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Conserved domains on  [gi|67624387|ref|XP_668476|]
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histone H2A variant [Cryptosporidium hominis TU502]

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
 33-151 3.41e-66

histone H2A; Provisional


:

Pssm-ID: 185399  Cd Length: 134  Bit Score: 197.66  E-value: 3.41e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387   33 QPTSRAARAGLQFPVGRIQRMLKHRIPGDcRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 112
Cdd:PTZ00017  16 KPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 67624387  113 ELDSLI-KATIAGGGVIPHIEKSLMGKALIGKKGKKGNMS 151
Cdd:PTZ00017  95 ELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQGKKQNKQ 134
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 33-151 3.41e-66

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 197.66  E-value: 3.41e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387   33 QPTSRAARAGLQFPVGRIQRMLKHRIPGDcRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 112
Cdd:PTZ00017  16 KPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 67624387  113 ELDSLI-KATIAGGGVIPHIEKSLMGKALIGKKGKKGNMS 151
Cdd:PTZ00017  95 ELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQGKKQNKQ 134
H2A smart00414
Histone 2A;
36-139 2.31e-52

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 161.35  E-value: 2.31e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387     36 SRAARAGLQFPVGRIQRMLKHRIPGDcRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 115
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....*
gi 67624387    116 SLIKA-TIAGGGVIPHIEKSLMGKA 139
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPKK 104
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 35-122 6.82e-45

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: 141.90  E-value: 6.82e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387  35 TSRAARAGLQFPVGRIQRMLKHRIPGdCRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 114
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYA-KRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEEL 79


                ....*...
gi 67624387 115 DSLIKATI 122
Cdd:cd00074  80 NKLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
36-147 2.87e-41

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 134.22  E-value: 2.87e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387  36 SRAARAGLQFPVGRIQRMLKHRiPGDCRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 115
Cdd:COG5262  18 SRSAKAGLIFPVGRVKRLLKKG-NYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELN 96

                        90       100       110
                ....*....|....*....|....*....|...
gi 67624387 116 SLIK-ATIAGGGVIPHIEKSLMGKAliGKKGKK 147
Cdd:COG5262  97 KLLGdVTIAQGGVLPNINPGLLPKS--SKKGSK 127
Histone pfam00125
Core histone H2A/H2B/H3/H4;
36-111 1.27e-14

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 65.92  E-value: 1.27e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67624387    36 SRAARAGLQFPVGRIQRMLKHRIPGDCRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGD 111
Cdd:pfam00125  51 SSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 33-151 3.41e-66

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 197.66  E-value: 3.41e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387   33 QPTSRAARAGLQFPVGRIQRMLKHRIPGDcRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 112
Cdd:PTZ00017  16 KPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQLAIRNDE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 67624387  113 ELDSLI-KATIAGGGVIPHIEKSLMGKALIGKKGKKGNMS 151
Cdd:PTZ00017  95 ELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQGKKQNKQ 134
PLN00154 PLN00154
histone H2A; Provisional
 33-139 1.52e-58

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 178.21  E-value: 1.52e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387   33 QPTSRAARAGLQFPVGRIQRMLKHRIPGDCRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 112
Cdd:PLN00154  27 KPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 106

                         90       100
                 ....*....|....*....|....*..
gi 67624387  113 ELDSLIKATIAGGGVIPHIEKSLMGKA 139
Cdd:PLN00154 107 ELDTLIKGTIAGGGVIPHIHKSLINKS 133
H2A smart00414
Histone 2A;
36-139 2.31e-52

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 161.35  E-value: 2.31e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387     36 SRAARAGLQFPVGRIQRMLKHRIPGDcRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 115
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79

                           90       100
                   ....*....|....*....|....*
gi 67624387    116 SLIKA-TIAGGGVIPHIEKSLMGKA 139
Cdd:smart00414  80 KLLKGvTIAQGGVLPNIHKVLLPKK 104
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 35-122 6.82e-45

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: 141.90  E-value: 6.82e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387  35 TSRAARAGLQFPVGRIQRMLKHRIPGdCRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 114
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYA-KRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEEL 79


                ....*...
gi 67624387 115 DSLIKATI 122
Cdd:cd00074  80 NKLFKGVT 87
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
36-147 2.87e-41

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 134.22  E-value: 2.87e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387  36 SRAARAGLQFPVGRIQRMLKHRiPGDCRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 115
Cdd:COG5262  18 SRSAKAGLIFPVGRVKRLLKKG-NYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHLQLAIRNDEELN 96

                        90       100       110
                ....*....|....*....|....*....|...
gi 67624387 116 SLIK-ATIAGGGVIPHIEKSLMGKAliGKKGKK 147
Cdd:COG5262  97 KLLGdVTIAQGGVLPNINPGLLPKS--SKKGSK 127
PLN00157 PLN00157
histone H2A; Provisional
 33-146 4.27e-37

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 123.81  E-value: 4.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387   33 QPTSRAARAGLQFPVGRIQRMLKHRIPGDcRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 112
Cdd:PLN00157  15 KATSRSAKAGLQFPVGRIARYLKAGKYAT-RVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQLAVRNDE 93

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 67624387  113 ELDSLIK-ATIAGGGVIPHIEKSLMGKALIGKKGK 146
Cdd:PLN00157  94 ELSKLLGgVTIAAGGVLPNIHSVLLPKKSGKSKGE 128
PLN00156 PLN00156
histone H2AX; Provisional
 35-151 5.52e-35

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 118.53  E-value: 5.52e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387   35 TSRAARAGLQFPVGRIQRMLKHRIPGDcRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 114
Cdd:PLN00156  20 VSRSSKAGLQFPVGRIARFLKAGKYAE-RVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHIQLAVRNDEEL 98

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 67624387  115 DSLIKA-TIAGGGVIPHIEKSLMGKALIGKKGKKGNMS 151
Cdd:PLN00156  99 SKLLGSvTIAAGGVLPNIHQTLLPKKVGKGKGDIGSAS 136
PLN00153 PLN00153
histone H2A; Provisional
 33-147 1.13e-31

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 109.81  E-value: 1.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387   33 QPTSRAARAGLQFPVGRIQRMLKHRIPGDcRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDE 112
Cdd:PLN00153  13 KAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVPRHIQLAIRNDE 91

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 67624387  113 ELDSLI-KATIAGGGVIPHIEKSLMGKALIGKKGKK 147
Cdd:PLN00153  92 ELGKLLgEVTIASGGVLPNIHAVLLPKKTKGGKGEE 127
PTZ00252 PTZ00252
histone H2A; Provisional
 35-146 4.51e-24

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 90.41  E-value: 4.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387   35 TSRAARAGLQFPVGRIQRMLKHRIPGDcRVGSTASVYAAAILEYLTAEVLELAGNAS--KDLKVKRITPRHLQLAIRGDE 112
Cdd:PTZ00252  16 SGRSAKAGLIFPVGRVGSLLRRGQYAR-RIGASGAVYMAAVLEYLTAELLELSVKAAaqQAKKPKRLTPRTVTLAVRHDD 94

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 67624387  113 ELDSLIK-ATIAGGGVIPHIEKSLMGKALIGKKGK 146
Cdd:PTZ00252  95 DLGSLLKnVTLSRGGVMPSLNKALAKKHKSGKKAK 129
Histone pfam00125
Core histone H2A/H2B/H3/H4;
36-111 1.27e-14

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 65.92  E-value: 1.27e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67624387    36 SRAARAGLQFPVGRIQRMLKHRIPGDCRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGD 111
Cdd:pfam00125  51 SSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 45-117 7.16e-13

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: 59.94  E-value: 7.16e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67624387  45 FPVGRIQRMLKhRIPGDCRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSL 117
Cdd:cd22915   2 FPVDKIHPLLK-KDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDL 73
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 35-114 1.87e-10

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: 54.61  E-value: 1.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67624387  35 TSRAARAGLQFPVGRIQR-MLKHRIpgDCRVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEE 113
Cdd:cd22913   9 RSKSARCGLTFSVGRFHRwMVDSRL--AKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAE 86


                .
gi 67624387 114 L 114
Cdd:cd22913  87 L 87
Histone_H2A_C pfam16211
C-terminus of histone H2A;
112-147 3.53e-08

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 46.76  E-value: 3.53e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 67624387   112 EELDSLIK-ATIAGGGVIPHIEKSLMGKaligKKGKK 147
Cdd:pfam16211   1 EELNKLLRgVTIAQGGVLPNIHKVLLPK----KTKKK 33
PLN00155 PLN00155
histone H2A; Provisional
 33-79 3.61e-08

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 47.39  E-value: 3.61e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 67624387   33 QPTSRAARAGLQFPVGRIQRMLKHRIPGDcRVGSTASVYAAAILEYL 79
Cdd:PLN00155  13 KAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYL 58
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
44-117 3.43e-04

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 38.02  E-value: 3.43e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67624387  44 QFPVGRIQRMLKhrIPGDC-RVGSTASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSL 117
Cdd:COG5247  23 RFPIARLKKIMQ--LDEDIgKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
HFD_DRAP1 cd22906
histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, ...
 45-117 6.12e-03

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: 33.65  E-value: 6.12e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67624387  45 FPVGRIQRMlkhrIPGDCRVG---STASVYAAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSL 117
Cdd:cd22906   4 FPAARIKKI----MQSDEEVGkvaAAVPVLISKALELFLEDLLTKAAEVAKERNAKTITPSHLKQCVESEEKFDFL 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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