H3 histone, family 3D [Danio rerio]
histone H3( domain architecture ID 10794185)
histone H3 is a core component of the nucleosome that wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PTZ00018 | PTZ00018 | histone H3; Provisional |
1-136 | 1.35e-89 | |||
histone H3; Provisional : Pssm-ID: 185400 [Multi-domain] Cd Length: 136 Bit Score: 255.99 E-value: 1.35e-89
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Name | Accession | Description | Interval | E-value | |||
PTZ00018 | PTZ00018 | histone H3; Provisional |
1-136 | 1.35e-89 | |||
histone H3; Provisional Pssm-ID: 185400 [Multi-domain] Cd Length: 136 Bit Score: 255.99 E-value: 1.35e-89
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HFD_H3 | cd22911 | histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ... |
40-133 | 8.07e-64 | |||
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a 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 the 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: 467036 Cd Length: 95 Bit Score: 189.29 E-value: 8.07e-64
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H3 | smart00428 | Histone H3; |
34-136 | 2.01e-60 | |||
Histone H3; Pssm-ID: 128705 [Multi-domain] Cd Length: 105 Bit Score: 181.11 E-value: 2.01e-60
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Histone | pfam00125 | Core histone H2A/H2B/H3/H4; |
1-132 | 5.53e-52 | |||
Core histone H2A/H2B/H3/H4; Pssm-ID: 459682 [Multi-domain] Cd Length: 126 Bit Score: 160.68 E-value: 5.53e-52
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Name | Accession | Description | Interval | E-value | |||
PTZ00018 | PTZ00018 | histone H3; Provisional |
1-136 | 1.35e-89 | |||
histone H3; Provisional Pssm-ID: 185400 [Multi-domain] Cd Length: 136 Bit Score: 255.99 E-value: 1.35e-89
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PLN00121 | PLN00121 | histone H3; Provisional |
1-136 | 1.89e-81 | |||
histone H3; Provisional Pssm-ID: 177733 [Multi-domain] Cd Length: 136 Bit Score: 235.72 E-value: 1.89e-81
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HFD_H3 | cd22911 | histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ... |
40-133 | 8.07e-64 | |||
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a 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 the 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: 467036 Cd Length: 95 Bit Score: 189.29 E-value: 8.07e-64
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H3 | smart00428 | Histone H3; |
34-136 | 2.01e-60 | |||
Histone H3; Pssm-ID: 128705 [Multi-domain] Cd Length: 105 Bit Score: 181.11 E-value: 2.01e-60
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Histone | pfam00125 | Core histone H2A/H2B/H3/H4; |
1-132 | 5.53e-52 | |||
Core histone H2A/H2B/H3/H4; Pssm-ID: 459682 [Multi-domain] Cd Length: 126 Bit Score: 160.68 E-value: 5.53e-52
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PLN00161 | PLN00161 | histone H3; Provisional |
1-133 | 3.04e-47 | |||
histone H3; Provisional Pssm-ID: 215082 [Multi-domain] Cd Length: 135 Bit Score: 148.99 E-value: 3.04e-47
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PLN00160 | PLN00160 | histone H3; Provisional |
43-134 | 2.69e-38 | |||
histone H3; Provisional Pssm-ID: 165727 Cd Length: 97 Bit Score: 125.16 E-value: 2.69e-38
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HFD_CENP-T | cd22920 | histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ... |
70-132 | 4.44e-05 | |||
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also called interphase centromere complex protein 22 (ICEN22), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression, and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENP-T is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Moreover, CENP-T is a component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENP-T has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis. Pssm-ID: 467045 Cd Length: 94 Bit Score: 39.85 E-value: 4.44e-05
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HFD_SF | cd00076 | histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ... |
68-128 | 4.50e-03 | |||
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10. Pssm-ID: 467021 Cd Length: 63 Bit Score: 33.73 E-value: 4.50e-03
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Blast search parameters | ||||
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