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Conserved domains on  [gi|124505075|ref|XP_001351279|]
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histone H2A.Z [Plasmodium falciparum 3D7]

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
 39-157 3.62e-67

histone H2A; Provisional


:

Pssm-ID: 185399  Cd Length: 134  Bit Score: 200.36  E-value: 3.62e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  39 APLSRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDE 118
Cdd:PTZ00017  16 KPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 124505075 119 ELDTLI-KATIAGGGVIPHIHKALMNKVPLPPTAQKKPKK 157
Cdd:PTZ00017  95 ELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQGKKQNKQ 134
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 39-157 3.62e-67

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 200.36  E-value: 3.62e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  39 APLSRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDE 118
Cdd:PTZ00017  16 KPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 124505075 119 ELDTLI-KATIAGGGVIPHIHKALMNKVPLPPTAQKKPKK 157
Cdd:PTZ00017  95 ELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQGKKQNKQ 134
H2A smart00414
Histone 2A;
42-144 1.10e-52

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 162.50  E-value: 1.10e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075    42 SRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEELD 121
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....
gi 124505075   122 TLIKA-TIAGGGVIPHIHKALMNK 144
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPK 103
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 42-128 8.73e-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: 139.59  E-value: 8.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  42 SRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEELD 121
Cdd:cd00074    2 SRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                 ....*..
gi 124505075 122 TLIKATI 128
Cdd:cd00074   81 KLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
42-158 2.71e-43

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 139.61  E-value: 2.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  42 SRASRAGLQFPVGRVHRMLKsRISSDGRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEELD 121
Cdd:COG5262   18 SRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELN 96

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 124505075 122 TLIK-ATIAGGGVIPHIHKALmnkvpLPPTAQKKPKKN 158
Cdd:COG5262   97 KLLGdVTIAQGGVLPNINPGL-----LPKSSKKGSKRS 129
Histone pfam00125
Core histone H2A/H2B/H3/H4;
42-117 2.92e-17

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 72.85  E-value: 2.92e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124505075   42 SRASRAGLQFPVGRVHRMLKSRISSDGRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGD 117
Cdd:pfam00125  51 SSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 39-157 3.62e-67

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 200.36  E-value: 3.62e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  39 APLSRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDE 118
Cdd:PTZ00017  16 KPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 124505075 119 ELDTLI-KATIAGGGVIPHIHKALMNKVPLPPTAQKKPKK 157
Cdd:PTZ00017  95 ELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQGKKQNKQ 134
PLN00154 PLN00154
histone H2A; Provisional
 39-145 2.44e-65

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 195.55  E-value: 2.44e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  39 APLSRASRAGLQFPVGRVHRMLKSRISSDGRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDE 118
Cdd:PLN00154  27 KPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 106

                         90       100
                 ....*....|....*....|....*..
gi 124505075 119 ELDTLIKATIAGGGVIPHIHKALMNKV 145
Cdd:PLN00154 107 ELDTLIKGTIAGGGVIPHIHKSLINKS 133
H2A smart00414
Histone 2A;
42-144 1.10e-52

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 162.50  E-value: 1.10e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075    42 SRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEELD 121
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....
gi 124505075   122 TLIKA-TIAGGGVIPHIHKALMNK 144
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPK 103
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 42-128 8.73e-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: 139.59  E-value: 8.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  42 SRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEELD 121
Cdd:cd00074    2 SRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                 ....*..
gi 124505075 122 TLIKATI 128
Cdd:cd00074   81 KLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
42-158 2.71e-43

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 139.61  E-value: 2.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  42 SRASRAGLQFPVGRVHRMLKsRISSDGRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEELD 121
Cdd:COG5262   18 SRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELN 96

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 124505075 122 TLIK-ATIAGGGVIPHIHKALmnkvpLPPTAQKKPKKN 158
Cdd:COG5262   97 KLLGdVTIAQGGVLPNINPGL-----LPKSSKKGSKRS 129
PLN00157 PLN00157
histone H2A; Provisional
 40-144 4.15e-37

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 123.81  E-value: 4.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  40 PLSRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEE 119
Cdd:PLN00157  16 ATSRSAKAGLQFPVGRIARYLKAGKYAT-RVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVRNDEE 94

                         90       100
                 ....*....|....*....|....*.
gi 124505075 120 LDTLIK-ATIAGGGVIPHIHKALMNK 144
Cdd:PLN00157  95 LSKLLGgVTIAAGGVLPNIHSVLLPK 120
PLN00156 PLN00156
histone H2AX; Provisional
 41-144 3.17e-36

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 122.00  E-value: 3.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  41 LSRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEEL 120
Cdd:PLN00156  20 VSRSSKAGLQFPVGRIARFLKAGKYAE-RVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHIQLAVRNDEEL 98

                         90       100
                 ....*....|....*....|....*
gi 124505075 121 DTLIKA-TIAGGGVIPHIHKALMNK 144
Cdd:PLN00156  99 SKLLGSvTIAAGGVLPNIHQTLLPK 123
PLN00153 PLN00153
histone H2A; Provisional
 41-144 9.10e-32

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 110.19  E-value: 9.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  41 LSRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEEL 120
Cdd:PLN00153  15 VSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVPRHIQLAIRNDEEL 93

                         90       100
                 ....*....|....*....|....*
gi 124505075 121 DTLI-KATIAGGGVIPHIHKALMNK 144
Cdd:PLN00153  94 GKLLgEVTIASGGVLPNIHAVLLPK 118
PTZ00252 PTZ00252
histone H2A; Provisional
 42-144 8.47e-23

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 87.71  E-value: 8.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  42 SRASRAGLQFPVGRVHRMLKsRISSDGRVGSTAAVYAAAILEYLTAEVLELA--GNATKDLKVKRITPRHLQLAIRGDEE 119
Cdd:PTZ00252  17 GRSAKAGLIFPVGRVGSLLR-RGQYARRIGASGAVYMAAVLEYLTAELLELSvkAAAQQAKKPKRLTPRTVTLAVRHDDD 95

                         90       100
                 ....*....|....*....|....*.
gi 124505075 120 LDTLIK-ATIAGGGVIPHIHKALMNK 144
Cdd:PTZ00252  96 LGSLLKnVTLSRGGVMPSLNKALAKK 121
Histone pfam00125
Core histone H2A/H2B/H3/H4;
42-117 2.92e-17

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 72.85  E-value: 2.92e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124505075   42 SRASRAGLQFPVGRVHRMLKSRISSDGRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGD 117
Cdd:pfam00125  51 SSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 42-120 3.74e-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: 61.55  E-value: 3.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  42 SRASRAGLQFPVGRVHR-MLKSRISSdgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEEL 120
Cdd:cd22913   10 SKSARCGLTFSVGRFHRwMVDSRLAK--RIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAEL 87
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 51-120 1.36e-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: 59.56  E-value: 1.36e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  51 FPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEEL 120
Cdd:cd22915    2 FPVDKIHPLLKKDLLVY-KVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVL 70
Histone_H2A_C pfam16211
C-terminus of histone H2A;
118-156 9.76e-09

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 48.30  E-value: 9.76e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 124505075  118 EELDTLIK-ATIAGGGVIPHIHKALmnkvpLPPTAQKKPK 156
Cdd:pfam16211   1 EELNKLLRgVTIAQGGVLPNIHKVL-----LPKKTKKKKK 35
PLN00155 PLN00155
histone H2A; Provisional
 41-85 1.43e-08

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 48.55  E-value: 1.43e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 124505075  41 LSRASRAGLQFPVGRVHRMLKSRISSDgRVGSTAAVYAAAILEYL 85
Cdd:PLN00155  15 VSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYL 58
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
50-123 1.10e-05

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 42.26  E-value: 1.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124505075  50 QFPVGRVHRMLKSRiSSDGRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEELDTL 123
Cdd:COG5247   23 RFPIARLKKIMQLD-EDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
HFD_DRAP1 cd22906
histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, ...
 51-123 3.78e-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: 3.78e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124505075  51 FPVGRVHRMlksrISSD---GRVGSTAAVYAAAILEYLTAEVLELAGNATKDLKVKRITPRHLQLAIRGDEELDTL 123
Cdd:cd22906    4 FPAARIKKI----MQSDeevGKVAAAVPVLISKALELFLEDLLTKAAEVAKERNAKTITPSHLKQCVESEEKFDFL 75
HFD_Dpb3-like cd23645
histone-fold domain found in Schizosaccharomyces pombe DNA polymerase epsilon subunit C (Dpb3) ...
 49-123 7.17e-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: 7.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505075  49 LQFPVGRVHRMLKSriSSDGRVGSTAAVYAAAI-----LEYLTAEVLELAgnatKDLKVKRITPRHLQLAIRGDEELDTL 123
Cdd:cd23645    1 TVLPLARVKRIIKA--DKDVKICSKDAVFLISKatelfIEYLAEQAYELA----KLEKRKTVQYKDLAKAVKRDDNLEFL 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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