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Conserved domains on  [gi|78706974|ref|NP_001027292|]
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histone H2A [Drosophila melanogaster]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 16-124 5.19e-70

histone H2A; Provisional


:

Pssm-ID: 185399  Cd Length: 134  Bit Score: 206.13  E-value: 5.19e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974   16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:PTZ00017  19 SRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEELNK 98

                         90       100
                 ....*....|....*....|....*....
gi 78706974   96 LLSGVTIAQGGVLPNIQAVLLPKKTEKKA 124
Cdd:PTZ00017  99 LLAGVTIASGGVLPNIHKVLLPKKSKPKQ 127
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 16-124 5.19e-70

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 206.13  E-value: 5.19e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974   16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:PTZ00017  19 SRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEELNK 98

                         90       100
                 ....*....|....*....|....*....
gi 78706974   96 LLSGVTIAQGGVLPNIQAVLLPKKTEKKA 124
Cdd:PTZ00017  99 LLAGVTIASGGVLPNIHKVLLPKKSKPKQ 127
H2A smart00414
Histone 2A;
16-121 2.87e-69

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 202.95  E-value: 2.87e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974     16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 78706974     96 LLSGVTIAQGGVLPNIQAVLLPKKTE 121
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 16-103 3.74e-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: 169.25  E-value: 3.74e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974  16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:cd00074   2 SRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELNK 81


                ....*...
gi 78706974  96 LLSGVTIA 103
Cdd:cd00074  82 LFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
16-124 7.06e-55

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 167.73  E-value: 7.06e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974  16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:COG5262  18 SRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELNK 97

                        90       100
                ....*....|....*....|....*....
gi 78706974  96 LLSGVTIAQGGVLPNIQAVLLPKKTEKKA 124
Cdd:COG5262  98 LLGDVTIAQGGVLPNINPGLLPKSSKKGS 126
Histone_H2A_C pfam16211
C-terminus of histone H2A;
91-124 8.52e-20

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 75.65  E-value: 8.52e-20
                          10        20        30
                  ....*....|....*....|....*....|....
gi 78706974    91 EELNKLLSGVTIAQGGVLPNIQAVLLPKKTEKKA 124
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKK 34
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 16-124 5.19e-70

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 206.13  E-value: 5.19e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974   16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:PTZ00017  19 SRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDEELNK 98

                         90       100
                 ....*....|....*....|....*....
gi 78706974   96 LLSGVTIAQGGVLPNIQAVLLPKKTEKKA 124
Cdd:PTZ00017  99 LLAGVTIASGGVLPNIHKVLLPKKSKPKQ 127
H2A smart00414
Histone 2A;
16-121 2.87e-69

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 202.95  E-value: 2.87e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974     16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 78706974     96 LLSGVTIAQGGVLPNIQAVLLPKKTE 121
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PLN00157 PLN00157
histone H2A; Provisional
 16-124 7.10e-65

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 192.76  E-value: 7.10e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974   16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:PLN00157  18 SRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVRNDEELSK 97

                         90       100
                 ....*....|....*....|....*....
gi 78706974   96 LLSGVTIAQGGVLPNIQAVLLPKKTEKKA 124
Cdd:PLN00157  98 LLGGVTIAAGGVLPNIHSVLLPKKSGKSK 126
PLN00156 PLN00156
histone H2AX; Provisional
 16-122 9.31e-59

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 177.85  E-value: 9.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974   16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:PLN00156  21 SRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHIQLAVRNDEELSK 100

                         90       100
                 ....*....|....*....|....*..
gi 78706974   96 LLSGVTIAQGGVLPNIQAVLLPKKTEK 122
Cdd:PLN00156 101 LLGSVTIAAGGVLPNIHQTLLPKKVGK 127
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 16-103 3.74e-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: 169.25  E-value: 3.74e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974  16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:cd00074   2 SRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELNK 81


                ....*...
gi 78706974  96 LLSGVTIA 103
Cdd:cd00074  82 LFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
16-124 7.06e-55

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 167.73  E-value: 7.06e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974  16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:COG5262  18 SRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELNK 97

                        90       100
                ....*....|....*....|....*....
gi 78706974  96 LLSGVTIAQGGVLPNIQAVLLPKKTEKKA 124
Cdd:COG5262  98 LLGDVTIAQGGVLPNINPGLLPKSSKKGS 126
PLN00153 PLN00153
histone H2A; Provisional
 16-121 7.83e-52

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 159.88  E-value: 7.83e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974   16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:PLN00153  16 SRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVPRHIQLAIRNDEELGK 95

                         90       100
                 ....*....|....*....|....*.
gi 78706974   96 LLSGVTIAQGGVLPNIQAVLLPKKTE 121
Cdd:PLN00153  96 LLGEVTIASGGVLPNIHAVLLPKKTK 121
PLN00154 PLN00154
histone H2A; Provisional
 16-122 4.21e-41

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 132.76  E-value: 4.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974   16 SRSNRAGLQFPVGRIHRLLRKGNYAE-RVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELN 94
Cdd:PLN00154  30 SRSSRAGLQFPVGRIHRQLKQRVSAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 109

                         90       100
                 ....*....|....*....|....*...
gi 78706974   95 KLLSGvTIAQGGVLPNIQAVLLPKKTEK 122
Cdd:PLN00154 110 TLIKG-TIAGGGVIPHIHKSLINKSTKK 136
PTZ00252 PTZ00252
histone H2A; Provisional
 16-124 4.31e-31

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 107.36  E-value: 4.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974   16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDN--KKTRIIPRHLQLAIRNDEEL 93
Cdd:PTZ00252  17 GRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPRTVTLAVRHDDDL 96

                         90       100       110
                 ....*....|....*....|....*....|..
gi 78706974   94 NKLLSGVTIAQGGVLPNIQAVLLPK-KTEKKA 124
Cdd:PTZ00252  97 GSLLKNVTLSRGGVMPSLNKALAKKhKSGKKA 128
Histone_H2A_C pfam16211
C-terminus of histone H2A;
91-124 8.52e-20

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 75.65  E-value: 8.52e-20
                          10        20        30
                  ....*....|....*....|....*....|....
gi 78706974    91 EELNKLLSGVTIAQGGVLPNIQAVLLPKKTEKKA 124
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKK 34
PLN00155 PLN00155
histone H2A; Provisional
 16-58 6.18e-18

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 71.66  E-value: 6.18e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 78706974   16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYL 58
Cdd:PLN00155  16 SRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 25-98 1.09e-17

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: 71.50  E-value: 1.09e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706974  25 FPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLS 98
Cdd:cd22915   2 FPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 16-97 4.74e-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: 63.09  E-value: 4.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974  16 SRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 95
Cdd:cd22913  10 SKSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAELWG 89


                ..
gi 78706974  96 LL 97
Cdd:cd22913  90 LL 91
Histone pfam00125
Core histone H2A/H2B/H3/H4;
16-88 1.99e-13

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 62.07  E-value: 1.99e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706974    16 SRSNRAGLQFPVGRIHRLLRKGNYAE-RVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIR 88
Cdd:pfam00125  51 SSTDLLIYKLPFARVVREVVQSTKTDlRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARR 124
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
24-105 6.69e-07

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 44.57  E-value: 6.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706974  24 QFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLSGVTIA 103
Cdd:COG5247  23 RFPIARLKKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFLKNMEQFK 102


                ..
gi 78706974 104 QG 105
Cdd:COG5247 103 NR 104
HFD_DRAP1 cd22906
histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, ...
 25-96 1.14e-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: 40.58  E-value: 1.14e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78706974  25 FPVGRIHRLLRKGnyaERVG---AGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNKL 96
Cdd:cd22906   4 FPAARIKKIMQSD---EEVGkvaAAVPVLISKALELFLEDLLTKAAEVAKERNAKTITPSHLKQCVESEEKFDFL 75
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 25-88 7.17e-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: 7.17e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706974  25 FPVGRIHRLLRKGNyAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIR 88
Cdd:cd22909   2 LPKAPVKRIIKKAG-AERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVKAEDIELAVK 64
CBFD_NFYB_HMF pfam00808
Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes ...
 25-87 1.69e-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: 1.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706974    25 FPVGRIHRLLRKGNYAERVGAGAPVYLAAVME----YLAAEVLELAGnaaRDNKKTrIIPRHLQLAI 87
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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