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Conserved domains on  [gi|1938877867]
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Chain g, Histone H2A type 1-B/E

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
 4-133 6.99e-70

histone H2A; Provisional


:

Pssm-ID: 185399  Cd Length: 134  Bit Score: 206.13  E-value: 6.99e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   4 MSGRGKQGGKARAKAK--TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTR 81
Cdd:PTZ00017    1 KGGKGKTGGGKAGKKKpvSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1938877867  82 IIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 133
Cdd:PTZ00017   81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 4-133 6.99e-70

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 206.13  E-value: 6.99e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   4 MSGRGKQGGKARAKAK--TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTR 81
Cdd:PTZ00017    1 KGGKGKTGGGKAGKKKpvSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1938877867  82 IIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 133
Cdd:PTZ00017   81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
H2A smart00414
Histone 2A;
20-125 9.12e-67

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 197.17  E-value: 9.12e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   20 TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 99
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 1938877867  100 LLGRVTIAQGGVLPNIQAVLLPKKTE 125
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 19-107 2.06e-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: 170.41  E-value: 2.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867  19 KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN 98
Cdd:cd00074     1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                  ....*....
gi 1938877867  99 KLLGRVTIA 107
Cdd:cd00074    81 KLFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
3-130 2.18e-53

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 164.26  E-value: 2.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   3 HMSGrGKQGGKARAKA-KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTR 81
Cdd:COG5262     1 VVSG-GKGGKAADARVsQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1938877867  82 IIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKA 130
Cdd:COG5262    80 IIPRHLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKR 128
Histone_H2A_C pfam16211
C-terminus of histone H2A;
95-129 2.71e-17

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 69.87  E-value: 2.71e-17
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1938877867  95 EELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHK 129
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 4-133 6.99e-70

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 206.13  E-value: 6.99e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   4 MSGRGKQGGKARAKAK--TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTR 81
Cdd:PTZ00017    1 KGGKGKTGGGKAGKKKpvSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1938877867  82 IIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 133
Cdd:PTZ00017   81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
H2A smart00414
Histone 2A;
20-125 9.12e-67

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 197.17  E-value: 9.12e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   20 TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 99
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 1938877867  100 LLGRVTIAQGGVLPNIQAVLLPKKTE 125
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PLN00157 PLN00157
histone H2A; Provisional
 4-133 1.03e-65

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 195.45  E-value: 1.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   4 MSGRGKQ-GGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRI 82
Cdd:PLN00157    1 MSGRGKRkGGGGGKKATSRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1938877867  83 IPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 133
Cdd:PLN00157   81 VPRHIQLAVRNDEELSKLLGGVTIAAGGVLPNIHSVLLPKKSGKSKGEPKD 131
PLN00156 PLN00156
histone H2AX; Provisional
 2-124 9.66e-58

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 175.54  E-value: 9.66e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   2 SHMSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTR 81
Cdd:PLN00156    3 GSGTTKGGRGKPKATKSVSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNR 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1938877867  82 IIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKT 124
Cdd:PLN00156   83 IVPRHIQLAVRNDEELSKLLGSVTIAAGGVLPNIHQTLLPKKV 125
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 19-107 2.06e-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: 170.41  E-value: 2.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867  19 KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN 98
Cdd:cd00074     1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                  ....*....
gi 1938877867  99 KLLGRVTIA 107
Cdd:cd00074    81 KLFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
3-130 2.18e-53

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 164.26  E-value: 2.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   3 HMSGrGKQGGKARAKA-KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTR 81
Cdd:COG5262     1 VVSG-GKGGKAADARVsQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1938877867  82 IIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKA 130
Cdd:COG5262    80 IIPRHLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKR 128
PLN00153 PLN00153
histone H2A; Provisional
 4-125 2.84e-53

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 163.74  E-value: 2.84e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   4 MSGRGKqGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRII 83
Cdd:PLN00153    1 MAGRGK-GKTSGKKAVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1938877867  84 PRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTE 125
Cdd:PLN00153   80 PRHIQLAIRNDEELGKLLGEVTIASGGVLPNIHAVLLPKKTK 121
PLN00154 PLN00154
histone H2A; Provisional
 1-125 8.08e-39

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 127.37  E-value: 8.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   1 GSHMSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKG-NYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKK 79
Cdd:PLN00154   11 AAKTTAAAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRvSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKV 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1938877867  80 TRIIPRHLQLAIRNDEELNKLLgRVTIAQGGVLPNIQAVLLPKKTE 125
Cdd:PLN00154   91 KRITPRHLQLAIRGDEELDTLI-KGTIAGGGVIPHIHKSLINKSTK 135
PTZ00252 PTZ00252
histone H2A; Provisional
 13-131 4.57e-32

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 110.44  E-value: 4.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867  13 KARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDN--KKTRIIPRHLQLA 90
Cdd:PTZ00252   10 KASKSGSGRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPRTVTLA 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1938877867  91 IRNDEELNKLLGRVTIAQGGVLPNIQAVlLPKKTESHHKAK 131
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; ...
 29-102 1.76e-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: 78.82  E-value: 1.76e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1938877867  29 FPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLG 102
Cdd:cd22915     2 FPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
PLN00155 PLN00155
histone H2A; Provisional
 4-62 7.13e-19

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 74.36  E-value: 7.13e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1938877867   4 MSGRGKqGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYL 62
Cdd:PLN00155    1 MAGRGK-GKTSGKKAVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
Histone_H2A_C pfam16211
C-terminus of histone H2A;
95-129 2.71e-17

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 69.87  E-value: 2.71e-17
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1938877867  95 EELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHK 129
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
Histone pfam00125
Core histone H2A/H2B/H3/H4;
7-92 1.04e-14

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 65.53  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867   7 RGKQGGKARAKAKTRSSRAGL---QFPVGRVHRLLRKGNYSE-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRI 82
Cdd:pfam00125  35 RYRPGTVALKEIRKYQSSTDLliyKLPFARVVREVVQSTKTDlRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTL 114

                          90
                  ....*....|
gi 1938877867  83 IPRHLQLAIR 92
Cdd:pfam00125 115 TPKDIQLARR 124
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 21-101 4.99e-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: 4.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938877867  21 RSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKL 100
Cdd:cd22913    11 KSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAELWGL 90


                  .
gi 1938877867 101 L 101
Cdd:cd22913    91 L 91
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
28-100 5.81e-07

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 44.95  E-value: 5.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1938877867  28 QFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKL 100
Cdd:COG5247    23 RFPIARLKKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
HFD_DRAP1 cd22906
histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, ...
 29-100 1.92e-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: 40.20  E-value: 1.92e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1938877867  29 FPVGRVHRLLRKgnySERVG---AGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKL 100
Cdd:cd22906     4 FPAARIKKIMQS---DEEVGkvaAAVPVLISKALELFLEDLLTKAAEVAKERNAKTITPSHLKQCVESEEKFDFL 75
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 29-92 1.02e-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: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1938877867  29 FPVGRVHRLLRKGNYsERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIR 92
Cdd:cd00076     1 LLRSAVARILKSAGF-DSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 29-92 2.69e-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: 34.06  E-value: 2.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1938877867  29 FPVGRVHRLLRKGNySERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIR 92
Cdd:cd22909     2 LPKAPVKRIIKKAG-AERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVKAEDIELAVK 64
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
29-80 2.75e-03

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


Pssm-ID: 441639  Cd Length: 67  Bit Score: 34.04  E-value: 2.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1938877867  29 FPVGRVHRLLRKgNYSERVGAGAPVYLAAVLEYLTAEILELAGNAAR-DNKKT 80
Cdd:COG2036     2 LPVAPVDRIIKK-AGAERVSEDAVEALAEILEEYAEEIAKEAVELAKhAGRKT 53
CBFD_NFYB_HMF pfam00808
Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes ...
 29-91 9.67e-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: 32.58  E-value: 9.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938877867  29 FPVGRVHRLLRKGNYSERVGAGAPVYLAAVLE----YLTAEILELAGnaaRDNKKTrIIPRHLQLAI 91
Cdd:pfam00808   3 LPIARVKRIMKSDPDAGRISQDAKELIAECVEefieFVASEAAEICN---KAGRKT-INPEHIKQAV 65
 
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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