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Conserved domains on  [gi|6319470|ref|NP_009552|]
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histone H2A [Saccharomyces cerevisiae S288C]

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

CATH:  1.10.20.10
Gene Ontology:  GO:0003677|GO:0030527|GO:0000786|GO:0006281
PubMed:  8121801|35331626|31965982|24647359
SCOP:  4000793

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 18-131 1.48e-68

histone H2A; Provisional


:

Pssm-ID: 185399  Cd Length: 134  Bit Score: 202.67  E-value: 1.48e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470    18 SRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNK 97
Cdd:PTZ00017  19 SRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEELNK 98

                         90       100       110
                 ....*....|....*....|....*....|....
gi 6319470    98 LLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQE 131
Cdd:PTZ00017  99 LLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 18-131 1.48e-68

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 202.67  E-value: 1.48e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470    18 SRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNK 97
Cdd:PTZ00017  19 SRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEELNK 98

                         90       100       110
                 ....*....|....*....|....*....|....
gi 6319470    98 LLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQE 131
Cdd:PTZ00017  99 LLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
H2A smart00414
Histone 2A;
18-123 5.11e-68

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 200.25  E-value: 5.11e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470      18 SRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNK 97
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 6319470      98 LLGNVTIAQGGVLPNIHQNLLPKKSA 123
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
17-132 2.02e-64

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 192.00  E-value: 2.02e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470   17 QSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELN 96
Cdd:COG5262  17 QSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELN 96

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6319470   97 KLLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQEL 132
Cdd:COG5262  97 KLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQEL 132
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 17-105 8.69e-57

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: 171.18  E-value: 8.69e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470   17 QSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELN 96
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*....
gi 6319470   97 KLLGNVTIA 105
Cdd:cd00074  81 KLFKGVTIA 89
Histone_H2A_C pfam16211
C-terminus of histone H2A;
93-127 2.61e-19

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 74.88  E-value: 2.61e-19
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6319470     93 DELNKLLGNVTIAQGGVLPNIHQNLLPKKSAKTAK 127
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 18-131 1.48e-68

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 202.67  E-value: 1.48e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470    18 SRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNK 97
Cdd:PTZ00017  19 SRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEELNK 98

                         90       100       110
                 ....*....|....*....|....*....|....
gi 6319470    98 LLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQE 131
Cdd:PTZ00017  99 LLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
H2A smart00414
Histone 2A;
18-123 5.11e-68

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 200.25  E-value: 5.11e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470      18 SRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNK 97
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 6319470      98 LLGNVTIAQGGVLPNIHQNLLPKKSA 123
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PLN00157 PLN00157
histone H2A; Provisional
 18-131 3.94e-65

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 193.91  E-value: 3.94e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470    18 SRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNK 97
Cdd:PLN00157  18 SRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVRNDEELSK 97

                         90       100       110
                 ....*....|....*....|....*....|....
gi 6319470    98 LLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQE 131
Cdd:PLN00157  98 LLGGVTIAAGGVLPNIHSVLLPKKSGKSKGEPKD 131
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
17-132 2.02e-64

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 192.00  E-value: 2.02e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470   17 QSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELN 96
Cdd:COG5262  17 QSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELN 96

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6319470   97 KLLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQEL 132
Cdd:COG5262  97 KLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQEL 132
PLN00156 PLN00156
histone H2AX; Provisional
 18-132 2.34e-59

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 179.78  E-value: 2.34e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470    18 SRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNK 97
Cdd:PLN00156  21 SRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHIQLAVRNDEELSK 100

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 6319470    98 LLGNVTIAQGGVLPNIHQNLLPKKSAKTAK----ASQEL 132
Cdd:PLN00156 101 LLGSVTIAAGGVLPNIHQTLLPKKVGKGKGdigsASQEF 139
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 17-105 8.69e-57

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: 171.18  E-value: 8.69e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470   17 QSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELN 96
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*....
gi 6319470   97 KLLGNVTIA 105
Cdd:cd00074  81 KLFKGVTIA 89
PLN00153 PLN00153
histone H2A; Provisional
 18-131 5.32e-52

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 160.65  E-value: 5.32e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470    18 SRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNK 97
Cdd:PLN00153  16 SRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVPRHIQLAIRNDEELGK 95

                         90       100       110
                 ....*....|....*....|....*....|....
gi 6319470    98 LLGNVTIAQGGVLPNIHQNLLPKKSaKTAKASQE 131
Cdd:PLN00153  96 LLGEVTIASGGVLPNIHAVLLPKKT-KGGKGEET 128
PLN00154 PLN00154
histone H2A; Provisional
 17-124 8.04e-39

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 127.37  E-value: 8.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470    17 QSRSAKAGLTFPVGRVHRLLR-RGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDEL 95
Cdd:PLN00154  29 TSRSSRAGLQFPVGRIHRQLKqRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 108

                         90       100
                 ....*....|....*....|....*....
gi 6319470    96 NKLLgNVTIAQGGVLPNIHQNLLPKKSAK 124
Cdd:PLN00154 109 DTLI-KGTIAGGGVIPHIHKSLINKSTKK 136
PTZ00252 PTZ00252
histone H2A; Provisional
 18-129 4.64e-37

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 122.76  E-value: 4.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470    18 SRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDN--KKTRIIPRHLQLAIRNDDEL 95
Cdd:PTZ00252  17 GRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPRTVTLAVRHDDDL 96

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 6319470    96 NKLLGNVTIAQGGVLPNIHQNLLPK-KSAKTAKAS 129
Cdd:PTZ00252  97 GSLLKNVTLSRGGVMPSLNKALAKKhKSGKKAKAT 131
Histone_H2A_C pfam16211
C-terminus of histone H2A;
93-127 2.61e-19

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 74.88  E-value: 2.61e-19
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6319470     93 DELNKLLGNVTIAQGGVLPNIHQNLLPKKSAKTAK 127
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 26-100 6.38e-19

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: 74.97  E-value: 6.38e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319470   26 TFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLG 100
Cdd:cd22915   1 LFPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
PLN00155 PLN00155
histone H2A; Provisional
 18-60 1.96e-17

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 70.89  E-value: 1.96e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 6319470    18 SRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYL 60
Cdd:PLN00155  16 SRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
Histone pfam00125
Core histone H2A/H2B/H3/H4;
17-90 1.45e-14

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 65.15  E-value: 1.45e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319470     17 QSRSAKAGLTFPVGRVHRLLRRGNYA-QRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIR 90
Cdd:pfam00125  50 QSSTDLLIYKLPFARVVREVVQSTKTdLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARR 124
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 17-99 1.82e-14

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: 64.24  E-value: 1.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319470   17 QSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELN 96
Cdd:cd22913   9 RSKSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAELW 88


                ...
gi 6319470   97 KLL 99
Cdd:cd22913  89 GLL 91
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
27-98 4.31e-06

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 42.64  E-value: 4.31e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319470   27 FPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKL 98
Cdd:COG5247  24 FPIARLKKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
HFD_DRAP1 cd22906
histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, ...
 27-98 2.31e-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: 2.31e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319470   27 FPVGRVHRLLRR----GnyaqRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKL 98
Cdd:cd22906   4 FPAARIKKIMQSdeevG----KVAAAVPVLISKALELFLEDLLTKAAEVAKERNAKTITPSHLKQCVESEEKFDFL 75
CBFD_NFYB_HMF pfam00808
Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes ...
 27-89 1.83e-03

Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes archaebacterial histones and histone like transcription factors from eukaryotes.


Pssm-ID: 395650  Cd Length: 65  Bit Score: 34.51  E-value: 1.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319470     27 FPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAA-RDNKKTrIIPRHLQLAI 89
Cdd:pfam00808   3 LPIARVKRIMKSDPDAGRISQDAKELIAECVEEFIEFVASEAAEICnKAGRKT-INPEHIKQAV 65
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 27-90 4.13e-03

histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


Pssm-ID: 467021  Cd Length: 63  Bit Score: 33.73  E-value: 4.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319470   27 FPVGRVHRLLRRGNYaQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIR 90
Cdd:cd00076   1 LLRSAVARILKSAGF-DSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
HFD_Dpb3-like cd23645
histone-fold domain found in Schizosaccharomyces pombe DNA polymerase epsilon subunit C (Dpb3) ...
 25-98 5.63e-03

histone-fold domain found in Schizosaccharomyces pombe DNA polymerase epsilon subunit C (Dpb3) and similar proteins; Schizosaccharomyces pombe Dpb3 is an accessory component of the DNA polymerase epsilon (DNA polymerase II) that is a heterotetramer consisting of cdc20/Pol2, Dpb2, Dpb3, and Dpb4, and participates in chromosomal DNA replication. Dpb3 is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair. The Dpb3-Dpb4 dimer associates with histone deacetylases, chromatin remodelers, and histones and plays a crucial role in the inheritance of histone hypoacetylation and H3K9 methylation in heterochromatin. The Dpb3-Dpb4 dimer is also required for the recruitment of sir2 to heterochromatin.


Pssm-ID: 467059 [Multi-domain]  Cd Length: 78  Bit Score: 33.74  E-value: 5.63e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319470   25 LTFPVGRVHRLLRRGNYAQRIGSGApVYLTAV-----LEYLAAEILElagNAARDNKKTrIIPRHLQLAIRNDDELNKL 98
Cdd:cd23645   1 TVLPLARVKRIIKADKDVKICSKDA-VFLISKatelfIEYLAEQAYE---LAKLEKRKT-VQYKDLAKAVKRDDNLEFL 74
 
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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