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Conserved domains on  [gi|17544704|ref|NP_501718|]
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Histone H2A [Caenorhabditis elegans]

Protein Classification

histone H2A family protein( domain architecture ID 12210400)

histone H2A family protein similar to histone 2A (H2A) that is a core component of nucleosome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
H2A smart00414
Histone 2A;
29-132 2.64e-51

Histone 2A;


:

Pssm-ID: 197711  Cd Length: 106  Bit Score: 158.65  E-value: 2.64e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704     29 SRSTRSGLTFPVGRIHRKLRETTRGkQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQETA 108
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYA-KRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....
gi 17544704    109 QLLDKVTLPQGGVTPmPIHPSLLP 132
Cdd:smart00414  80 KLLKGVTIAQGGVLP-NIHKVLLP 102
 
Name Accession Description Interval E-value
H2A smart00414
Histone 2A;
29-132 2.64e-51

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 158.65  E-value: 2.64e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704     29 SRSTRSGLTFPVGRIHRKLRETTRGkQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQETA 108
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYA-KRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....
gi 17544704    109 QLLDKVTLPQGGVTPmPIHPSLLP 132
Cdd:smart00414  80 KLLKGVTIAQGGVLP-NIHKVLLP 102
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 29-117 2.77e-39

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: 127.65  E-value: 2.77e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704  29 SRSTRSGLTFPVGRIHRKLRETTRgKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQETA 108
Cdd:cd00074   2 SRSKRAGLQFPVGRIHRLLKKGTY-AKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*....
gi 17544704 109 QLLDKVTLP 117
Cdd:cd00074  81 KLFKGVTIA 89
PTZ00017 PTZ00017
histone H2A; Provisional
 28-132 3.18e-37

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 123.70  E-value: 3.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704   28 ISRSTRSGLTFPVGRIHRKLReTTRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQET 107
Cdd:PTZ00017  18 VSRSAKAGLQFPVGRVHRYLK-KGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEEL 96

                         90       100
                 ....*....|....*....|....*
gi 17544704  108 AQLLDKVTLPQGGVTPMpIHPSLLP 132
Cdd:PTZ00017  97 NKLLAGVTIASGGVLPN-IHKVLLP 120
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
29-132 1.12e-31

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 109.57  E-value: 1.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704  29 SRSTRSGLTFPVGRIHRKLRETtRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQETA 108
Cdd:COG5262  18 SRSAKAGLIFPVGRVKRLLKKG-NYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELN 96

                        90       100
                ....*....|....*....|....
gi 17544704 109 QLLDKVTLPQGGVTPMpIHPSLLP 132
Cdd:COG5262  97 KLLGDVTIAQGGVLPN-INPGLLP 119
Histone pfam00125
Core histone H2A/H2B/H3/H4;
27-104 1.15e-18

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 76.32  E-value: 1.15e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17544704    27 RISRSTRSGLTFPVGRIHRKLRETTRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGD 104
Cdd:pfam00125  49 YQSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
 
Name Accession Description Interval E-value
H2A smart00414
Histone 2A;
29-132 2.64e-51

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 158.65  E-value: 2.64e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704     29 SRSTRSGLTFPVGRIHRKLRETTRGkQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQETA 108
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYA-KRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....
gi 17544704    109 QLLDKVTLPQGGVTPmPIHPSLLP 132
Cdd:smart00414  80 KLLKGVTIAQGGVLP-NIHKVLLP 102
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 29-117 2.77e-39

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: 127.65  E-value: 2.77e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704  29 SRSTRSGLTFPVGRIHRKLRETTRgKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQETA 108
Cdd:cd00074   2 SRSKRAGLQFPVGRIHRLLKKGTY-AKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*....
gi 17544704 109 QLLDKVTLP 117
Cdd:cd00074  81 KLFKGVTIA 89
PTZ00017 PTZ00017
histone H2A; Provisional
 28-132 3.18e-37

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 123.70  E-value: 3.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704   28 ISRSTRSGLTFPVGRIHRKLReTTRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQET 107
Cdd:PTZ00017  18 VSRSAKAGLQFPVGRVHRYLK-KGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEEL 96

                         90       100
                 ....*....|....*....|....*
gi 17544704  108 AQLLDKVTLPQGGVTPMpIHPSLLP 132
Cdd:PTZ00017  97 NKLLAGVTIASGGVLPN-IHKVLLP 120
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
29-132 1.12e-31

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 109.57  E-value: 1.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704  29 SRSTRSGLTFPVGRIHRKLRETtRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQETA 108
Cdd:COG5262  18 SRSAKAGLIFPVGRVKRLLKKG-NYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELN 96

                        90       100
                ....*....|....*....|....
gi 17544704 109 QLLDKVTLPQGGVTPMpIHPSLLP 132
Cdd:COG5262  97 KLLGDVTIAQGGVLPN-INPGLLP 119
PLN00157 PLN00157
histone H2A; Provisional
 28-132 1.50e-31

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 109.17  E-value: 1.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704   28 ISRSTRSGLTFPVGRIHRKLRETtRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQET 107
Cdd:PLN00157  17 TSRSAKAGLQFPVGRIARYLKAG-KYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVRNDEEL 95

                         90       100
                 ....*....|....*....|....*
gi 17544704  108 AQLLDKVTLPQGGVTPmPIHPSLLP 132
Cdd:PLN00157  96 SKLLGGVTIAAGGVLP-NIHSVLLP 119
PLN00156 PLN00156
histone H2AX; Provisional
 28-132 1.71e-29

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 104.28  E-value: 1.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704   28 ISRSTRSGLTFPVGRIHRKLReTTRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQET 107
Cdd:PLN00156  20 VSRSSKAGLQFPVGRIARFLK-AGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHIQLAVRNDEEL 98

                         90       100
                 ....*....|....*....|....*
gi 17544704  108 AQLLDKVTLPQGGVTPmPIHPSLLP 132
Cdd:PLN00156  99 SKLLGSVTIAAGGVLP-NIHQTLLP 122
PLN00154 PLN00154
histone H2A; Provisional
 28-131 5.06e-29

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 103.10  E-value: 5.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704   28 ISRSTRSGLTFPVGRIHRKLRETTRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQET 107
Cdd:PLN00154  29 TSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 108

                         90       100
                 ....*....|....*....|....
gi 17544704  108 AQLLdKVTLPQGGVTPMpIHPSLL 131
Cdd:PLN00154 109 DTLI-KGTIAGGGVIPH-IHKSLI 130
PLN00153 PLN00153
histone H2A; Provisional
 28-132 1.99e-28

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 101.33  E-value: 1.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704   28 ISRSTRSGLTFPVGRIHRKLRETtRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQET 107
Cdd:PLN00153  15 VSRSAKAGLQFPVGRIARYLKKG-KYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVPRHIQLAIRNDEEL 93

                         90       100
                 ....*....|....*....|....*
gi 17544704  108 AQLLDKVTLPQGGVTPmPIHPSLLP 132
Cdd:PLN00153  94 GKLLGEVTIASGGVLP-NIHAVLLP 117
PTZ00252 PTZ00252
histone H2A; Provisional
 29-123 2.74e-21

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 83.09  E-value: 2.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704   29 SRSTRSGLTFPVGRIHRKLRettRGK--QRISAGASVFMAATLEYLTTELMEMSAIAANES--KKSRVTPRHLHLAIYGD 104
Cdd:PTZ00252  17 GRSAKAGLIFPVGRVGSLLR---RGQyaRRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPRTVTLAVRHD 93

                         90
                 ....*....|....*....
gi 17544704  105 QETAQLLDKVTLPQGGVTP 123
Cdd:PTZ00252  94 DDLGSLLKNVTLSRGGVMP 112
Histone pfam00125
Core histone H2A/H2B/H3/H4;
27-104 1.15e-18

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 76.32  E-value: 1.15e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17544704    27 RISRSTRSGLTFPVGRIHRKLRETTRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGD 104
Cdd:pfam00125  49 YQSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 27-77 8.54e-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: 55.38  E-value: 8.54e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 17544704  27 RISRSTRSGLTFPVGRIHRKLRETTRGKqRISAGASVFMAATLEYLTTELM 77
Cdd:cd22913   8 RRSKSARCGLTFSVGRFHRWMVDSRLAK-RIHEHAAVYLTACMENLLEEIF 57
PLN00155 PLN00155
histone H2A; Provisional
 28-72 3.64e-10

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 52.40  E-value: 3.64e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 17544704   28 ISRSTRSGLTFPVGRIHRKLRettRGK--QRISAGASVFMAATLEYL 72
Cdd:PLN00155  15 VSRSAKAGLQFPVGRIARYLK---KGKyaERIGAGAPVYLAAVLEYL 58
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 37-111 8.78e-09

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: 49.16  E-value: 8.78e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17544704  37 TFPVGRIHRKLRETtRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQETAQLL 111
Cdd:cd22915   1 LFPVDKIHPLLKKD-LLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLF 74
Histone_H2A_C pfam16211
C-terminus of histone H2A;
106-132 5.69e-04

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 35.59  E-value: 5.69e-04
                          10        20
                  ....*....|....*....|....*...
gi 17544704   106 ETAQLLDKVTLPQGGVtpMP-IHPSLLP 132
Cdd:pfam16211   2 ELNKLLRGVTIAQGGV--LPnIHKVLLP 27
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 38-101 9.46e-04

histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription regulators and similar proteins; The family includes many archaeal histone-fold proteins and histone-like transcription regulators, which may bind and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. They can increase the resistance of DNA to thermal denaturation.


Pssm-ID: 467034  Cd Length: 64  Bit Score: 35.60  E-value: 9.46e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17544704  38 FPVGRIHRKLRETtrGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAI 101
Cdd:cd22909   2 LPKAPVKRIIKKA--GAERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVKAEDIELAV 63
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
38-123 3.41e-03

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 35.32  E-value: 3.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544704  38 FPVGRIhRKLRETTRGKQRISAGASVFMAATLEYLTTELMEMSAIAANESKKSRVTPRHLHLAIYGDQETAQLLDKVTLP 117
Cdd:COG5247  24 FPIARL-KKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFLKNMEQFK 102


                ....*.
gi 17544704 118 QGGVTP 123
Cdd:COG5247 103 NRETQP 108
 
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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