ--SRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEI 64
PLN00156 PLN00156
histone H2AX; Provisional
 1-66 1.66e-14

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 62.68  E-value: 1.66e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41406069    1 MAGGKAGKDSGKAKA-KAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEV 66
Cdd:PLN00156   2 AGSGTTKGGRGKPKAtKSVSRSSKAGLQFPVGRIARFLKAGKYAE-RVGAGAPVYLSAVLEYLAAEV 67
PLN00153 PLN00153
histone H2A; Provisional
 1-66 6.19e-13

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 58.58  E-value: 6.19e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41406069    1 MAGGKAGKDSGKakaKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEV 66
Cdd:PLN00153   1 MAGRGKGKTSGK---KAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYLTAEV 62
PLN00155 PLN00155
histone H2A; Provisional
 1-62 3.91e-10

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 49.71  E-value: 3.91e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41406069   1 MAGGKAGKDSGKakaKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYL 62
Cdd:PLN00155  1 MAGRGKGKTSGK---KAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYL 58
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 18-66 4.72e-09

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: 48.06  E-value: 4.72e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41406069  18 VSRSQRAGLQFPVGRIHRHL-KTRTTShgRVGATAAVYSAAILEYLTAEV 66
Cdd:cd22913   9 RSKSARCGLTFSVGRFHRWMvDSRLAK--RIHEHAAVYLTACMENLLEEI 56
PTZ00252 PTZ00252
histone H2A; Provisional
 12-66 9.72e-08

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 45.34  E-value: 9.72e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41406069   12 KAKAKAVSRSQRAGLQFPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEV 66
Cdd:PTZ00252  10 KASKSGSGRSAKAGLIFPVGRVGSLLR-RGQYARRIGASGAVYMAAVLEYLTAEL 63
Histone pfam00125
Core histone H2A/H2B/H3/H4;
5-66 3.43e-05

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 38.57  E-value: 3.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41406069     5 KAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEV 66
Cdd:pfam00125  37 RPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVEL 98
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 28-66 4.01e-04

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: 34.52  E-value: 4.01e-04
                       10        20        30
               ....*....|....*....|....*....|....*....
gi 41406069 28 FPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEV 66
Cdd:cd22915  2 FPVDKIHPLLK-KDLLVYKVDPQVSLYLVAVLEYIAADI 39
 
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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