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Conserved domains on  [gi|15219078|ref|NP_175683|]
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histone H2A protein 9 [Arabidopsis thaliana]

Protein Classification

PLN00154 family protein( domain architecture ID 11476415)

PLN00154 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
1-134 1.00e-71

histone H2A; Provisional


:

Pssm-ID: 177756  Cd Length: 136  Bit Score: 210.96  E-value: 1.00e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078    1 MSGKGAKGLIMGKPSGSDKDKDK--KKPITRSSRAGLQFPVGRVHRLLKTRSTAHGRVGATAAVYTAAILEYLTAEVLEL 78
Cdd:PLN00154   1 MSGKGGKGLLAAKTTAAAAKKDKdkKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLEL 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15219078   79 AGNASKDLKVKRISPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKSAKE 134
Cdd:PLN00154  81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKSTKK 136
 
Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
1-134 1.00e-71

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 210.96  E-value: 1.00e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078    1 MSGKGAKGLIMGKPSGSDKDKDK--KKPITRSSRAGLQFPVGRVHRLLKTRSTAHGRVGATAAVYTAAILEYLTAEVLEL 78
Cdd:PLN00154   1 MSGKGGKGLLAAKTTAAAAKKDKdkKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLEL 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15219078   79 AGNASKDLKVKRISPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKSAKE 134
Cdd:PLN00154  81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKSTKK 136
H2A smart00414
Histone 2A;
28-133 2.79e-55

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 168.28  E-value: 2.79e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078     28 TRSSRAGLQFPVGRVHRLLKTRSTAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEELD 107
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79
                           90       100
                   ....*....|....*....|....*..
gi 15219078    108 TLIKG-TIAGGGVIPHIHKSLINKSAK 133
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPKKTG 106
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
28-114 4.63e-46

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: 144.21  E-value: 4.63e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078  28 TRSSRAGLQFPVGRVHRLLKtRSTAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEELD 107
Cdd:cd00074   2 SRSKRAGLQFPVGRIHRLLK-KGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80

                ....*..
gi 15219078 108 TLIKGTI 114
Cdd:cd00074  81 KLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
28-134 3.26e-42

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 136.15  E-value: 3.26e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078  28 TRSSRAGLQFPVGRVHRLLKTRSTAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEELD 107
Cdd:COG5262  18 SRSAKAGLIFPVGRVKRLLKKGNYRM-RIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELN 96
                        90       100
                ....*....|....*....|....*...
gi 15219078 108 TLIKG-TIAGGGVIPHIHKSLINKSAKE 134
Cdd:COG5262  97 KLLGDvTIAQGGVLPNINPGLLPKSSKK 124
Histone pfam00125
Core histone H2A/H2B/H3/H4;
27-103 2.37e-16

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 69.77  E-value: 2.37e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219078    27 ITRSSRAGLQFPVGRVHRLLKTRSTAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGD 103
Cdd:pfam00125  50 QSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
 
Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
1-134 1.00e-71

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 210.96  E-value: 1.00e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078    1 MSGKGAKGLIMGKPSGSDKDKDK--KKPITRSSRAGLQFPVGRVHRLLKTRSTAHGRVGATAAVYTAAILEYLTAEVLEL 78
Cdd:PLN00154   1 MSGKGGKGLLAAKTTAAAAKKDKdkKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLEL 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15219078   79 AGNASKDLKVKRISPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKSAKE 134
Cdd:PLN00154  81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKSTKK 136
PTZ00017 PTZ00017
histone H2A; Provisional
1-133 1.29e-59

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 179.94  E-value: 1.29e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078    1 MSGKGAKGliMGKPSGSDkdkdkkkPITRSSRAGLQFPVGRVHRLLKTRSTAHgRVGATAAVYTAAILEYLTAEVLELAG 80
Cdd:PTZ00017   1 KGGKGKTG--GGKAGKKK-------PVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAG 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15219078   81 NASKDLKVKRISPRHLQLAIRGDEELDTLIKG-TIAGGGVIPHIHKSLINKSAK 133
Cdd:PTZ00017  71 NAAKDNKKKRITPRHIQLAIRNDEELNKLLAGvTIASGGVLPNIHKVLLPKKSK 124
H2A smart00414
Histone 2A;
28-133 2.79e-55

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 168.28  E-value: 2.79e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078     28 TRSSRAGLQFPVGRVHRLLKTRSTAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEELD 107
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79
                           90       100
                   ....*....|....*....|....*..
gi 15219078    108 TLIKG-TIAGGGVIPHIHKSLINKSAK 133
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPKKTG 106
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
28-114 4.63e-46

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: 144.21  E-value: 4.63e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078  28 TRSSRAGLQFPVGRVHRLLKtRSTAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEELD 107
Cdd:cd00074   2 SRSKRAGLQFPVGRIHRLLK-KGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80

                ....*..
gi 15219078 108 TLIKGTI 114
Cdd:cd00074  81 KLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
28-134 3.26e-42

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 136.15  E-value: 3.26e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078  28 TRSSRAGLQFPVGRVHRLLKTRSTAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEELD 107
Cdd:COG5262  18 SRSAKAGLIFPVGRVKRLLKKGNYRM-RIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELN 96
                        90       100
                ....*....|....*....|....*...
gi 15219078 108 TLIKG-TIAGGGVIPHIHKSLINKSAKE 134
Cdd:COG5262  97 KLLGDvTIAQGGVLPNINPGLLPKSSKK 124
PLN00157 PLN00157
histone H2A; Provisional
26-133 5.85e-39

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 127.66  E-value: 5.85e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078   26 PITRSSRAGLQFPVGRVHRLLKTRSTAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEE 105
Cdd:PLN00157  16 ATSRSAKAGLQFPVGRIARYLKAGKYAT-RVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVRNDEE 94
                         90       100
                 ....*....|....*....|....*....
gi 15219078  106 LDTLIKG-TIAGGGVIPHIHKSLINKSAK 133
Cdd:PLN00157  95 LSKLLGGvTIAAGGVLPNIHSVLLPKKSG 123
PLN00156 PLN00156
histone H2AX; Provisional
1-132 1.73e-36

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 121.61  E-value: 1.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078    1 MSGKGAKGlimgKPSGSDKdkdkkkpITRSSRAGLQFPVGRVHRLLKTRSTAHgRVGATAAVYTAAILEYLTAEVLELAG 80
Cdd:PLN00156   5 GTTKGGRG----KPKATKS-------VSRSSKAGLQFPVGRIARFLKAGKYAE-RVGAGAPVYLSAVLEYLAAEVLELAG 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15219078   81 NASKDLKVKRISPRHLQLAIRGDEELDTLIKG-TIAGGGVIPHIHKSLINKSA 132
Cdd:PLN00156  73 NAARDNKKNRIVPRHIQLAVRNDEELSKLLGSvTIAAGGVLPNIHQTLLPKKV 125
PLN00153 PLN00153
histone H2A; Provisional
27-133 1.33e-31

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 109.04  E-value: 1.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078   27 ITRSSRAGLQFPVGRVHRLLKTRSTAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEEL 106
Cdd:PLN00153  15 VSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVPRHIQLAIRNDEEL 93
                         90       100
                 ....*....|....*....|....*...
gi 15219078  107 DTLI-KGTIAGGGVIPHIHKSLINKSAK 133
Cdd:PLN00153  94 GKLLgEVTIASGGVLPNIHAVLLPKKTK 121
PTZ00252 PTZ00252
histone H2A; Provisional
29-130 5.75e-23

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 86.94  E-value: 5.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078   29 RSSRAGLQFPVGRVHRLLKTRSTAHgRVGATAAVYTAAILEYLTAEVLELAGNAS--KDLKVKRISPRHLQLAIRGDEEL 106
Cdd:PTZ00252  18 RSAKAGLIFPVGRVGSLLRRGQYAR-RIGASGAVYMAAVLEYLTAELLELSVKAAaqQAKKPKRLTPRTVTLAVRHDDDL 96
                         90       100
                 ....*....|....*....|....*
gi 15219078  107 DTLIKG-TIAGGGVIPHIHKSLINK 130
Cdd:PTZ00252  97 GSLLKNvTLSRGGVMPSLNKALAKK 121
Histone pfam00125
Core histone H2A/H2B/H3/H4;
27-103 2.37e-16

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 69.77  E-value: 2.37e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219078    27 ITRSSRAGLQFPVGRVHRLLKTRSTAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGD 103
Cdd:pfam00125  50 QSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
37-106 5.35e-13

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: 59.94  E-value: 5.35e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078  37 FPVGRVHRLLKtRSTAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEEL 106
Cdd:cd22915   2 FPVDKIHPLLK-KDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVL 70
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
29-117 8.74e-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: 55.00  E-value: 8.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078  29 RSSRAGLQFPVGRVHR-LLKTRSTAhgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEEL- 106
Cdd:cd22913  11 KSARCGLTFSVGRFHRwMVDSRLAK--RIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAELw 88
                        90
                ....*....|....*..
gi 15219078 107 ------DTLIKGTIAGG 117
Cdd:cd22913  89 gllqpyEHLICGRNASG 105
PLN00155 PLN00155
histone H2A; Provisional
1-71 4.40e-09

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 49.32  E-value: 4.40e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219078    1 MSGKGAkglimGKPSGSDKdkdkkkpITRSSRAGLQFPVGRVHRLLKTRSTAHgRVGATAAVYTAAILEYL 71
Cdd:PLN00155   1 MAGRGK-----GKTSGKKA-------VSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYL 58
Histone_H2A_C pfam16211
C-terminus of histone H2A;
104-133 9.33e-09

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 47.91  E-value: 9.33e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 15219078   104 EELDTLIKG-TIAGGGVIPHIHKSLINKSAK 133
Cdd:pfam16211   1 EELNKLLRGvTIAQGGVLPNIHKVLLPKKTK 31
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
11-109 5.52e-07

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 45.34  E-value: 5.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219078  11 MGKPSGSDKDKDKKKPITRSSRaglQFPVGRVHRLLKTRSTAhGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKR 90
Cdd:COG5247   1 GGSPVGNMGTMPKQNSQKKKKT---RFPIARLKKIMQLDEDI-GKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKR 76
                        90
                ....*....|....*....
gi 15219078  91 ISPRHLQLAIRGDEELDTL 109
Cdd:COG5247  77 MTSEFLKRATESDEKFDFL 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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