|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00017 |
PTZ00017 |
histone H2A; Provisional |
1-138 |
2.17e-68 |
|
histone H2A; Provisional
Pssm-ID: 185399 Cd Length: 134 Bit Score: 202.67 E-value: 2.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 1 MSGRGKKLAAPQKSKTSVSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLR 80
Cdd:PTZ00017 1 KGGKGKTGGGKAGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1226253483 81 IAPRHIQLAVRNDEELNTLLGGVTISEGGVLPNIQAVLLPKKTKaarePNAGTEAQSQ 138
Cdd:PTZ00017 81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSK----PKQGKKQNKQ 134
|
|
| H2A |
smart00414 |
Histone 2A; |
19-124 |
4.07e-63 |
|
Histone 2A;
Pssm-ID: 197711 Cd Length: 106 Bit Score: 188.31 E-value: 4.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 19 SRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLRIAPRHIQLAVRNDEELNT 98
Cdd:smart00414 1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80
|
90 100
....*....|....*....|....*.
gi 1226253483 99 LLGGVTISEGGVLPNIQAVLLPKKTK 124
Cdd:smart00414 81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
|
|
| HFD_H2A |
cd00074 |
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ... |
18-106 |
2.70e-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: 2.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 18 VSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLRIAPRHIQLAVRNDEELN 97
Cdd:cd00074 1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80
|
....*....
gi 1226253483 98 TLLGGVTIS 106
Cdd:cd00074 81 KLFKGVTIA 89
|
|
| HTA1 |
COG5262 |
Histone H2A [Chromatin structure and dynamics]; |
3-130 |
3.35e-51 |
|
Histone H2A [Chromatin structure and dynamics];
Pssm-ID: 227587 [Multi-domain] Cd Length: 132 Bit Score: 158.87 E-value: 3.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 3 GRGKKLAAPqksKTSVSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLRIA 82
Cdd:COG5262 5 GKGGKAADA---RVSQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRII 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1226253483 83 PRHIQLAVRNDEELNTLLGGVTISEGGVLPNIQAVLLPKKTKAAREPN 130
Cdd:COG5262 82 PRHLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRS 129
|
|
| Histone_H2A_C |
pfam16211 |
C-terminus of histone H2A; |
94-126 |
3.04e-17 |
|
C-terminus of histone H2A;
Pssm-ID: 465070 Cd Length: 35 Bit Score: 69.87 E-value: 3.04e-17
10 20 30
....*....|....*....|....*....|...
gi 1226253483 94 EELNTLLGGVTISEGGVLPNIQAVLLPKKTKAA 126
Cdd:pfam16211 1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKK 33
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00017 |
PTZ00017 |
histone H2A; Provisional |
1-138 |
2.17e-68 |
|
histone H2A; Provisional
Pssm-ID: 185399 Cd Length: 134 Bit Score: 202.67 E-value: 2.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 1 MSGRGKKLAAPQKSKTSVSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLR 80
Cdd:PTZ00017 1 KGGKGKTGGGKAGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1226253483 81 IAPRHIQLAVRNDEELNTLLGGVTISEGGVLPNIQAVLLPKKTKaarePNAGTEAQSQ 138
Cdd:PTZ00017 81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSK----PKQGKKQNKQ 134
|
|
| PLN00157 |
PLN00157 |
histone H2A; Provisional |
1-129 |
9.05e-64 |
|
histone H2A; Provisional
Pssm-ID: 177758 Cd Length: 132 Bit Score: 190.83 E-value: 9.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 1 MSGRGKKLAAPQKSKtSVSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLR 80
Cdd:PLN00157 1 MSGRGKRKGGGGGKK-ATSRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1226253483 81 IAPRHIQLAVRNDEELNTLLGGVTISEGGVLPNIQAVLLPKKTKAAREP 129
Cdd:PLN00157 80 IVPRHIQLAVRNDEELSKLLGGVTIAAGGVLPNIHSVLLPKKSGKSKGE 128
|
|
| H2A |
smart00414 |
Histone 2A; |
19-124 |
4.07e-63 |
|
Histone 2A;
Pssm-ID: 197711 Cd Length: 106 Bit Score: 188.31 E-value: 4.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 19 SRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLRIAPRHIQLAVRNDEELNT 98
Cdd:smart00414 1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80
|
90 100
....*....|....*....|....*.
gi 1226253483 99 LLGGVTISEGGVLPNIQAVLLPKKTK 124
Cdd:smart00414 81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
|
|
| PLN00156 |
PLN00156 |
histone H2AX; Provisional |
2-123 |
1.64e-54 |
|
histone H2AX; Provisional
Pssm-ID: 215080 Cd Length: 139 Bit Score: 167.84 E-value: 1.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 2 SGRGKKlaapqKSKTSVSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLRI 81
Cdd:PLN00156 9 GGRGKP-----KATKSVSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRI 83
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1226253483 82 APRHIQLAVRNDEELNTLLGGVTISEGGVLPNIQAVLLPKKT 123
Cdd:PLN00156 84 VPRHIQLAVRNDEELSKLLGSVTIAAGGVLPNIHQTLLPKKV 125
|
|
| HFD_H2A |
cd00074 |
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ... |
18-106 |
2.70e-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: 2.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 18 VSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLRIAPRHIQLAVRNDEELN 97
Cdd:cd00074 1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80
|
....*....
gi 1226253483 98 TLLGGVTIS 106
Cdd:cd00074 81 KLFKGVTIA 89
|
|
| PLN00153 |
PLN00153 |
histone H2A; Provisional |
1-127 |
3.04e-51 |
|
histone H2A; Provisional
Pssm-ID: 165721 [Multi-domain] Cd Length: 129 Bit Score: 159.11 E-value: 3.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 1 MSGRGKklaAPQKSKTSVSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLR 80
Cdd:PLN00153 1 MAGRGK---GKTSGKKAVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNR 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1226253483 81 IAPRHIQLAVRNDEELNTLLGGVTISEGGVLPNIQAVLLPKKTKAAR 127
Cdd:PLN00153 78 IVPRHIQLAIRNDEELGKLLGEVTIASGGVLPNIHAVLLPKKTKGGK 124
|
|
| HTA1 |
COG5262 |
Histone H2A [Chromatin structure and dynamics]; |
3-130 |
3.35e-51 |
|
Histone H2A [Chromatin structure and dynamics];
Pssm-ID: 227587 [Multi-domain] Cd Length: 132 Bit Score: 158.87 E-value: 3.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 3 GRGKKLAAPqksKTSVSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLRIA 82
Cdd:COG5262 5 GKGGKAADA---RVSQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRII 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1226253483 83 PRHIQLAVRNDEELNTLLGGVTISEGGVLPNIQAVLLPKKTKAAREPN 130
Cdd:COG5262 82 PRHLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRS 129
|
|
| PLN00154 |
PLN00154 |
histone H2A; Provisional |
1-124 |
1.06e-38 |
|
histone H2A; Provisional
Pssm-ID: 177756 Cd Length: 136 Bit Score: 127.37 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 1 MSGRGKK-LAAPQKS----------KTSVSRSARAGLQFPVGRIARLLRKGNFA-ARIGSGAAVYLTAVIEYLCAEVLEL 68
Cdd:PLN00154 1 MSGKGGKgLLAAKTTaaaakkdkdkKKPTSRSSRAGLQFPVGRIHRQLKQRVSAhGRVGATAAVYTAAILEYLTAEVLEL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1226253483 69 AGNASRDNKKLRIAPRHIQLAVRNDEELNTLLGGvTISEGGVLPNIQAVLLPKKTK 124
Cdd:PLN00154 81 AGNASKDLKVKRITPRHLQLAIRGDEELDTLIKG-TIAGGGVIPHIHKSLINKSTK 135
|
|
| PTZ00252 |
PTZ00252 |
histone H2A; Provisional |
7-131 |
1.29e-32 |
|
histone H2A; Provisional
Pssm-ID: 240330 Cd Length: 134 Bit Score: 111.98 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 7 KLAAPQKSKTSVSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDN--KKLRIAPR 84
Cdd:PTZ00252 5 KQAKKKASKSGSGRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPR 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1226253483 85 HIQLAVRNDEELNTLLGGVTISEGGVLPNIQAVlLPKKTKAAREPNA 131
Cdd:PTZ00252 85 TVTLAVRHDDDLGSLLKNVTLSRGGVMPSLNKA-LAKKHKSGKKAKA 130
|
|
| PLN00155 |
PLN00155 |
histone H2A; Provisional |
1-61 |
4.87e-18 |
|
histone H2A; Provisional
Pssm-ID: 165723 Cd Length: 58 Bit Score: 72.43 E-value: 4.87e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1226253483 1 MSGRGKklaAPQKSKTSVSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYL 61
Cdd:PLN00155 1 MAGRGK---GKTSGKKAVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
|
|
| Histone_H2A_C |
pfam16211 |
C-terminus of histone H2A; |
94-126 |
3.04e-17 |
|
C-terminus of histone H2A;
Pssm-ID: 465070 Cd Length: 35 Bit Score: 69.87 E-value: 3.04e-17
10 20 30
....*....|....*....|....*....|...
gi 1226253483 94 EELNTLLGGVTISEGGVLPNIQAVLLPKKTKAA 126
Cdd:pfam16211 1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKK 33
|
|
| HFD_SOS1_rpt2 |
cd22915 |
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ... |
28-101 |
3.23e-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: 63.03 E-value: 3.23e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1226253483 28 FPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLRIAPRHIQLAVRNDEELNTLLG 101
Cdd:cd22915 2 FPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
|
|
| HFD_ABTB2-like |
cd22913 |
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ... |
14-100 |
2.02e-13 |
|
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: 61.93 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 14 SKTSVSRSARAGLQFPVGRIARLLRKGNFAARIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLRIAPRHIQLAVRND 93
Cdd:cd22913 5 DQLRRSKSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINND 84
|
....*..
gi 1226253483 94 EELNTLL 100
Cdd:cd22913 85 AELWGLL 91
|
|
| Histone |
pfam00125 |
Core histone H2A/H2B/H3/H4; |
13-91 |
1.21e-12 |
|
Core histone H2A/H2B/H3/H4;
Pssm-ID: 459682 [Multi-domain] Cd Length: 126 Bit Score: 60.52 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226253483 13 KSKTSVSRSARAGLQFPVGRIARLLRKGNFAA-RIGSGAAVYLTAVIEYLCAEVLELAGNASRDNKKLRIAPRHIQLAVR 91
Cdd:pfam00125 45 EIRKYQSSTDLLIYKLPFARVVREVVQSTKTDlRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARR 124
|
|
| |
