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Conserved domains on  [gi|15232536|ref|NP_191019|]
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histone H2A 11 [Arabidopsis thaliana]

Protein Classification

PLN00154 family protein( domain architecture ID 11476415)

PLN00154 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
 1-136 2.75e-78

histone H2A; Provisional


:

Pssm-ID: 177756  Cd Length: 136  Bit Score: 227.52  E-value: 2.75e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536    1 MAGKGGKGLVAAKTMAANKDKDKDKKKPISRSARAGIQFPVGRIHRQLKTRVSAHGRVGATAAVYTASILEYLTAEVLEL 80
Cdd:PLN00154   1 MSGKGGKGLLAAKTTAAAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15232536   81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKTTKE 136
Cdd:PLN00154  81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKSTKK 136
 
Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
 1-136 2.75e-78

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 227.52  E-value: 2.75e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536    1 MAGKGGKGLVAAKTMAANKDKDKDKKKPISRSARAGIQFPVGRIHRQLKTRVSAHGRVGATAAVYTASILEYLTAEVLEL 80
Cdd:PLN00154   1 MSGKGGKGLLAAKTTAAAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15232536   81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKTTKE 136
Cdd:PLN00154  81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKSTKK 136
H2A smart00414
Histone 2A;
30-135 5.94e-55

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 167.51  E-value: 5.94e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536     30 SRSARAGIQFPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 109
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....*..
gi 15232536    110 TLIKG-TIAGGGVIPHIHKSLINKTTK 135
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPKKTG 106
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 30-116 1.56e-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: 140.36  E-value: 1.56e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536  30 SRSARAGIQFPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 109
Cdd:cd00074   2 SRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*..
gi 15232536 110 TLIKGTI 116
Cdd:cd00074  81 KLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
3-136 1.68e-41

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 134.22  E-value: 1.68e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536   3 GKGGKGLVAAKTMaankdkdkdkkkpiSRSARAGIQFPVGRIHRQLKtRVSAHGRVGATAAVYTASILEYLTAEVLELAG 82
Cdd:COG5262   5 GKGGKAADARVSQ--------------SRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAG 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232536  83 NASKDLKVKRITPRHLQLAIRGDEELDTLIKG-TIAGGGVIPHIHKSLINKTTKE 136
Cdd:COG5262  70 NAARDNKKKRIIPRHLQLAIRNDEELNKLLGDvTIAQGGVLPNINPGLLPKSSKK 124
Histone pfam00125
Core histone H2A/H2B/H3/H4;
29-105 1.48e-18

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 75.55  E-value: 1.48e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232536    29 ISRSARAGIQFPVGRIHRQLKTRVSAHGRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGD 105
Cdd:pfam00125  50 QSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
 
Name Accession Description Interval E-value
PLN00154 PLN00154
histone H2A; Provisional
 1-136 2.75e-78

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 227.52  E-value: 2.75e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536    1 MAGKGGKGLVAAKTMAANKDKDKDKKKPISRSARAGIQFPVGRIHRQLKTRVSAHGRVGATAAVYTASILEYLTAEVLEL 80
Cdd:PLN00154   1 MSGKGGKGLLAAKTTAAAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15232536   81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKTTKE 136
Cdd:PLN00154  81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKSTKK 136
PTZ00017 PTZ00017
histone H2A; Provisional
 1-135 2.50e-60

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 181.87  E-value: 2.50e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536    1 MAGKGGKGlvAAKTMAAnkdkdkdkkKPISRSARAGIQFPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYLTAEVLEL 80
Cdd:PTZ00017   1 KGGKGKTG--GGKAGKK---------KPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLEL 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15232536   81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKG-TIAGGGVIPHIHKSLINKTTK 135
Cdd:PTZ00017  69 AGNAAKDNKKKRITPRHIQLAIRNDEELNKLLAGvTIASGGVLPNIHKVLLPKKSK 124
H2A smart00414
Histone 2A;
30-135 5.94e-55

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 167.51  E-value: 5.94e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536     30 SRSARAGIQFPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 109
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....*..
gi 15232536    110 TLIKG-TIAGGGVIPHIHKSLINKTTK 135
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPKKTG 106
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 30-116 1.56e-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: 140.36  E-value: 1.56e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536  30 SRSARAGIQFPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 109
Cdd:cd00074   2 SRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*..
gi 15232536 110 TLIKGTI 116
Cdd:cd00074  81 KLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
3-136 1.68e-41

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 134.22  E-value: 1.68e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536   3 GKGGKGLVAAKTMaankdkdkdkkkpiSRSARAGIQFPVGRIHRQLKtRVSAHGRVGATAAVYTASILEYLTAEVLELAG 82
Cdd:COG5262   5 GKGGKAADARVSQ--------------SRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAG 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232536  83 NASKDLKVKRITPRHLQLAIRGDEELDTLIKG-TIAGGGVIPHIHKSLINKTTKE 136
Cdd:COG5262  70 NAARDNKKKRIIPRHLQLAIRNDEELNKLLGDvTIAQGGVLPNINPGLLPKSSKK 124
PLN00157 PLN00157
histone H2A; Provisional
 28-135 1.46e-38

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 126.89  E-value: 1.46e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536   28 PISRSARAGIQFPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEE 107
Cdd:PLN00157  16 ATSRSAKAGLQFPVGRIARYLKAGKYAT-RVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVRNDEE 94

                         90       100
                 ....*....|....*....|....*....
gi 15232536  108 LDTLIKG-TIAGGGVIPHIHKSLINKTTK 135
Cdd:PLN00157  95 LSKLLGGvTIAAGGVLPNIHSVLLPKKSG 123
PLN00156 PLN00156
histone H2AX; Provisional
 29-134 4.41e-35

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 118.15  E-value: 4.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536   29 ISRSARAGIQFPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 108
Cdd:PLN00156  20 VSRSSKAGLQFPVGRIARFLKAGKYAE-RVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHIQLAVRNDEEL 98

                         90       100
                 ....*....|....*....|....*..
gi 15232536  109 DTLIKG-TIAGGGVIPHIHKSLINKTT 134
Cdd:PLN00156  99 SKLLGSvTIAAGGVLPNIHQTLLPKKV 125
PLN00153 PLN00153
histone H2A; Provisional
 15-135 1.65e-32

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 111.35  E-value: 1.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536   15 MAANKDKDKDKKKPISRSARAGIQFPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRIT 94
Cdd:PLN00153   1 MAGRGKGKTSGKKAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15232536   95 PRHLQLAIRGDEELDTLI-KGTIAGGGVIPHIHKSLINKTTK 135
Cdd:PLN00153  80 PRHIQLAIRNDEELGKLLgEVTIASGGVLPNIHAVLLPKKTK 121
PTZ00252 PTZ00252
histone H2A; Provisional
 30-132 9.61e-22

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 83.86  E-value: 9.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536   30 SRSARAGIQFPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYLTAEVLELAGNAS--KDLKVKRITPRHLQLAIRGDEE 107
Cdd:PTZ00252  17 GRSAKAGLIFPVGRVGSLLRRGQYAR-RIGASGAVYMAAVLEYLTAELLELSVKAAaqQAKKPKRLTPRTVTLAVRHDDD 95

                         90       100
                 ....*....|....*....|....*.
gi 15232536  108 LDTLIKG-TIAGGGVIPHIHKSLINK 132
Cdd:PTZ00252  96 LGSLLKNvTLSRGGVMPSLNKALAKK 121
Histone pfam00125
Core histone H2A/H2B/H3/H4;
29-105 1.48e-18

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 75.55  E-value: 1.48e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232536    29 ISRSARAGIQFPVGRIHRQLKTRVSAHGRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGD 105
Cdd:pfam00125  50 QSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 29-119 3.15e-12

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: 58.85  E-value: 3.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536  29 ISRSARAGIQFPVGRIHRQL-KTRVSAhgRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEE 107
Cdd:cd22913   9 RSKSARCGLTFSVGRFHRWMvDSRLAK--RIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAE 86

                        90
                ....*....|....*....
gi 15232536 108 L-------DTLIKGTIAGG 119
Cdd:cd22913  87 LwgllqpyEHLICGRNASG 105
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 39-108 7.42e-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: 56.86  E-value: 7.42e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232536  39 FPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 108
Cdd:cd22915   2 FPVDKIHPLLKKDLLVY-KVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVL 70
Histone_H2A_C pfam16211
C-terminus of histone H2A;
106-135 1.62e-09

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 49.84  E-value: 1.62e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 15232536   106 EELDTLIKG-TIAGGGVIPHIHKSLINKTTK 135
Cdd:pfam16211   1 EELNKLLRGvTIAQGGVLPNIHKVLLPKKTK 31
PLN00155 PLN00155
histone H2A; Provisional
 15-73 3.54e-09

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 49.71  E-value: 3.54e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15232536   15 MAANKDKDKDKKKPISRSARAGIQFPVGRIHRQLKTRVSAHgRVGATAAVYTASILEYL 73
Cdd:PLN00155   1 MAGRGKGKTSGKKAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYL 58
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
38-111 1.26e-05

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 41.49  E-value: 1.26e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232536  38 QFPVGRIHRQLKTRVSAhGRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTL 111
Cdd:COG5247  23 RFPIARLKKIMQLDEDI-GKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
HFD_DRAP1 cd22906
histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, ...
 39-111 4.78e-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: 36.34  E-value: 4.78e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232536  39 FPVGRIHR--QLKTRVsahGRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTL 111
Cdd:cd22906   4 FPAARIKKimQSDEEV---GKVAAAVPVLISKALELFLEDLLTKAAEVAKERNAKTITPSHLKQCVESEEKFDFL 75
 
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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