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Conserved domains on  [gi|767936779|ref|XP_011542032|]
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core histone macro-H2A.1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 177-367 7.53e-125

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: 357.01  E-value: 7.53e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 177 TPADGFTVLSTKSLFLGQKLNLIHSEISNLAgfeVEAIINPTNADIDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEV 256
Cdd:cd02904    1 GPGDGFTILSEKKLFLGQKLTVVQGDIASIK---ADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 257 AGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSY 336
Cdd:cd02904   78 AGAAISPGHNLPAKFVIHCNSPSWGSDKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNY 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767936779 337 FVSTMSSSIKTVYFVLFDSESIGIYVQEMAK 367
Cdd:cd02904  158 FVSVMSSSLKQIYFVLFDMESIGIYTSELAK 188
H2A smart00414
Histone 2A;
14-119 2.26e-63

Histone 2A;


:

Pssm-ID: 197711  Cd Length: 106  Bit Score: 197.56  E-value: 2.26e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779    14 SRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQ 93
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 767936779    94 LLKGVTIASGGVLPNIHPELLAKKRG 119
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
COG1754 super family cl34356
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown];
112-160 3.37e-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: 39.41  E-value: 3.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767936779 112 ELLAKKRGSKG-KLEAIITPPPAKK--AKSPSQKKPVSKKAGGKKGARKSKK 160
Cdd:COG1754  838 ELLAEKRAKGPaKKKKAAKKAAAKKaaAKKTAAKKAAAKKAAAKKAAAKKAA 889
 
Name Accession Description Interval E-value
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 177-367 7.53e-125

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: 357.01  E-value: 7.53e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 177 TPADGFTVLSTKSLFLGQKLNLIHSEISNLAgfeVEAIINPTNADIDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEV 256
Cdd:cd02904    1 GPGDGFTILSEKKLFLGQKLTVVQGDIASIK---ADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 257 AGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSY 336
Cdd:cd02904   78 AGAAISPGHNLPAKFVIHCNSPSWGSDKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNY 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767936779 337 FVSTMSSSIKTVYFVLFDSESIGIYVQEMAK 367
Cdd:cd02904  158 FVSVMSSSLKQIYFVLFDMESIGIYTSELAK 188
H2A smart00414
Histone 2A;
14-119 2.26e-63

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 197.56  E-value: 2.26e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779    14 SRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQ 93
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 767936779    94 LLKGVTIASGGVLPNIHPELLAKKRG 119
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PTZ00017 PTZ00017
histone H2A; Provisional
 4-126 2.17e-57

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 183.02  E-value: 2.17e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   4 RGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILL 83
Cdd:PTZ00017   9 GGKAGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767936779  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 3.78e-49

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: 3.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779  13 TSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELN 92
Cdd:cd00074    1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                 ....*....
gi 767936779  93 QLLKGVTIA 101
Cdd:cd00074   81 KLFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
4-128 8.70e-45

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 150.78  E-value: 8.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   4 RGGKKKSTKT--SRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHI 81
Cdd:COG5262    6 KGGKAADARVsqSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767936779  82 LLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAII 128
Cdd:COG5262   86 QLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQEL 132
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 215-329 1.52e-35

Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent: in certain cases it is believed to bind non-covalently; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site.


Pssm-ID: 460286  Cd Length: 116  Bit Score: 125.76  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779  215 INPTNADIDLKDDLGNTLEKKGGKEFVEAVLELRKknGPLEVAGAAVSAGHGLPAKFVIHCNSPVW---GADKCEELLEK 291
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWrhgGSHGEEELLES 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767936779  292 TVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLI 329
Cdd:pfam01661  79 CYRNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 210-367 3.81e-35

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 126.44  E-value: 3.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 210 EVEAIINPTNAD------IDLkddlgnTLEKKGGKEFVEAVLELRKKnGPLEVAGAAVSAGHGLPAKFVIHCNSPVW--G 281
Cdd:COG2110   12 DVDAIVNAANSSllggggVAG------AIHRAAGPELLEECRRLCKQ-GGCPTGEAVITPAGNLPAKYVIHTVGPVWrgG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 282 ADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVStmSSSIKTVYFVLFDSESIGIY 361
Cdd:COG2110   85 GPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEE--HPSLEEVRFVLFDEEDYEAY 162


                 ....*.
gi 767936779 362 VQEMAK 367
Cdd:COG2110  163 RRALAR 168
PRK00431 PRK00431
ADP-ribose-binding protein;
209-367 9.40e-34

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 123.03  E-value: 9.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 209 FEVEAIINPTNAdidlkddlgnTLE----------KKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSP 278
Cdd:PRK00431  15 LEVDAIVNAANS----------SLLggggvdgaihRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHTVGP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 279 VW--GADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYfvSTMSSSIKTVYFVLFDSE 356
Cdd:PRK00431  85 VWrgGEDNEAELLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREF--LTRHKSPEEVYFVCYDEE 162

                        170
                 ....*....|.
gi 767936779 357 SIGIYVQEMAK 367
Cdd:PRK00431 163 AYRLYERLLTQ 173
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 205-329 5.94e-26

Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji).


Pssm-ID: 214701  Cd Length: 133  Bit Score: 101.23  E-value: 5.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   205 NLAGFEVEAIINPTNADIDLKDDLGNTLEKKGGKE-FVEAVLELRKknGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGAD 283
Cdd:smart00506   8 DITKPRADAIVNAANSDGAHGGGVAGAIARAAGKAlSKEEVRKLAG--GECPVGTAVVTEGGNLPAKYVIHAVGPRASGH 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 767936779   284 --KCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLI 329
Cdd:smart00506  86 skEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
Histone_H2A_C pfam16211
C-terminus of histone H2A;
89-123 1.25e-14

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 67.17  E-value: 1.25e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767936779   89 EELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGK 123
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
COG1754 COG1754
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown];
112-160 3.37e-03

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


Pssm-ID: 441360 [Multi-domain]  Cd Length: 892  Bit Score: 39.41  E-value: 3.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767936779 112 ELLAKKRGSKG-KLEAIITPPPAKK--AKSPSQKKPVSKKAGGKKGARKSKK 160
Cdd:COG1754  838 ELLAEKRAKGPaKKKKAAKKAAAKKaaAKKTAAKKAAAKKAAAKKAAAKKAA 889
 
Name Accession Description Interval E-value
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 177-367 7.53e-125

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: 357.01  E-value: 7.53e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 177 TPADGFTVLSTKSLFLGQKLNLIHSEISNLAgfeVEAIINPTNADIDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEV 256
Cdd:cd02904    1 GPGDGFTILSEKKLFLGQKLTVVQGDIASIK---ADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 257 AGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSY 336
Cdd:cd02904   78 AGAAISPGHNLPAKFVIHCNSPSWGSDKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNY 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767936779 337 FVSTMSSSIKTVYFVLFDSESIGIYVQEMAK 367
Cdd:cd02904  158 FVSVMSSSLKQIYFVLFDMESIGIYTSELAK 188
H2A smart00414
Histone 2A;
14-119 2.26e-63

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 197.56  E-value: 2.26e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779    14 SRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQ 93
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 767936779    94 LLKGVTIASGGVLPNIHPELLAKKRG 119
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PTZ00017 PTZ00017
histone H2A; Provisional
 4-126 2.17e-57

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 183.02  E-value: 2.17e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   4 RGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILL 83
Cdd:PTZ00017   9 GGKAGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITPRHIQL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767936779  84 AVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEA 126
Cdd:PTZ00017  89 AIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKKQ 131
PLN00157 PLN00157
histone H2A; Provisional
 4-123 5.98e-54

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 174.27  E-value: 5.98e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   4 RGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILL 83
Cdd:PLN00157   8 KGGGGGKKATSRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRIVPRHIQL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767936779  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 3.78e-49

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: 3.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779  13 TSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELN 92
Cdd:cd00074    1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                 ....*....
gi 767936779  93 QLLKGVTIA 101
Cdd:cd00074   81 KLFKGVTIA 89
PLN00156 PLN00156
histone H2AX; Provisional
 2-123 7.76e-48

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 158.98  E-value: 7.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   2 SSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHI 81
Cdd:PLN00156   9 GGRGKPKATKSVSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHI 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767936779  82 LLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGsKGK 123
Cdd:PLN00156  89 QLAVRNDEELSKLLGSVTIAAGGVLPNIHQTLLPKKVG-KGK 129
PLN00153 PLN00153
histone H2A; Provisional
 1-126 4.23e-45

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 151.41  E-value: 4.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   1 MSSRGGKKKSTK--TSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTP 78
Cdd:PLN00153   1 MAGRGKGKTSGKkaVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767936779  79 RHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKK-RGSKGKLEA 126
Cdd:PLN00153  81 RHIQLAIRNDEELGKLLGEVTIASGGVLPNIHAVLLPKKtKGGKGEETA 129
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
4-128 8.70e-45

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 150.78  E-value: 8.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   4 RGGKKKSTKT--SRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHI 81
Cdd:COG5262    6 KGGKAADARVsqSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRHL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767936779  82 LLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAII 128
Cdd:COG5262   86 QLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQEL 132
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 215-329 1.52e-35

Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent: in certain cases it is believed to bind non-covalently; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site.


Pssm-ID: 460286  Cd Length: 116  Bit Score: 125.76  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779  215 INPTNADIDLKDDLGNTLEKKGGKEFVEAVLELRKknGPLEVAGAAVSAGHGLPAKFVIHCNSPVW---GADKCEELLEK 291
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWrhgGSHGEEELLES 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767936779  292 TVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLI 329
Cdd:pfam01661  79 CYRNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 210-367 3.81e-35

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 126.44  E-value: 3.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 210 EVEAIINPTNAD------IDLkddlgnTLEKKGGKEFVEAVLELRKKnGPLEVAGAAVSAGHGLPAKFVIHCNSPVW--G 281
Cdd:COG2110   12 DVDAIVNAANSSllggggVAG------AIHRAAGPELLEECRRLCKQ-GGCPTGEAVITPAGNLPAKYVIHTVGPVWrgG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 282 ADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVStmSSSIKTVYFVLFDSESIGIY 361
Cdd:COG2110   85 GPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEE--HPSLEEVRFVLFDEEDYEAY 162


                 ....*.
gi 767936779 362 VQEMAK 367
Cdd:COG2110  163 RRALAR 168
PRK00431 PRK00431
ADP-ribose-binding protein;
209-367 9.40e-34

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 123.03  E-value: 9.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 209 FEVEAIINPTNAdidlkddlgnTLE----------KKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSP 278
Cdd:PRK00431  15 LEVDAIVNAANS----------SLLggggvdgaihRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHTVGP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 279 VW--GADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYfvSTMSSSIKTVYFVLFDSE 356
Cdd:PRK00431  85 VWrgGEDNEAELLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREF--LTRHKSPEEVYFVCYDEE 162

                        170
                 ....*....|.
gi 767936779 357 SIGIYVQEMAK 367
Cdd:PRK00431 163 AYRLYERLLTQ 173
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 213-332 1.54e-33

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.


Pssm-ID: 394871  Cd Length: 121  Bit Score: 120.97  E-value: 1.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 213 AIINPTNADIDLKDDLGNTLEKKGGKEFVEAVlELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVW-GADKCEELLEK 291
Cdd:cd02749    2 AIVNPANNDLYLGGGVAKAISKKAGGDLQEEC-EERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVAsSKKKTYEPLKK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767936779 292 TVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKA 332
Cdd:cd02749   81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 205-350 4.75e-33

macrodomain, Af1521-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. The macrodomains in this family show similarity to Af1521, a protein from Archaeoglobus fulgidus containing a stand-alone macrodomain. Af1521 binds ADP-ribose and exhibits phosphatase activity toward ADP-ribose-1"-monophosphate (Appr-1"-p). Also included in this family are the N-terminal (or first) macrodomains of BAL (B-aggressive lymphoma) proteins which contain multiple macrodomains, such as the first macrodomain of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


Pssm-ID: 394877 [Multi-domain]  Cd Length: 158  Bit Score: 120.67  E-value: 4.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 205 NLAGFEVEAIINPTNADIDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADK 284
Cdd:cd02907   10 DITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHAVGPRWSGGS 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767936779 285 ---CEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYF 350
Cdd:cd02907   90 keeCEDLLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIKDFSESNSSSSLKEIRL 158
PLN00154 PLN00154
histone H2A; Provisional
 2-116 1.20e-32

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 118.89  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   2 SSRGGKKKSTK---TSRSAKAGVIFPVGRMLRYIKKGHPKY-RIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVT 77
Cdd:PLN00154  15 TAAAAKKDKDKkkpTSRSSRAGLQFPVGRIHRQLKQRVSAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRIT 94

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767936779  78 PRHILLAVANDEELNQLLKGvTIASGGVLPNIHPELLAK 116
Cdd:PLN00154  95 PRHLQLAIRGDEELDTLIKG-TIAGGGVIPHIHKSLINK 132
PTZ00252 PTZ00252
histone H2A; Provisional
 4-121 1.87e-31

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 115.83  E-value: 1.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   4 RGGKKKSTK--TSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDN--KKGRVTPR 79
Cdd:PTZ00252   5 KQAKKKASKsgSGRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPR 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767936779  80 HILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSK 121
Cdd:PTZ00252  85 TVTLAVRHDDDLGSLLKNVTLSRGGVMPSLNKALAKKHKSGK 126
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 195-365 2.14e-29

macrodomain, O-acetyl-ADP-ribose (OAADPr) 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. This family includes eukaryotic macrodomain proteins such as human MacroD1 and MacroD2, and bacterial proteins such as Escherichia coli YmdB; these have been shown to be O-acetyl-ADP-ribose (OAADPr) deacetylases that efficiently catalyze the hydrolysis of OAADPr to produce ADP-ribose and free acetate. OAADPr is a sirtuin reaction product generated from the NAD+-dependent protein deacetylation reactions and has been implicated as a signaling molecule. By acting on mono-ADP-ribosylated substrates, OAADPr deacetylases may reverse cellular ADP-ribosylation.


Pssm-ID: 438955  Cd Length: 166  Bit Score: 111.45  E-value: 2.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 195 KLNLIHSEISNLagfEVEAIINPTNAD------IDlkddlgNTLEKKGGKEFVEavlELRKKNGPLEVAGAAVSAGHGLP 268
Cdd:cd02908    1 KISLWRGDITKL---EVDAIVNAANSSllggggVD------GAIHRAAGPELLE---ECRKLGGVCPTGEAKITPGYNLP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 269 AKFVIHCNSPVW--GADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFvsTMSSSIK 346
Cdd:cd02908   69 AKYVIHTVGPIGegGVEEEPELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWL--EEHDKID 146

                        170
                 ....*....|....*....
gi 767936779 347 TVYFVLFDSESIGIYVQEM 365
Cdd:cd02908  147 RIIFVVFLDEDYKIYEELL 165
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 211-367 9.46e-28

macrodomain, B-aggressive lymphoma (BAL)-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 show similarity to BAL (B-aggressive lymphoma) proteins, which contain one to three macrodomains. Most BAL family macrodomains belong to this family except for the most N-terminal domain in multiple-domain containing proteins. This family includes the second and third macrodomains of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


Pssm-ID: 394874  Cd Length: 175  Bit Score: 107.34  E-value: 9.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 211 VEAIINPTNADIDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEVAgaaVSAGHGLPAKFVIHCNSPVWGADKCEeLLE 290
Cdd:cd02903   22 TDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPASGDVI---VTSGGNLPCKYVYHVVLPHYNPGNEK-TLK 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767936779 291 KTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIYVQEMAK 367
Cdd:cd02903   98 DIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLKEVRFVIFPPETLQAFSDELAK 174
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 205-329 5.94e-26

Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji).


Pssm-ID: 214701  Cd Length: 133  Bit Score: 101.23  E-value: 5.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779   205 NLAGFEVEAIINPTNADIDLKDDLGNTLEKKGGKE-FVEAVLELRKknGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGAD 283
Cdd:smart00506   8 DITKPRADAIVNAANSDGAHGGGVAGAIARAAGKAlSKEEVRKLAG--GECPVGTAVVTEGGNLPAKYVIHAVGPRASGH 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 767936779   284 --KCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLI 329
Cdd:smart00506  86 skEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
194-361 1.97e-21

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 92.35  E-value: 1.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 194 QKLNLIHSEISNLAgfeVEAIINPTNAD-----IDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAA-VSAGHGL 267
Cdd:PRK04143  83 DNIFLWQGDITRLK---VDAIVNAANSRllgcfQPNHDCIDNAIHTFAGVQLRLDCAEIMTEQGRKEATGQAkITRAYNL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 268 PAKFVIHCNSPVWGADKC----EELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSS 343
Cdd:PRK04143 160 PAKYVIHTVGPIIRKQPVspirADLLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKTVLSWLKENPSK 239

                        170
                 ....*....|....*...
gi 767936779 344 siKTVYFVLFDSESIGIY 361
Cdd:PRK04143 240 --LKVVFNVFTDEDLELY 255
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 205-336 1.21e-17

Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein Ttha0132; 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. This family is composed of uncharacterized proteins containing a stand-alone macrodomain, similar to Thermus thermophilus hypothetical protein Ttha0132.


Pssm-ID: 394879  Cd Length: 147  Bit Score: 79.01  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 205 NLAGFEVEAIINPTNADIDLKDDLGNTLEKKGGKE-FVEAVlelrkKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGAD 283
Cdd:cd03330    8 DITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEiEREAM-----RKGPIRVGEAVETGAGKLPAKYVIHAAVMGMPGR 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767936779 284 KCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSY 336
Cdd:cd03330   83 SSEESIRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKC 135
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 206-365 4.40e-16

macrodomain, GDAP2-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. This family contains proteins similar to human GDAP2, the ganglioside induced differentiation associated protein 2, whose gene is expressed at a higher level in differentiated Neuro2a cells compared with non-differentiated cells. GDAP2 contains an N-terminal macrodomain and a C-terminal Sec14p-like lipid binding domain. It is specifically expressed in brain and testis.


Pssm-ID: 394876  Cd Length: 169  Bit Score: 74.96  E-value: 4.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 206 LAGFEVEAIINPTNADIDLKDDLGNTLEKKGGKEFVEavlELRKkNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWgADK- 284
Cdd:cd02905   10 LTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELRE---ELAK-LGGCRTGEAKLTKGYNLPARYVIHTVGPRY-NEKy 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779 285 ---CEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSyFVSTMSSSIKTVYFVLFDSEsIGIY 361
Cdd:cd02905   85 rtaAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRR-FLEKHGSSFEAVVFVVTEEE-METY 162


                 ....
gi 767936779 362 VQEM 365
Cdd:cd02905  163 ERLL 166
PLN00155 PLN00155
histone H2A; Provisional
 1-56 6.43e-15

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 68.58  E-value: 6.43e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767936779   1 MSSRGGKKKSTK--TSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYL 56
Cdd:PLN00155   1 MAGRGKGKTSGKkaVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
Histone_H2A_C pfam16211
C-terminus of histone H2A;
89-123 1.25e-14

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 67.17  E-value: 1.25e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767936779   89 EELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGK 123
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 22-95 2.16e-14

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: 67.65  E-value: 2.16e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767936779  22 IFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLL 95
Cdd:cd22915    1 LFPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLF 74
Histone pfam00125
Core histone H2A/H2B/H3/H4;
2-85 4.17e-12

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 62.84  E-value: 4.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779    2 SSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKG-HPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRH 80
Cdd:pfam00125  39 GTVALKEIRKYQSSTDLLIYKLPFARVVREVVQStKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKD 118


                  ....*
gi 767936779   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 2.39e-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: 56.92  E-value: 2.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779  11 TKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEE 90
Cdd:cd22913    7 LRRSKSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAE 86


                 .
gi 767936779  91 L 91
Cdd:cd22913   87 L 87
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
23-103 3.10e-05

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


Pssm-ID: 227572  Cd Length: 113  Bit Score: 42.64  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936779  23 FPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIAS 102
Cdd:COG5247   24 FPIARLKKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFLKNMEQFKN 103


                 .
gi 767936779 103 G 103
Cdd:COG5247  104 R 104
COG1754 COG1754
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown];
112-160 3.37e-03

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


Pssm-ID: 441360 [Multi-domain]  Cd Length: 892  Bit Score: 39.41  E-value: 3.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767936779 112 ELLAKKRGSKG-KLEAIITPPPAKK--AKSPSQKKPVSKKAGGKKGARKSKK 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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