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Conserved domains on  [gi|568983379|ref|XP_006517321|]
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core histone macro-H2A.1 isoform X2 [Mus musculus]

Protein Classification

histone H2A family protein( domain architecture ID 12210400)

histone H2A family protein similar to histone 2A (H2A) that is a core component of nucleosome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
H2A smart00414
Histone 2A;
14-119 3.94e-62

Histone 2A;


:

Pssm-ID: 197711  Cd Length: 106  Bit Score: 188.31  E-value: 3.94e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379    14 SRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQ 93
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 568983379    94 LLKGVTIASGGVLPNIHPELLAKKRG 119
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
Macro_SF super family cl00019
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 177-195 7.51e-04

macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


The actual alignment was detected with superfamily member cd02904:

Pssm-ID: 469581  Cd Length: 188  Bit Score: 38.83  E-value: 7.51e-04
                         10
                 ....*....|....*....
gi 568983379 177 TPTDGFTVLSTKSLFLGQK 195
Cdd:cd02904    1 GPGDGFTILSEKKLFLGQK 19
COG1754 super family cl34356
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown];
112-160 1.59e-03

Uncharacterized C-terminal domain of topoisomerase IA [Function unknown];


The actual alignment was detected with superfamily member COG1754:

Pssm-ID: 441360 [Multi-domain]  Cd Length: 892  Bit Score: 38.64  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568983379 112 ELLAKKRGSKG-KLEAIITPPPAKK--AKSPSQKKPVAKKTGGKKGARKSKK 160
Cdd:COG1754  838 ELLAEKRAKGPaKKKKAAKKAAAKKaaAKKTAAKKAAAKKAAAKKAAAKKAA 889
 
Name Accession Description Interval E-value
H2A smart00414
Histone 2A;
14-119 3.94e-62

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 188.31  E-value: 3.94e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379    14 SRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQ 93
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 568983379    94 LLKGVTIASGGVLPNIHPELLAKKRG 119
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PTZ00017 PTZ00017
histone H2A; Provisional
 4-126 3.14e-55

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 171.47  E-value: 3.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379   4 RGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILL 83
Cdd:PTZ00017   9 GGKAGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568983379  84 AVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEA 126
Cdd:PTZ00017  89 AIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQ 131
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 13-101 9.02e-51

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: 158.85  E-value: 9.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379  13 TSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELN 92
Cdd:cd00074    1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                 ....*....
gi 568983379  93 QLLKGVTIA 101
Cdd:cd00074   81 KLFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
4-128 3.80e-44

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 143.46  E-value: 3.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379   4 RGGKKKSTKT--SRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHI 81
Cdd:COG5262    6 KGGKAADARVsqSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568983379  82 LLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAII 128
Cdd:COG5262   86 QLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQEL 132
Histone_H2A_C pfam16211
C-terminus of histone H2A;
89-123 1.39e-14

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 64.48  E-value: 1.39e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568983379   89 EELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGK 123
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 177-195 7.51e-04

macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family are similar to macroH2A, a variant of the major-type core histone H2A, which contains an N-terminal H2A domain and a C-terminal nonhistone macrodomain. Histone macroH2A is enriched on the inactive X chromosome of mammalian female cells. It does not bind poly ADP-ribose, but does bind the monomeric SirT1 metabolite O-acetyl-ADP-ribose (OAADPR) with high affinity through its macrodomain. This family also includes the ADP-ribose binding macrodomain of the macroH2A variant, macroH2A1.1. The macroH2A1.1 isoform inhibits PARP1-dependent DNA-damage induced chromatin dynamics. The putative ADP-ribose binding pocket of the human macroH2A2 macrodomain exhibits marked structural differences compared with the macroH2A1.1 variant.


Pssm-ID: 394875  Cd Length: 188  Bit Score: 38.83  E-value: 7.51e-04
                         10
                 ....*....|....*....
gi 568983379 177 TPTDGFTVLSTKSLFLGQK 195
Cdd:cd02904    1 GPGDGFTILSEKKLFLGQK 19
COG1754 COG1754
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown];
112-160 1.59e-03

Uncharacterized C-terminal domain of topoisomerase IA [Function unknown];


Pssm-ID: 441360 [Multi-domain]  Cd Length: 892  Bit Score: 38.64  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568983379 112 ELLAKKRGSKG-KLEAIITPPPAKK--AKSPSQKKPVAKKTGGKKGARKSKK 160
Cdd:COG1754  838 ELLAEKRAKGPaKKKKAAKKAAAKKaaAKKTAAKKAAAKKAAAKKAAAKKAA 889
 
Name Accession Description Interval E-value
H2A smart00414
Histone 2A;
14-119 3.94e-62

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 188.31  E-value: 3.94e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379    14 SRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQ 93
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 568983379    94 LLKGVTIASGGVLPNIHPELLAKKRG 119
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PTZ00017 PTZ00017
histone H2A; Provisional
 4-126 3.14e-55

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 171.47  E-value: 3.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379   4 RGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILL 83
Cdd:PTZ00017   9 GGKAGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568983379  84 AVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEA 126
Cdd:PTZ00017  89 AIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQ 131
PLN00157 PLN00157
histone H2A; Provisional
 4-123 9.13e-52

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 162.71  E-value: 9.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379   4 RGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILL 83
Cdd:PLN00157   8 KGGGGGKKATSRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568983379  84 AVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGK 123
Cdd:PLN00157  88 AVRNDEELSKLLGGVTIAAGGVLPNIHSVLLPKKSGKSKG 127
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 13-101 9.02e-51

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: 158.85  E-value: 9.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379  13 TSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELN 92
Cdd:cd00074    1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                 ....*....
gi 568983379  93 QLLKGVTIA 101
Cdd:cd00074   81 KLFKGVTIA 89
PLN00156 PLN00156
histone H2AX; Provisional
 2-123 1.57e-46

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 149.73  E-value: 1.57e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379   2 SSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHI 81
Cdd:PLN00156   9 GGRGKPKATKSVSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHI 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568983379  82 LLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGK 123
Cdd:PLN00156  89 QLAVRNDEELSKLLGSVTIAAGGVLPNIHQTLLPKKVGKGKG 130
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
4-128 3.80e-44

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 143.46  E-value: 3.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379   4 RGGKKKSTKT--SRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHI 81
Cdd:COG5262    6 KGGKAADARVsqSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568983379  82 LLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAII 128
Cdd:COG5262   86 QLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQEL 132
PLN00153 PLN00153
histone H2A; Provisional
 1-126 4.81e-43

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 140.62  E-value: 4.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379   1 MSSRGGKKKSTK--TSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTP 78
Cdd:PLN00153   1 MAGRGKGKTSGKkaVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568983379  79 RHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKK-RGSKGKLEA 126
Cdd:PLN00153  81 RHIQLAIRNDEELGKLLGEVTIASGGVLPNIHAVLLPKKtKGGKGEETA 129
PLN00154 PLN00154
histone H2A; Provisional
 7-116 3.16e-31

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 110.42  E-value: 3.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379   7 KKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKY-RIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAV 85
Cdd:PLN00154  23 KDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAI 102

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568983379  86 ANDEELNQLLKGvTIASGGVLPNIHPELLAK 116
Cdd:PLN00154 103 RGDEELDTLIKG-TIAGGGVIPHIHKSLINK 132
PTZ00252 PTZ00252
histone H2A; Provisional
 4-121 2.61e-29

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 105.43  E-value: 2.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379   4 RGGKKKSTK--TSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDN--KKGRVTPR 79
Cdd:PTZ00252   5 KQAKKKASKsgSGRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPR 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568983379  80 HILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSK 121
Cdd:PTZ00252  85 TVTLAVRHDDDLGSLLKNVTLSRGGVMPSLNKALAKKHKSGK 126
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 22-95 5.70e-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: 69.19  E-value: 5.70e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568983379  22 IFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLL 95
Cdd:cd22915    1 LFPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLF 74
Histone_H2A_C pfam16211
C-terminus of histone H2A;
89-123 1.39e-14

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 64.48  E-value: 1.39e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568983379   89 EELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGK 123
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
PLN00155 PLN00155
histone H2A; Provisional
 1-56 3.12e-13

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 61.65  E-value: 3.12e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568983379   1 MSSRGGKKKSTK--TSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYL 56
Cdd:PLN00155   1 MAGRGKGKTSGKkaVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
Histone pfam00125
Core histone H2A/H2B/H3/H4;
2-85 1.06e-11

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 59.37  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379    2 SSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKG-HPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRH 80
Cdd:pfam00125  39 GTVALKEIRKYQSSTDLLIYKLPFARVVREVVQStKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKD 118


                  ....*
gi 568983379   81 ILLAV 85
Cdd:pfam00125 119 IQLAR 123
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 11-91 5.11e-11

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: 56.92  E-value: 5.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379  11 TKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEE 90
Cdd:cd22913    7 LRRSKSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAE 86


                 .
gi 568983379  91 L 91
Cdd:cd22913   87 L 87
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
23-103 5.42e-05

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 41.10  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983379  23 FPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIAS 102
Cdd:COG5247   24 FPIARLKKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFLKNMEQFKN 103


                 .
gi 568983379 103 G 103
Cdd:COG5247  104 R 104
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 177-195 7.51e-04

macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family are similar to macroH2A, a variant of the major-type core histone H2A, which contains an N-terminal H2A domain and a C-terminal nonhistone macrodomain. Histone macroH2A is enriched on the inactive X chromosome of mammalian female cells. It does not bind poly ADP-ribose, but does bind the monomeric SirT1 metabolite O-acetyl-ADP-ribose (OAADPR) with high affinity through its macrodomain. This family also includes the ADP-ribose binding macrodomain of the macroH2A variant, macroH2A1.1. The macroH2A1.1 isoform inhibits PARP1-dependent DNA-damage induced chromatin dynamics. The putative ADP-ribose binding pocket of the human macroH2A2 macrodomain exhibits marked structural differences compared with the macroH2A1.1 variant.


Pssm-ID: 394875  Cd Length: 188  Bit Score: 38.83  E-value: 7.51e-04
                         10
                 ....*....|....*....
gi 568983379 177 TPTDGFTVLSTKSLFLGQK 195
Cdd:cd02904    1 GPGDGFTILSEKKLFLGQK 19
COG1754 COG1754
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown];
112-160 1.59e-03

Uncharacterized C-terminal domain of topoisomerase IA [Function unknown];


Pssm-ID: 441360 [Multi-domain]  Cd Length: 892  Bit Score: 38.64  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568983379 112 ELLAKKRGSKG-KLEAIITPPPAKK--AKSPSQKKPVAKKTGGKKGARKSKK 160
Cdd:COG1754  838 ELLAEKRAKGPaKKKKAAKKAAAKKaaAKKTAAKKAAAKKAAAKKAAAKKAA 889
 
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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