|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00154 |
PLN00154 |
histone H2A; Provisional |
6-121 |
5.42e-63 |
|
histone H2A; Provisional
Pssm-ID: 177756 Cd Length: 136 Bit Score: 188.61 E-value: 5.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 6 AGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPR 85
Cdd:PLN00154 17 AAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPR 96
|
90 100 110
....*....|....*....|....*....|....*.
gi 119581480 86 HLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGK 121
Cdd:PLN00154 97 HLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINK 132
|
|
| H2A |
smart00414 |
Histone 2A; |
19-124 |
5.72e-58 |
|
Histone 2A;
Pssm-ID: 197711 Cd Length: 106 Bit Score: 174.83 E-value: 5.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 19 SRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 98
Cdd:smart00414 1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79
|
90 100
....*....|....*....|....*..
gi 119581480 99 SLIKA-TIAGGGVIPHIHKSLIGKKGQ 124
Cdd:smart00414 80 KLLKGvTIAQGGVLPNIHKVLLPKKTG 106
|
|
| HFD_H2A |
cd00074 |
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ... |
18-105 |
2.92e-46 |
|
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: 144.60 E-value: 2.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 18 VSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 97
Cdd:cd00074 1 QSRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEEL 79
|
....*...
gi 119581480 98 DSLIKATI 105
Cdd:cd00074 80 NKLFKGVT 87
|
|
| HTA1 |
COG5262 |
Histone H2A [Chromatin structure and dynamics]; |
1-122 |
7.19e-44 |
|
Histone H2A [Chromatin structure and dynamics];
Pssm-ID: 227587 [Multi-domain] Cd Length: 132 Bit Score: 140.00 E-value: 7.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 1 MAGGKAGKDSGKAKAKavSRSQRAGLQFPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVK 80
Cdd:COG5262 2 VSGGKGGKAADARVSQ--SRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 119581480 81 RITPRHLQLAIRGDEELDSLIK-ATIAGGGVIPHIHKSLIGKK 122
Cdd:COG5262 79 RIIPRHLQLAIRNDEELNKLLGdVTIAQGGVLPNINPGLLPKS 121
|
|
| Histone |
pfam00125 |
Core histone H2A/H2B/H3/H4; |
5-94 |
1.40e-17 |
|
Core histone H2A/H2B/H3/H4;
Pssm-ID: 459682 [Multi-domain] Cd Length: 126 Bit Score: 72.85 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 5 KAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITP 84
Cdd:pfam00125 37 RPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTP 116
|
90
....*....|
gi 119581480 85 RHLQLAIRGD 94
Cdd:pfam00125 117 KDIQLARRLR 126
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00154 |
PLN00154 |
histone H2A; Provisional |
6-121 |
5.42e-63 |
|
histone H2A; Provisional
Pssm-ID: 177756 Cd Length: 136 Bit Score: 188.61 E-value: 5.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 6 AGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPR 85
Cdd:PLN00154 17 AAAKKDKDKKKPTSRSSRAGLQFPVGRIHRQLKQRVSAHGRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRITPR 96
|
90 100 110
....*....|....*....|....*....|....*.
gi 119581480 86 HLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGK 121
Cdd:PLN00154 97 HLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINK 132
|
|
| PTZ00017 |
PTZ00017 |
histone H2A; Provisional |
3-128 |
1.69e-61 |
|
histone H2A; Provisional
Pssm-ID: 185399 Cd Length: 134 Bit Score: 184.56 E-value: 1.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 3 GGKAGKDSGK-AKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKR 81
Cdd:PTZ00017 2 GGKGKTGGGKaGKKKPVSRSAKAGLQFPVGRVHRYLKKGRYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 119581480 82 ITPRHLQLAIRGDEELDSLI-KATIAGGGVIPHIHKSLIGKKGQQKTA 128
Cdd:PTZ00017 81 ITPRHIQLAIRNDEELNKLLaGVTIASGGVLPNIHKVLLPKKSKPKQG 128
|
|
| H2A |
smart00414 |
Histone 2A; |
19-124 |
5.72e-58 |
|
Histone 2A;
Pssm-ID: 197711 Cd Length: 106 Bit Score: 174.83 E-value: 5.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 19 SRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELD 98
Cdd:smart00414 1 SRSARAGLQFPVGRIHRLLRKGTYAK-RVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELN 79
|
90 100
....*....|....*....|....*..
gi 119581480 99 SLIKA-TIAGGGVIPHIHKSLIGKKGQ 124
Cdd:smart00414 80 KLLKGvTIAQGGVLPNIHKVLLPKKTG 106
|
|
| HFD_H2A |
cd00074 |
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ... |
18-105 |
2.92e-46 |
|
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: 144.60 E-value: 2.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 18 VSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEEL 97
Cdd:cd00074 1 QSRSKRAGLQFPVGRIHRLLKKGTYAK-RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEEL 79
|
....*...
gi 119581480 98 DSLIKATI 105
Cdd:cd00074 80 NKLFKGVT 87
|
|
| HTA1 |
COG5262 |
Histone H2A [Chromatin structure and dynamics]; |
1-122 |
7.19e-44 |
|
Histone H2A [Chromatin structure and dynamics];
Pssm-ID: 227587 [Multi-domain] Cd Length: 132 Bit Score: 140.00 E-value: 7.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 1 MAGGKAGKDSGKAKAKavSRSQRAGLQFPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVK 80
Cdd:COG5262 2 VSGGKGGKAADARVSQ--SRSAKAGLIFPVGRVKRLLK-KGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 119581480 81 RITPRHLQLAIRGDEELDSLIK-ATIAGGGVIPHIHKSLIGKK 122
Cdd:COG5262 79 RIIPRHLQLAIRNDEELNKLLGdVTIAQGGVLPNINPGLLPKS 121
|
|
| PLN00157 |
PLN00157 |
histone H2A; Provisional |
3-128 |
1.44e-41 |
|
histone H2A; Provisional
Pssm-ID: 177758 Cd Length: 132 Bit Score: 134.21 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 3 GGKAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRI 82
Cdd:PLN00157 2 SGRGKRKGGGGGKKATSRSAKAGLQFPVGRIARYLKAGKYAT-RVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 119581480 83 TPRHLQLAIRGDEELDSLIK-ATIAGGGVIPHIHKSLIGKKGQQKTA 128
Cdd:PLN00157 81 VPRHIQLAVRNDEELSKLLGgVTIAAGGVLPNIHSVLLPKKSGKSKG 127
|
|
| PLN00156 |
PLN00156 |
histone H2AX; Provisional |
1-125 |
1.98e-39 |
|
histone H2AX; Provisional
Pssm-ID: 215080 Cd Length: 139 Bit Score: 128.93 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 1 MAGGKAGKDSGKAKA-KAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKV 79
Cdd:PLN00156 2 AGSGTTKGGRGKPKAtKSVSRSSKAGLQFPVGRIARFLKAGKYAE-RVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 119581480 80 KRITPRHLQLAIRGDEELDSLIKA-TIAGGGVIPHIHKSLIGKKGQQ 125
Cdd:PLN00156 81 NRIVPRHIQLAVRNDEELSKLLGSvTIAAGGVLPNIHQTLLPKKVGK 127
|
|
| PLN00153 |
PLN00153 |
histone H2A; Provisional |
1-122 |
1.32e-34 |
|
histone H2A; Provisional
Pssm-ID: 165721 [Multi-domain] Cd Length: 129 Bit Score: 116.36 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 1 MAGGKAGKDSGKakaKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVK 80
Cdd:PLN00153 1 MAGRGKGKTSGK---KAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 119581480 81 RITPRHLQLAIRGDEELDSLI-KATIAGGGVIPHIHKSLIGKK 122
Cdd:PLN00153 77 RIVPRHIQLAIRNDEELGKLLgEVTIASGGVLPNIHAVLLPKK 119
|
|
| PTZ00252 |
PTZ00252 |
histone H2A; Provisional |
12-128 |
1.16e-21 |
|
histone H2A; Provisional
Pssm-ID: 240330 Cd Length: 134 Bit Score: 83.47 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 12 KAKAKAVSRSQRAGLQFPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNAS--KDLKVKRITPRHLQL 89
Cdd:PTZ00252 10 KASKSGSGRSAKAGLIFPVGRVGSLLR-RGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAaqQAKKPKRLTPRTVTL 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 119581480 90 AIRGDEELDSLIK-ATIAGGGVIPHIHKSLIGKKGQQKTA 128
Cdd:PTZ00252 89 AVRHDDDLGSLLKnVTLSRGGVMPSLNKALAKKHKSGKKA 128
|
|
| Histone |
pfam00125 |
Core histone H2A/H2B/H3/H4; |
5-94 |
1.40e-17 |
|
Core histone H2A/H2B/H3/H4;
Pssm-ID: 459682 [Multi-domain] Cd Length: 126 Bit Score: 72.85 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 5 KAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITP 84
Cdd:pfam00125 37 RPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTP 116
|
90
....*....|
gi 119581480 85 RHLQLAIRGD 94
Cdd:pfam00125 117 KDIQLARRLR 126
|
|
| HFD_SOS1_rpt2 |
cd22915 |
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ... |
28-100 |
8.30e-12 |
|
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: 56.48 E-value: 8.30e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119581480 28 FPVGRIHRHLKtRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSL 100
Cdd:cd22915 2 FPVDKIHPLLK-KDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDL 73
|
|
| PLN00155 |
PLN00155 |
histone H2A; Provisional |
1-62 |
9.55e-12 |
|
histone H2A; Provisional
Pssm-ID: 165723 Cd Length: 58 Bit Score: 55.87 E-value: 9.55e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119581480 1 MAGGKAGKDSGKakaKAVSRSQRAGLQFPVGRIHRHLKTRTTSHgRVGATAAVYSAAILEYL 62
Cdd:PLN00155 1 MAGRGKGKTSGK---KAVSRSAKAGLQFPVGRIARYLKKGKYAE-RIGAGAPVYLAAVLEYL 58
|
|
| HFD_ABTB2-like |
cd22913 |
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ... |
18-97 |
3.58e-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: 55.77 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581480 18 VSRSQRAGLQFPVGRIHRHL-KTRTTShgRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEE 96
Cdd:cd22913 9 RSKSARCGLTFSVGRFHRWMvDSRLAK--RIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAE 86
|
.
gi 119581480 97 L 97
Cdd:cd22913 87 L 87
|
|
| Histone_H2A_C |
pfam16211 |
C-terminus of histone H2A; |
95-128 |
1.35e-09 |
|
C-terminus of histone H2A;
Pssm-ID: 465070 Cd Length: 35 Bit Score: 49.84 E-value: 1.35e-09
10 20 30
....*....|....*....|....*....|....*
gi 119581480 95 EELDSLIK-ATIAGGGVIPHIHKSLIGKKGQQKTA 128
Cdd:pfam16211 1 EELNKLLRgVTIAQGGVLPNIHKVLLPKKTKKKKK 35
|
|
| BUR6 |
COG5247 |
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription]; |
27-100 |
2.29e-05 |
|
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
Pssm-ID: 227572 Cd Length: 113 Bit Score: 40.72 E-value: 2.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119581480 27 QFPVGRIHRHLKTrTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSL 100
Cdd:COG5247 23 RFPIARLKKIMQL-DEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
|
|
|