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Conserved domains on  [gi|20357599|ref|NP_619541|]
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histone H2A.V isoform 2 [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
 6-108 5.85e-55

histone H2A; Provisional


The actual alignment was detected with superfamily member PLN00154:

Pssm-ID: 177756  Cd Length: 136  Bit Score: 167.43  E-value: 5.85e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599    6 AGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPR 85
Cdd:PLN00154  17 AAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPR 96

                         90       100
                 ....*....|....*....|...
gi 20357599   86 HLQLAIRGDEELDSLIKATIAGG 108
Cdd:PLN00154  97 HLQLAIRGDEELDTLIKGTIAGG 119
 
Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
 6-108 5.85e-55

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 167.43  E-value: 5.85e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599    6 AGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPR 85
Cdd:PLN00154  17 AAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPR 96

                         90       100
                 ....*....|....*....|...
gi 20357599   86 HLQLAIRGDEELDSLIKATIAGG 108
Cdd:PLN00154  97 HLQLAIRGDEELDTLIKGTIAGG 119
H2A smart00414
Histone 2A;
19-108 4.31e-49

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 151.72  E-value: 4.31e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599     19 SRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 98
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90
                   ....*....|.
gi 20357599     99 SLIKA-TIAGG 108
Cdd:smart00414  80 KLLKGvTIAQG 90
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 18-105 1.77e-45

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: 141.90  E-value: 1.77e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599  18 VSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 97
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEEL 79


                ....*...
gi 20357599  98 DSLIKATI 105
Cdd:cd00074  80 NKLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
1-108 7.42e-39

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 126.52  E-value: 7.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599   1 MAGGKAGKDSGKAKAKavSRSQRAGLQFPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVK 80
Cdd:COG5262   2 VSGGKGGKAADARVSQ--SRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKK 78

                        90       100
                ....*....|....*....|....*....
gi 20357599  81 RITPRHLQLAIRGDEELDSLIK-ATIAGG 108
Cdd:COG5262  79 RIIPRHLQLAIRNDEELNKLLGdVTIAQG 107
Histone pfam00125
Core histone H2A/H2B/H3/H4;
5-94 6.37e-17

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 70.54  E-value: 6.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599     5 KAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITP 84
Cdd:pfam00125  37 RPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTP 116

                          90
                  ....*....|
gi 20357599    85 RHLQLAIRGD 94
Cdd:pfam00125 117 KDIQLARRLR 126
 
Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
 6-108 5.85e-55

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 167.43  E-value: 5.85e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599    6 AGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPR 85
Cdd:PLN00154  17 AAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPR 96

                         90       100
                 ....*....|....*....|...
gi 20357599   86 HLQLAIRGDEELDSLIKATIAGG 108
Cdd:PLN00154  97 HLQLAIRGDEELDTLIKGTIAGG 119
PTZ00017 PTZ00017
histone H2A; Provisional
 3-108 9.03e-53

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 161.84  E-value: 9.03e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599    3 GGKAGKDSGK-AKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKR 81
Cdd:PTZ00017   2 GGKGKTGGGKaGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80

                         90       100
                 ....*....|....*....|....*...
gi 20357599   82 ITPRHLQLAIRGDEELDSLI-KATIAGG 108
Cdd:PTZ00017  81 ITPRHIQLAIRNDEELNKLLaGVTIASG 108
H2A smart00414
Histone 2A;
19-108 4.31e-49

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 151.72  E-value: 4.31e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599     19 SRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 98
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90
                   ....*....|.
gi 20357599     99 SLIKA-TIAGG 108
Cdd:smart00414  80 KLLKGvTIAQG 90
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 18-105 1.77e-45

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: 141.90  E-value: 1.77e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599  18 VSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 97
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEEL 79


                ....*...
gi 20357599  98 DSLIKATI 105
Cdd:cd00074  80 NKLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
1-108 7.42e-39

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 126.52  E-value: 7.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599   1 MAGGKAGKDSGKAKAKavSRSQRAGLQFPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVK 80
Cdd:COG5262   2 VSGGKGGKAADARVSQ--SRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKK 78

                        90       100
                ....*....|....*....|....*....
gi 20357599  81 RITPRHLQLAIRGDEELDSLIK-ATIAGG 108
Cdd:COG5262  79 RIIPRHLQLAIRNDEELNKLLGdVTIAQG 107
PLN00157 PLN00157
histone H2A; Provisional
 3-108 1.73e-35

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 118.03  E-value: 1.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599    3 GGKAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRI 82
Cdd:PLN00157   2 SGRGKRKGGGGGKKATSRSAKAGLQFPVGRIARYLKAGKYAT-RVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRI 80

                         90       100
                 ....*....|....*....|....*..
gi 20357599   83 TPRHLQLAIRGDEELDSLIK-ATIAGG 108
Cdd:PLN00157  81 VPRHIQLAVRNDEELSKLLGgVTIAAG 107
PLN00156 PLN00156
histone H2AX; Provisional
 1-108 2.78e-33

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 112.75  E-value: 2.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599    1 MAGGKAGKDSGKAKA-KAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKV 79
Cdd:PLN00156   2 AGSGTTKGGRGKPKAtKSVSRSSKAGLQFPVGRIARFLKAGKYAE-RVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKK 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 20357599   80 KRITPRHLQLAIRGDEELDSLIKA-TIAGG 108
Cdd:PLN00156  81 NRIVPRHIQLAVRNDEELSKLLGSvTIAAG 110
PLN00153 PLN00153
histone H2A; Provisional
 1-108 1.29e-29

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 103.26  E-value: 1.29e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599    1 MAGGKAGKDSGKakaKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVK 80
Cdd:PLN00153   1 MAGRGKGKTSGK---KAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKN 76

                         90       100
                 ....*....|....*....|....*....
gi 20357599   81 RITPRHLQLAIRGDEELDSLI-KATIAGG 108
Cdd:PLN00153  77 RIVPRHIQLAIRNDEELGKLLgEVTIASG 105
PTZ00252 PTZ00252
histone H2A; Provisional
 12-102 4.48e-17

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 71.15  E-value: 4.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599   12 KAKAKAVSRSQRAGLQFPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNAS--KDLKVKRITPRHLQL 89
Cdd:PTZ00252  10 KASKSGSGRSAKAGLIFPVGRVGSLLR-RGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAaqQAKKPKRLTPRTVTL 88

                         90
                 ....*....|...
gi 20357599   90 AIRGDEELDSLIK 102
Cdd:PTZ00252  89 AVRHDDDLGSLLK 101
Histone pfam00125
Core histone H2A/H2B/H3/H4;
5-94 6.37e-17

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 70.54  E-value: 6.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599     5 KAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITP 84
Cdd:pfam00125  37 RPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTP 116

                          90
                  ....*....|
gi 20357599    85 RHLQLAIRGD 94
Cdd:pfam00125 117 KDIQLARRLR 126
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 28-100 1.98e-12

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: 57.63  E-value: 1.98e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20357599  28 FPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSL 100
Cdd:cd22915   2 FPVDKIHPLLK-KDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDL 73
PLN00155 PLN00155
histone H2A; Provisional
 1-62 7.08e-12

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 55.87  E-value: 7.08e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20357599    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) ...
 18-97 6.12e-11

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: 54.61  E-value: 6.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20357599  18 VSRSQRAGLQFPVGRIHRHL-KTRTTShgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEE 96
Cdd:cd22913   9 RSKSARCGLTFSVGRFHRWMvDSRLAK--RIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAE 86


                .
gi 20357599  97 L 97
Cdd:cd22913  87 L 87
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
27-100 1.18e-05

Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];


Pssm-ID: 227572  Cd Length: 113  Bit Score: 41.10  E-value: 1.18e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20357599  27 QFPVGRIHRHLKTrTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSL 100
Cdd:COG5247  23 RFPIARLKKIMQL-DEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
 
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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