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Conserved domains on  [gi|998528101|ref|XP_015466415|]
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Histone H2A.Z [Debaryomyces fabryi]

Protein Classification

histone H2A family protein( domain architecture ID 1000142)

histone H2A family protein may be 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 super family cl30549
histone H2A; Provisional
 17-132 2.12e-56

histone H2A; Provisional


The actual alignment was detected with superfamily member PTZ00017:

Pssm-ID: 185399  Cd Length: 134  Bit Score: 171.85  E-value: 2.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  17 TAKSTTSHSARAGLQFPVGRIKRYLKRTAQNKiRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIR 96
Cdd:PTZ00017  13 GKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIR 91

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 998528101  97 GDEELDNLI-KATIAFGGVLPHINKALLLKVEKKKQK 132
Cdd:PTZ00017  92 NDEELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQG 128
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 17-132 2.12e-56

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 171.85  E-value: 2.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  17 TAKSTTSHSARAGLQFPVGRIKRYLKRTAQNKiRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIR 96
Cdd:PTZ00017  13 GKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIR 91

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 998528101  97 GDEELDNLI-KATIAFGGVLPHINKALLLKVEKKKQK 132
Cdd:PTZ00017  92 NDEELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQG 128
H2A smart00414
Histone 2A;
23-128 7.62e-54

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 164.43  E-value: 7.62e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101    23 SHSARAGLQFPVGRIKRYLKRTAQNKiRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEELD 102
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....*..
gi 998528101   103 NLIKA-TIAFGGVLPHINKALLLKVEK 128
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPKKTG 106
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
18-132 1.20e-50

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 157.33  E-value: 1.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  18 AKSTTSHSARAGLQFPVGRIKRYLKRTaQNKIRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRG 97
Cdd:COG5262   13 ARVSQSRSAKAGLIFPVGRVKRLLKKG-NYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRN 91

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 998528101  98 DEELDNLIK-ATIAFGGVLPHINKALLLKVEKKKQK 132
Cdd:COG5262   92 DEELNKLLGdVTIAQGGVLPNINPGLLPKSSKKGSK 127
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 22-109 8.80e-44

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: 138.43  E-value: 8.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  22 TSHSARAGLQFPVGRIKRYLKRTAQNKiRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEEL 101
Cdd:cd00074    1 QSRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEEL 79


                 ....*...
gi 998528101 102 DNLIKATI 109
Cdd:cd00074   80 NKLFKGVT 87
Histone pfam00125
Core histone H2A/H2B/H3/H4;
23-98 3.57e-14

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 63.99  E-value: 3.57e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998528101   23 SHSARAGLQFPVGRIKRYLKRTAQNKIRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGD 98
Cdd:pfam00125  51 SSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 17-132 2.12e-56

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 171.85  E-value: 2.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  17 TAKSTTSHSARAGLQFPVGRIKRYLKRTAQNKiRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIR 96
Cdd:PTZ00017  13 GKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIR 91

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 998528101  97 GDEELDNLI-KATIAFGGVLPHINKALLLKVEKKKQK 132
Cdd:PTZ00017  92 NDEELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQG 128
H2A smart00414
Histone 2A;
23-128 7.62e-54

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 164.43  E-value: 7.62e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101    23 SHSARAGLQFPVGRIKRYLKRTAQNKiRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEELD 102
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....*..
gi 998528101   103 NLIKA-TIAFGGVLPHINKALLLKVEK 128
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPKKTG 106
PLN00154 PLN00154
histone H2A; Provisional
 19-129 7.40e-52

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 160.49  E-value: 7.40e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  19 KSTTSHSARAGLQFPVGRIKRYLKRTAQNKIRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGD 98
Cdd:PLN00154  26 KKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGD 105

                         90       100       110
                 ....*....|....*....|....*....|.
gi 998528101  99 EELDNLIKATIAFGGVLPHINKALLLKVEKK 129
Cdd:PLN00154 106 EELDTLIKGTIAGGGVIPHIHKSLINKSTKK 136
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
18-132 1.20e-50

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 157.33  E-value: 1.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  18 AKSTTSHSARAGLQFPVGRIKRYLKRTaQNKIRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRG 97
Cdd:COG5262   13 ARVSQSRSAKAGLIFPVGRVKRLLKKG-NYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRN 91

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 998528101  98 DEELDNLIK-ATIAFGGVLPHINKALLLKVEKKKQK 132
Cdd:COG5262   92 DEELNKLLGdVTIAQGGVLPNINPGLLPKSSKKGSK 127
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 22-109 8.80e-44

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: 138.43  E-value: 8.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  22 TSHSARAGLQFPVGRIKRYLKRTAQNKiRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEEL 101
Cdd:cd00074    1 QSRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEEL 79


                 ....*...
gi 998528101 102 DNLIKATI 109
Cdd:cd00074   80 NKLFKGVT 87
PLN00157 PLN00157
histone H2A; Provisional
 17-132 2.46e-41

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 133.82  E-value: 2.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  17 TAKSTTSHSARAGLQFPVGRIKRYLKRtAQNKIRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIR 96
Cdd:PLN00157  12 GGKKATSRSAKAGLQFPVGRIARYLKA-GKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVR 90

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 998528101  97 GDEELDNLIK-ATIAFGGVLPHINKALLLKVEKKKQK 132
Cdd:PLN00157  91 NDEELSKLLGgVTIAAGGVLPNIHSVLLPKKSGKSKG 127
PLN00156 PLN00156
histone H2AX; Provisional
 18-125 9.04e-38

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 125.08  E-value: 9.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  18 AKSTTSHSARAGLQFPVGRIKRYLKrTAQNKIRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRG 97
Cdd:PLN00156  16 ATKSVSRSSKAGLQFPVGRIARFLK-AGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHIQLAVRN 94

                         90       100
                 ....*....|....*....|....*....
gi 998528101  98 DEELDNLIKA-TIAFGGVLPHINKALLLK 125
Cdd:PLN00156  95 DEELSKLLGSvTIAAGGVLPNIHQTLLPK 123
PLN00153 PLN00153
histone H2A; Provisional
 17-128 3.36e-34

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 115.59  E-value: 3.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  17 TAKSTTSHSARAGLQFPVGRIKRYLKRTAQNKiRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIR 96
Cdd:PLN00153  10 SGKKAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVPRHIQLAIR 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 998528101  97 GDEELDNLI-KATIAFGGVLPHINKALLLKVEK 128
Cdd:PLN00153  89 NDEELGKLLgEVTIASGGVLPNIHAVLLPKKTK 121
PTZ00252 PTZ00252
histone H2A; Provisional
 19-131 3.22e-25

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 92.72  E-value: 3.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  19 KSTTSHSARAGLQFPVGRIKRYLKRtAQNKIRVGSKSAIYLTAVLEYLTAEVLELAGNAA--KDLKVKRITPRHLQLAIR 96
Cdd:PTZ00252  13 KSGSGRSAKAGLIFPVGRVGSLLRR-GQYARRIGASGAVYMAAVLEYLTAELLELSVKAAaqQAKKPKRLTPRTVTLAVR 91

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 998528101  97 GDEELDNLIK-ATIAFGGVLPHINKALLLKVEKKKQ 131
Cdd:PTZ00252  92 HDDDLGSLLKnVTLSRGGVMPSLNKALAKKHKSGKK 127
Histone pfam00125
Core histone H2A/H2B/H3/H4;
23-98 3.57e-14

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 63.99  E-value: 3.57e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998528101   23 SHSARAGLQFPVGRIKRYLKRTAQNKIRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGD 98
Cdd:pfam00125  51 SSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 22-101 7.69e-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: 60.01  E-value: 7.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998528101  22 TSHSARAGLQFPVGRIKRYL--KRTAqnkIRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDE 99
Cdd:cd22913    9 RSKSARCGLTFSVGRFHRWMvdSRLA---KRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDA 85


                 ..
gi 998528101 100 EL 101
Cdd:cd22913   86 EL 87
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 32-104 1.42e-12

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: 58.79  E-value: 1.42e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 998528101  32 FPVGRIKRYLKRTAQNKiRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEELDNL 104
Cdd:cd22915    2 FPVDKIHPLLKKDLLVY-KVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDL 73
PLN00155 PLN00155
histone H2A; Provisional
 17-66 5.97e-11

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 53.94  E-value: 5.97e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 998528101  17 TAKSTTSHSARAGLQFPVGRIKRYLKRTAQNKiRVGSKSAIYLTAVLEYL 66
Cdd:PLN00155  10 SGKKAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYL 58
Histone_H2A_C pfam16211
C-terminus of histone H2A;
99-132 6.49e-10

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 50.61  E-value: 6.49e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 998528101   99 EELDNLIK-ATIAFGGVLPHINKALLLKVEKKKQK 132
Cdd:pfam16211   1 EELNKLLRgVTIAQGGVLPNIHKVLLPKKTKKKKK 35
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
31-104 3.97e-05

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 40.33  E-value: 3.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998528101  31 QFPVGRIKRYLKrTAQNKIRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEELDNL 104
Cdd:COG5247   23 RFPIARLKKIMQ-LDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
 
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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