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Conserved domains on  [gi|71031070|ref|XP_765177|]
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histone H2A [Theileria parva strain Muguga]

Protein Classification

histone H2A( domain architecture ID 11487859)

histone H2A is a core component of the nucleosome which plays a central role in DNA double strand break (DSB) repair

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 34-151 1.23e-67

histone H2A; Provisional


:

Pssm-ID: 185399  Cd Length: 134  Bit Score: 201.13  E-value: 1.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070   34 TPMSRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 113
Cdd:PTZ00017  16 KPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDE 94

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71031070  114 ELDTLV-KATIAGGGVIPHIHKALMNKGPAPVLVKPPKR 151
Cdd:PTZ00017  95 ELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQGKKQNK 133
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 34-151 1.23e-67

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 201.13  E-value: 1.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070   34 TPMSRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 113
Cdd:PTZ00017  16 KPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDE 94

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71031070  114 ELDTLV-KATIAGGGVIPHIHKALMNKGPAPVLVKPPKR 151
Cdd:PTZ00017  95 ELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQGKKQNK 133
H2A smart00414
Histone 2A;
37-139 1.79e-52

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 161.73  E-value: 1.79e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070     37 SRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 116
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....
gi 71031070    117 TLVKA-TIAGGGVIPHIHKALMNK 139
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPK 103
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
36-139 1.30e-43

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 140.38  E-value: 1.30e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070  36 MSRAARAGLQFPVGRVHRMLKsRVSADGRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 115
Cdd:COG5262  17 QSRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEEL 95

                        90       100
                ....*....|....*....|....*
gi 71031070 116 DTLVK-ATIAGGGVIPHIHKALMNK 139
Cdd:COG5262  96 NKLLGdVTIAQGGVLPNINPGLLPK 120
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 37-123 3.66e-43

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: 137.66  E-value: 3.66e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070  37 SRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 116
Cdd:cd00074   2 SRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*..
gi 71031070 117 TLVKATI 123
Cdd:cd00074  81 KLFKGVT 87
Histone pfam00125
Core histone H2A/H2B/H3/H4;
36-112 4.34e-17

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 72.47  E-value: 4.34e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71031070    36 MSRAARAGLQFPVGRVHRMLKSRVSADGRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGD 112
Cdd:pfam00125  50 QSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 34-151 1.23e-67

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 201.13  E-value: 1.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070   34 TPMSRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 113
Cdd:PTZ00017  16 KPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDE 94

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71031070  114 ELDTLV-KATIAGGGVIPHIHKALMNKGPAPVLVKPPKR 151
Cdd:PTZ00017  95 ELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQGKKQNK 133
PLN00154 PLN00154
histone H2A; Provisional
 35-139 2.40e-65

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 195.55  E-value: 2.40e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070   35 PMSRAARAGLQFPVGRVHRMLKSRVSADGRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEE 114
Cdd:PLN00154  28 PTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEE 107

                         90       100
                 ....*....|....*....|....*
gi 71031070  115 LDTLVKATIAGGGVIPHIHKALMNK 139
Cdd:PLN00154 108 LDTLIKGTIAGGGVIPHIHKSLINK 132
H2A smart00414
Histone 2A;
37-139 1.79e-52

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 161.73  E-value: 1.79e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070     37 SRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 116
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....
gi 71031070    117 TLVKA-TIAGGGVIPHIHKALMNK 139
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPK 103
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
36-139 1.30e-43

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 140.38  E-value: 1.30e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070  36 MSRAARAGLQFPVGRVHRMLKsRVSADGRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 115
Cdd:COG5262  17 QSRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEEL 95

                        90       100
                ....*....|....*....|....*
gi 71031070 116 DTLVK-ATIAGGGVIPHIHKALMNK 139
Cdd:COG5262  96 NKLLGdVTIAQGGVLPNINPGLLPK 120
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 37-123 3.66e-43

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: 137.66  E-value: 3.66e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070  37 SRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 116
Cdd:cd00074   2 SRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*..
gi 71031070 117 TLVKATI 123
Cdd:cd00074  81 KLFKGVT 87
PLN00157 PLN00157
histone H2A; Provisional
 35-139 2.98e-37

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 124.19  E-value: 2.98e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070   35 PMSRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEE 114
Cdd:PLN00157  16 ATSRSAKAGLQFPVGRIARYLKAGKYAT-RVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVRNDEE 94

                         90       100
                 ....*....|....*....|....*.
gi 71031070  115 LDTLVK-ATIAGGGVIPHIHKALMNK 139
Cdd:PLN00157  95 LSKLLGgVTIAAGGVLPNIHSVLLPK 120
PLN00156 PLN00156
histone H2AX; Provisional
 36-139 1.57e-36

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 122.38  E-value: 1.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070   36 MSRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 115
Cdd:PLN00156  20 VSRSSKAGLQFPVGRIARFLKAGKYAE-RVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHIQLAVRNDEEL 98

                         90       100
                 ....*....|....*....|....*
gi 71031070  116 DTLVKA-TIAGGGVIPHIHKALMNK 139
Cdd:PLN00156  99 SKLLGSvTIAAGGVLPNIHQTLLPK 123
PLN00153 PLN00153
histone H2A; Provisional
 36-139 3.21e-32

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 111.35  E-value: 3.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070   36 MSRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 115
Cdd:PLN00153  15 VSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVPRHIQLAIRNDEEL 93

                         90       100
                 ....*....|....*....|....*
gi 71031070  116 DTLV-KATIAGGGVIPHIHKALMNK 139
Cdd:PLN00153  94 GKLLgEVTIASGGVLPNIHAVLLPK 118
PTZ00252 PTZ00252
histone H2A; Provisional
 37-139 1.45e-22

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 86.55  E-value: 1.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070   37 SRAARAGLQFPVGRVHRMLKsRVSADGRVGSTAAVYASAILEYLTAEVLELAGNAS--KDLKVKRITPRHLQLAIRGDEE 114
Cdd:PTZ00252  17 GRSAKAGLIFPVGRVGSLLR-RGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAaqQAKKPKRLTPRTVTLAVRHDDD 95

                         90       100
                 ....*....|....*....|....*.
gi 71031070  115 LDTLVK-ATIAGGGVIPHIHKALMNK 139
Cdd:PTZ00252  96 LGSLLKnVTLSRGGVMPSLNKALAKK 121
Histone pfam00125
Core histone H2A/H2B/H3/H4;
36-112 4.34e-17

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 72.47  E-value: 4.34e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71031070    36 MSRAARAGLQFPVGRVHRMLKSRVSADGRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGD 112
Cdd:pfam00125  50 QSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 37-115 4.23e-13

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: 61.55  E-value: 4.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070  37 SRAARAGLQFPVGRVHR-MLKSRVSAdgRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 115
Cdd:cd22913  10 SKSARCGLTFSVGRFHRwMVDSRLAK--RIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAEL 87
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 46-115 1.78e-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: 58.79  E-value: 1.78e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031070  46 FPVGRVHRMLKsRVSADGRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 115
Cdd:cd22915   2 FPVDKIHPLLK-KDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVL 70
PLN00155 PLN00155
histone H2A; Provisional
 36-80 9.31e-09

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 48.94  E-value: 9.31e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 71031070   36 MSRAARAGLQFPVGRVHRMLKSRVSADgRVGSTAAVYASAILEYL 80
Cdd:PLN00155  15 VSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYL 58
Histone_H2A_C pfam16211
C-terminus of histone H2A;
113-139 1.11e-08

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 47.91  E-value: 1.11e-08
                          10        20
                  ....*....|....*....|....*...
gi 71031070   113 EELDTLVK-ATIAGGGVIPHIHKALMNK 139
Cdd:pfam16211   1 EELNKLLRgVTIAQGGVLPNIHKVLLPK 28
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
45-118 2.09e-06

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 44.18  E-value: 2.09e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71031070  45 QFPVGRVHRMLKSRVSAdGRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTL 118
Cdd:COG5247  23 RFPIARLKKIMQLDEDI-GKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
HFD_DRAP1 cd22906
histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, ...
 46-118 3.77e-04

histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, also called Dr1-associated corepressor or negative cofactor 2-alpha (NC2-alpha), acts as a corepressor for Dr1 (down-regulator of transcription 1)-mediated repression of transcription. It forms a heterodimer with Dr1. The association of the Dr1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. DRAP1 can bind to DNA on its own. It also binds TATA-binding protein-associated factor 172 (BTAF1).


Pssm-ID: 467031 [Multi-domain]  Cd Length: 75  Bit Score: 37.12  E-value: 3.77e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71031070  46 FPVGRVHRMLKSrvsaD---GRVGSTAAVYASAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTL 118
Cdd:cd22906   4 FPAARIKKIMQS----DeevGKVAAAVPVLISKALELFLEDLLTKAAEVAKERNAKTITPSHLKQCVESEEKFDFL 75
 
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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