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Conserved domains on  [gi|19557656|ref|NP_003504|]
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histone H2A type 1-B/E [Homo sapiens]

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
 1-130 6.06e-70

histone H2A; Provisional


:

Pssm-ID: 185399  Cd Length: 134  Bit Score: 206.13  E-value: 6.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656    1 MSGRGKQGGKARAKAK--TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTR 78
Cdd:PTZ00017   1 KGGKGKTGGGKAGKKKpvSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19557656   79 IIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 130
Cdd:PTZ00017  81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 1-130 6.06e-70

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 206.13  E-value: 6.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656    1 MSGRGKQGGKARAKAK--TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTR 78
Cdd:PTZ00017   1 KGGKGKTGGGKAGKKKpvSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19557656   79 IIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 130
Cdd:PTZ00017  81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
H2A smart00414
Histone 2A;
17-122 7.74e-67

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 197.17  E-value: 7.74e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656     17 TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 96
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 19557656     97 LLGRVTIAQGGVLPNIQAVLLPKKTE 122
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 16-104 3.73e-56

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: 169.64  E-value: 3.73e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656  16 KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN 95
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*....
gi 19557656  96 KLLGRVTIA 104
Cdd:cd00074  81 KLFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
3-127 2.12e-53

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 164.26  E-value: 2.12e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656   3 GRGKQGGKARAKA-KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIP 81
Cdd:COG5262   3 SGGKGGKAADARVsQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19557656  82 RHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKA 127
Cdd:COG5262  83 RHLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKR 128
Histone_H2A_C pfam16211
C-terminus of histone H2A;
92-126 2.26e-17

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 69.87  E-value: 2.26e-17
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19557656    92 EELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHK 126
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 1-130 6.06e-70

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 206.13  E-value: 6.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656    1 MSGRGKQGGKARAKAK--TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTR 78
Cdd:PTZ00017   1 KGGKGKTGGGKAGKKKpvSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19557656   79 IIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 130
Cdd:PTZ00017  81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
H2A smart00414
Histone 2A;
17-122 7.74e-67

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 197.17  E-value: 7.74e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656     17 TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 96
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 19557656     97 LLGRVTIAQGGVLPNIQAVLLPKKTE 122
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PLN00157 PLN00157
histone H2A; Provisional
 1-130 1.39e-65

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 195.07  E-value: 1.39e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656    1 MSGRGKQ-GGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRI 79
Cdd:PLN00157   1 MSGRGKRkGGGGGKKATSRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19557656   80 IPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 130
Cdd:PLN00157  81 VPRHIQLAVRNDEELSKLLGGVTIAAGGVLPNIHSVLLPKKSGKSKGEPKD 131
PLN00156 PLN00156
histone H2AX; Provisional
 1-121 1.23e-57

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 175.16  E-value: 1.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656    1 MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRII 80
Cdd:PLN00156   5 GTTKGGRGKPKATKSVSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIV 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19557656   81 PRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKT 121
Cdd:PLN00156  85 PRHIQLAVRNDEELSKLLGSVTIAAGGVLPNIHQTLLPKKV 125
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 16-104 3.73e-56

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: 169.64  E-value: 3.73e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656  16 KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN 95
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*....
gi 19557656  96 KLLGRVTIA 104
Cdd:cd00074  81 KLFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
3-127 2.12e-53

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 164.26  E-value: 2.12e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656   3 GRGKQGGKARAKA-KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIP 81
Cdd:COG5262   3 SGGKGGKAADARVsQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19557656  82 RHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKA 127
Cdd:COG5262  83 RHLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKR 128
PLN00153 PLN00153
histone H2A; Provisional
 1-122 2.73e-53

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 163.74  E-value: 2.73e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656    1 MSGRGKqGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRII 80
Cdd:PLN00153   1 MAGRGK-GKTSGKKAVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 19557656   81 PRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTE 122
Cdd:PLN00153  80 PRHIQLAIRNDEELGKLLGEVTIASGGVLPNIHAVLLPKKTK 121
PLN00154 PLN00154
histone H2A; Provisional
 1-122 4.42e-39

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 128.14  E-value: 4.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656    1 MSGRGKQGGKA-------------RAKAKTRSSRAGLQFPVGRVHRLLRKG-NYSERVGAGAPVYLAAVLEYLTAEILEL 66
Cdd:PLN00154   1 MSGKGGKGLLAakttaaaakkdkdKKKPTSRSSRAGLQFPVGRIHRQLKQRvSAHGRVGATAAVYTAAILEYLTAEVLEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19557656   67 AGNAARDNKKTRIIPRHLQLAIRNDEELNKLLgRVTIAQGGVLPNIQAVLLPKKTE 122
Cdd:PLN00154  81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLI-KGTIAGGGVIPHIHKSLINKSTK 135
PTZ00252 PTZ00252
histone H2A; Provisional
 10-128 4.62e-32

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 110.05  E-value: 4.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656   10 KARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDN--KKTRIIPRHLQLA 87
Cdd:PTZ00252  10 KASKSGSGRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPRTVTLA 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19557656   88 IRNDEELNKLLGRVTIAQGGVLPNIQAVlLPKKTESHHKAK 128
Cdd:PTZ00252  90 VRHDDDLGSLLKNVTLSRGGVMPSLNKA-LAKKHKSGKKAK 129
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 26-99 2.64e-20

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: 78.43  E-value: 2.64e-20
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19557656  26 FPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLG 99
Cdd:cd22915   2 FPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
PLN00155 PLN00155
histone H2A; Provisional
 1-59 6.69e-19

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 74.36  E-value: 6.69e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19557656    1 MSGRGKqGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYL 59
Cdd:PLN00155   1 MAGRGK-GKTSGKKAVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
Histone_H2A_C pfam16211
C-terminus of histone H2A;
92-126 2.26e-17

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 69.87  E-value: 2.26e-17
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19557656    92 EELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHK 126
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
Histone pfam00125
Core histone H2A/H2B/H3/H4;
4-89 1.54e-14

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 65.15  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656     4 RGKQGGKARAKAKTRSSRAGL---QFPVGRVHRLLRKGNYSE-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRI 79
Cdd:pfam00125  35 RYRPGTVALKEIRKYQSSTDLliyKLPFARVVREVVQSTKTDlRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTL 114

                          90
                  ....*....|
gi 19557656    80 IPRHLQLAIR 89
Cdd:pfam00125 115 TPKDIQLARR 124
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 18-98 3.65e-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: 60.78  E-value: 3.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19557656  18 RSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKL 97
Cdd:cd22913  11 KSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAELWGL 90


                .
gi 19557656  98 L 98
Cdd:cd22913  91 L 91
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
25-97 7.04e-07

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 44.95  E-value: 7.04e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19557656  25 QFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKL 97
Cdd:COG5247  23 RFPIARLKKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
HFD_DRAP1 cd22906
histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, ...
 26-97 2.42e-05

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: 39.81  E-value: 2.42e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19557656  26 FPVGRVHRLLRKgnySERVG---AGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKL 97
Cdd:cd22906   4 FPAARIKKIMQS---DEEVGkvaAAVPVLISKALELFLEDLLTKAAEVAKERNAKTITPSHLKQCVESEEKFDFL 75
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 26-89 1.11e-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: 35.27  E-value: 1.11e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19557656  26 FPVGRVHRLLRKGNYsERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIR 89
Cdd:cd00076   1 LLRSAVARILKSAGF-DSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
26-77 3.84e-03

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 441639  Cd Length: 67  Bit Score: 33.65  E-value: 3.84e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 19557656  26 FPVGRVHRLLRKgNYSERVGAGAPVYLAAVLEYLTAEILELAGNAAR-DNKKT 77
Cdd:COG2036   2 LPVAPVDRIIKK-AGAERVSEDAVEALAEILEEYAEEIAKEAVELAKhAGRKT 53
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 26-89 3.87e-03

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: 33.67  E-value: 3.87e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19557656  26 FPVGRVHRLLRKGNySERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIR 89
Cdd:cd22909   2 LPKAPVKRIIKKAG-AERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVKAEDIELAVK 64
 
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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