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Conserved domains on  [gi|15241016|ref|NP_198119|]
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histone H2A 7 [Arabidopsis thaliana]

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

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List of domain hits

 Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 12-140 1.67e-66

histone H2A; Provisional


:

Pssm-ID: 185399  Cd Length: 134  Bit Score: 198.05  E-value: 1.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016   12 RGAGGRKGGDRKKSVSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINP 91
Cdd:PTZ00017   4 KGKTGGGKAGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITP 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15241016   92 RHLCLAIRNDEELGRLLHGVTIASGGVLPNINPVLLPKKSTASSSQAEK 140
Cdd:PTZ00017  84 RHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 12-140 1.67e-66

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 198.05  E-value: 1.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016   12 RGAGGRKGGDRKKSVSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINP 91
Cdd:PTZ00017   4 KGKTGGGKAGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITP 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15241016   92 RHLCLAIRNDEELGRLLHGVTIASGGVLPNINPVLLPKKSTASSSQAEK 140
Cdd:PTZ00017  84 RHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
H2A smart00414
Histone 2A;
27-131 1.53e-62

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 187.16  E-value: 1.53e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016     27 SKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPRHLCLAIRNDEELGR 106
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*
gi 15241016    107 LLHGVTIASGGVLPNINPVLLPKKS 131
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKT 105
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 26-114 3.14e-52

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: 160.39  E-value: 3.14e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016  26 VSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPRHLCLAIRNDEELG 105
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*....
gi 15241016 106 RLLHGVTIA 114
Cdd:cd00074  81 KLFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
13-139 3.27e-51

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 159.64  E-value: 3.27e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016  13 GAGGRKGGDRKKSVSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPR 92
Cdd:COG5262   4 GGKGGKAADARVSQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPR 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15241016  93 HLCLAIRNDEELGRLLHGVTIASGGVLPNINPVLLPKKSTASSSQAE 139
Cdd:COG5262  84 HLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQ 130
Histone_H2A_C pfam16211
C-terminus of histone H2A;
102-136 2.58e-15

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 65.25  E-value: 2.58e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 15241016   102 EELGRLLHGVTIASGGVLPNINPVLLPKKSTASSS 136
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 12-140 1.67e-66

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 198.05  E-value: 1.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016   12 RGAGGRKGGDRKKSVSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINP 91
Cdd:PTZ00017   4 KGKTGGGKAGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITP 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15241016   92 RHLCLAIRNDEELGRLLHGVTIASGGVLPNINPVLLPKKSTASSSQAEK 140
Cdd:PTZ00017  84 RHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQN 132
PLN00157 PLN00157
histone H2A; Provisional
 13-141 1.79e-65

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 195.45  E-value: 1.79e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016   13 GAGGRKGG-DRKKSVSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINP 91
Cdd:PLN00157   3 GRGKRKGGgGGKKATSRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15241016   92 RHLCLAIRNDEELGRLLHGVTIASGGVLPNINPVLLPKKSTASSSQAEKA 141
Cdd:PLN00157  83 RHIQLAVRNDEELSKLLGGVTIAAGGVLPNIHSVLLPKKSGKSKGEPKDP 132
H2A smart00414
Histone 2A;
27-131 1.53e-62

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 187.16  E-value: 1.53e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016     27 SKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPRHLCLAIRNDEELGR 106
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*
gi 15241016    107 LLHGVTIASGGVLPNINPVLLPKKS 131
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKT 105
PLN00156 PLN00156
histone H2AX; Provisional
 10-131 2.45e-56

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 172.84  E-value: 2.45e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016   10 PTRGAGGRKGGDRKKSVSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRI 89
Cdd:PLN00156   4 SGTTKGGRGKPKATKSVSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRI 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15241016   90 NPRHLCLAIRNDEELGRLLHGVTIASGGVLPNINPVLLPKKS 131
Cdd:PLN00156  84 VPRHIQLAVRNDEELSKLLGSVTIAAGGVLPNIHQTLLPKKV 125
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 26-114 3.14e-52

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: 160.39  E-value: 3.14e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016  26 VSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPRHLCLAIRNDEELG 105
Cdd:cd00074   1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                ....*....
gi 15241016 106 RLLHGVTIA 114
Cdd:cd00074  81 KLFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
13-139 3.27e-51

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 159.64  E-value: 3.27e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016  13 GAGGRKGGDRKKSVSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPR 92
Cdd:COG5262   4 GGKGGKAADARVSQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPR 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15241016  93 HLCLAIRNDEELGRLLHGVTIASGGVLPNINPVLLPKKSTASSSQAE 139
Cdd:COG5262  84 HLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQ 130
PLN00153 PLN00153
histone H2A; Provisional
 12-139 7.36e-51

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 158.34  E-value: 7.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016   12 RGAGGRKGgdrKKSVSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINP 91
Cdd:PLN00153   4 RGKGKTSG---KKAVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15241016   92 RHLCLAIRNDEELGRLLHGVTIASGGVLPNINPVLLPKKSTASSSQAE 139
Cdd:PLN00153  81 RHIQLAIRNDEELGKLLGEVTIASGGVLPNIHAVLLPKKTKGGKGEET 128
PLN00154 PLN00154
histone H2A; Provisional
 8-131 3.03e-38

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 126.60  E-value: 3.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016    8 TKPTRGAGGRKGGDRKKSVSKSVKAGLQFPVGRIARYLKKGRYAL-RYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKK 86
Cdd:PLN00154  11 AAKTTAAAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKV 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15241016   87 NRINPRHLCLAIRNDEELGRLLHGvTIASGGVLPNINPVLLPKKS 131
Cdd:PLN00154  91 KRITPRHLQLAIRGDEELDTLIKG-TIAGGGVIPHIHKSLINKST 134
PTZ00252 PTZ00252
histone H2A; Provisional
 22-138 8.47e-30

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 105.04  E-value: 8.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016   22 RKKSVSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDN--KKNRINPRHLCLAIR 99
Cdd:PTZ00252  12 SKSGSGRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPRTVTLAVR 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15241016  100 NDEELGRLLHGVTIASGGVLPNINPVLLPKKSTASSSQA 138
Cdd:PTZ00252  92 HDDDLGSLLKNVTLSRGGVMPSLNKALAKKHKSGKKAKA 130
PLN00155 PLN00155
histone H2A; Provisional
 12-69 1.81e-18

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 73.97  E-value: 1.81e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241016   12 RGAGGRKGgdrKKSVSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYL 69
Cdd:PLN00155   4 RGKGKTSG---KKAVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 36-109 2.64e-16

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: 68.80  E-value: 2.64e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15241016  36 FPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPRHLCLAIRNDEELGRLLH 109
Cdd:cd22915   2 FPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
Histone_H2A_C pfam16211
C-terminus of histone H2A;
102-136 2.58e-15

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 65.25  E-value: 2.58e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 15241016   102 EELGRLLHGVTIASGGVLPNINPVLLPKKSTASSS 136
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 18-109 8.07e-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: 8.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016  18 KGGDRKKSvSKSVKAGLQFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPRHLCLA 97
Cdd:cd22913   2 SSGDQLRR-SKSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYG 80

                        90
                ....*....|..
gi 15241016  98 IRNDEELGRLLH 109
Cdd:cd22913  81 INNDAELWGLLQ 92
Histone pfam00125
Core histone H2A/H2B/H3/H4;
21-99 1.83e-12

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 60.14  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016    21 DRKKSVSKSVKAGLQFPVGRIARYLKKGRYA-LRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPRHLCLAIR 99
Cdd:pfam00125  45 EIRKYQSSTDLLIYKLPFARVVREVVQSTKTdLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARR 124
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
35-116 1.80e-04

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 38.79  E-value: 1.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241016  35 QFPVGRIARYLKKGRYALRYGSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPRHLCLAIRNDEELGRLLHGVTIA 114
Cdd:COG5247  23 RFPIARLKKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFLKNMEQFK 102


                ..
gi 15241016 115 SG 116
Cdd:COG5247 103 NR 104
HFD_DRAP1 cd22906
histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, ...
 36-104 1.73e-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: 35.19  E-value: 1.73e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15241016  36 FPVGRIARYLKK----GRYAlrygSGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRINPRHLCLAIRNDEEL 104
Cdd:cd22906   4 FPAARIKKIMQSdeevGKVA----AAVPVLISKALELFLEDLLTKAAEVAKERNAKTITPSHLKQCVESEEKF 72
 
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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