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Conserved domains on  [gi|41406067|ref|NP_958844|]
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histone H2A.V isoform 3 [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
 2-95 1.22e-58

histone H2A; Provisional


The actual alignment was detected with superfamily member PLN00154:

Pssm-ID: 177756  Cd Length: 136  Bit Score: 176.29  E-value: 1.22e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067    2 FPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAG 81
Cdd:PLN00154  39 FPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAG 118

                         90
                 ....*....|....
gi 41406067   82 GGVIPHIHKSLIGK 95
Cdd:PLN00154 119 GGVIPHIHKSLINK 132
 
Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
 2-95 1.22e-58

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 176.29  E-value: 1.22e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067    2 FPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAG 81
Cdd:PLN00154  39 FPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAG 118

                         90
                 ....*....|....
gi 41406067   82 GGVIPHIHKSLIGK 95
Cdd:PLN00154 119 GGVIPHIHKSLINK 132
H2A smart00414
Histone 2A;
2-98 7.95e-53

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 160.58  E-value: 7.95e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067      2 FPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKA-TIA 80
Cdd:smart00414  10 FPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNKLLKGvTIA 88

                           90
                   ....*....|....*...
gi 41406067     81 GGGVIPHIHKSLIGKKGQ 98
Cdd:smart00414  89 QGGVLPNIHKVLLPKKTG 106
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 2-79 2.89e-40

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: 128.03  E-value: 2.89e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41406067   2 FPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATI 79
Cdd:cd00074  11 FPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELNKLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
2-96 1.95e-39

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 127.67  E-value: 1.95e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067   2 FPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIK-ATIA 80
Cdd:COG5262  27 FPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELNKLLGdVTIA 105

                        90
                ....*....|....*.
gi 41406067  81 GGGVIPHIHKSLIGKK 96
Cdd:COG5262 106 QGGVLPNINPGLLPKS 121
Histone pfam00125
Core histone H2A/H2B/H3/H4;
1-68 4.30e-17

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 70.54  E-value: 4.30e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41406067     1 MFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGD 68
Cdd:pfam00125  59 KLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
 
Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
 2-95 1.22e-58

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 176.29  E-value: 1.22e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067    2 FPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAG 81
Cdd:PLN00154  39 FPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAG 118

                         90
                 ....*....|....
gi 41406067   82 GGVIPHIHKSLIGK 95
Cdd:PLN00154 119 GGVIPHIHKSLINK 132
PTZ00017 PTZ00017
histone H2A; Provisional
 2-102 7.25e-55

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 166.84  E-value: 7.25e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067    2 FPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLI-KATIA 80
Cdd:PTZ00017  28 FPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEELNKLLaGVTIA 106

                         90       100
                 ....*....|....*....|..
gi 41406067   81 GGGVIPHIHKSLIGKKGQQKTA 102
Cdd:PTZ00017 107 SGGVLPNIHKVLLPKKSKPKQG 128
H2A smart00414
Histone 2A;
2-98 7.95e-53

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 160.58  E-value: 7.95e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067      2 FPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKA-TIA 80
Cdd:smart00414  10 FPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNKLLKGvTIA 88

                           90
                   ....*....|....*...
gi 41406067     81 GGGVIPHIHKSLIGKKGQ 98
Cdd:smart00414  89 QGGVLPNIHKVLLPKKTG 106
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 2-79 2.89e-40

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: 128.03  E-value: 2.89e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41406067   2 FPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATI 79
Cdd:cd00074  11 FPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELNKLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
2-96 1.95e-39

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 127.67  E-value: 1.95e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067   2 FPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIK-ATIA 80
Cdd:COG5262  27 FPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELNKLLGdVTIA 105

                        90
                ....*....|....*.
gi 41406067  81 GGGVIPHIHKSLIGKK 96
Cdd:COG5262 106 QGGVLPNINPGLLPKS 121
PLN00157 PLN00157
histone H2A; Provisional
 2-102 6.61e-35

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 116.10  E-value: 6.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067    2 FPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIK-ATIA 80
Cdd:PLN00157  27 FPVGRIARYLKAGKYAT-RVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVRNDEELSKLLGgVTIA 105

                         90       100
                 ....*....|....*....|..
gi 41406067   81 GGGVIPHIHKSLIGKKGQQKTA 102
Cdd:PLN00157 106 AGGVLPNIHSVLLPKKSGKSKG 127
PLN00156 PLN00156
histone H2AX; Provisional
 2-99 1.71e-33

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 112.75  E-value: 1.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067    2 FPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKA-TIA 80
Cdd:PLN00156  30 FPVGRIARFLKAGKYAE-RVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHIQLAVRNDEELSKLLGSvTIA 108

                         90
                 ....*....|....*....
gi 41406067   81 GGGVIPHIHKSLIGKKGQQ 99
Cdd:PLN00156 109 AGGVLPNIHQTLLPKKVGK 127
PLN00153 PLN00153
histone H2A; Provisional
 2-96 3.47e-29

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 101.72  E-value: 3.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067    2 FPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLI-KATIA 80
Cdd:PLN00153  25 FPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVPRHIQLAIRNDEELGKLLgEVTIA 103

                         90
                 ....*....|....*.
gi 41406067   81 GGGVIPHIHKSLIGKK 96
Cdd:PLN00153 104 SGGVLPNIHAVLLPKK 119
PTZ00252 PTZ00252
histone H2A; Provisional
 1-100 2.80e-20

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 78.85  E-value: 2.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41406067    1 MFPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNAS--KDLKVKRITPRHLQLAIRGDEELDSLIK-A 77
Cdd:PTZ00252  25 IFPVGRVGSLLR-RGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAaqQAKKPKRLTPRTVTLAVRHDDDLGSLLKnV 103

                         90       100
                 ....*....|....*....|....
gi 41406067   78 TIAGGGVIPHIHKSLIGK-KGQQK 100
Cdd:PTZ00252 104 TLSRGGVMPSLNKALAKKhKSGKK 127
Histone pfam00125
Core histone H2A/H2B/H3/H4;
1-68 4.30e-17

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 70.54  E-value: 4.30e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41406067     1 MFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGD 68
Cdd:pfam00125  59 KLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 2-74 1.72e-11

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: 54.94  E-value: 1.72e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41406067   2 FPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSL 74
Cdd:cd22915   2 FPVDKIHPLLK-KDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDL 73
Histone_H2A_C pfam16211
C-terminus of histone H2A;
69-102 3.88e-10

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 50.22  E-value: 3.88e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 41406067    69 EELDSLIK-ATIAGGGVIPHIHKSLIGKKGQQKTA 102
Cdd:pfam16211   1 EELNKLLRgVTIAQGGVLPNIHKVLLPKKTKKKKK 35
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
2-74 5.16e-06

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 41.87  E-value: 5.16e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41406067   2 FPVGRIHRHLKTrTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSL 74
Cdd:COG5247  24 FPIARLKKIMQL-DEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 2-71 5.52e-06

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: 41.52  E-value: 5.52e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41406067   2 FPVGRIHRHL-KTRTTShgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 71
Cdd:cd22913  19 FSVGRFHRWMvDSRLAK--RIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAEL 87
PLN00155 PLN00155
histone H2A; Provisional
 2-36 6.54e-05

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 37.76  E-value: 6.54e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 41406067    2 FPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYL 36
Cdd:PLN00155  25 FPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYL 58
 
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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