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histone H2B, partial [Sphenarium purpurascens]
histone H2B family protein( domain architecture ID 19223400)
histone H2B is one of 4 core histone proteins, H2A, H2B, H3 and H4 to form the nucleosome core particle
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
HFD_H2B | cd22910 | histone-fold domain found in histone H2B and similar proteins; Histone H2B is a core component ... |
33-120 | 4.65e-61 | |||
histone-fold domain found in histone H2B and similar proteins; Histone H2B 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. Some histone H2B family members have broad antibacterial activity, which may contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid. : Pssm-ID: 467035 Cd Length: 94 Bit Score: 181.95 E-value: 4.65e-61
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Name | Accession | Description | Interval | E-value | |||
HFD_H2B | cd22910 | histone-fold domain found in histone H2B and similar proteins; Histone H2B is a core component ... |
33-120 | 4.65e-61 | |||
histone-fold domain found in histone H2B and similar proteins; Histone H2B 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. Some histone H2B family members have broad antibacterial activity, which may contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid. Pssm-ID: 467035 Cd Length: 94 Bit Score: 181.95 E-value: 4.65e-61
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H2B | smart00427 | Histone H2B; |
33-121 | 1.18e-53 | |||
Histone H2B; Pssm-ID: 197718 Cd Length: 97 Bit Score: 163.46 E-value: 1.18e-53
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PLN00158 | PLN00158 | histone H2B; Provisional |
17-122 | 8.95e-53 | |||
histone H2B; Provisional Pssm-ID: 215081 Cd Length: 116 Bit Score: 161.78 E-value: 8.95e-53
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Histone | pfam00125 | Core histone H2A/H2B/H3/H4; |
33-99 | 3.14e-20 | |||
Core histone H2A/H2B/H3/H4; Pssm-ID: 459682 [Multi-domain] Cd Length: 126 Bit Score: 79.40 E-value: 3.14e-20
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Name | Accession | Description | Interval | E-value | |||
HFD_H2B | cd22910 | histone-fold domain found in histone H2B and similar proteins; Histone H2B is a core component ... |
33-120 | 4.65e-61 | |||
histone-fold domain found in histone H2B and similar proteins; Histone H2B 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. Some histone H2B family members have broad antibacterial activity, which may contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid. Pssm-ID: 467035 Cd Length: 94 Bit Score: 181.95 E-value: 4.65e-61
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H2B | smart00427 | Histone H2B; |
33-121 | 1.18e-53 | |||
Histone H2B; Pssm-ID: 197718 Cd Length: 97 Bit Score: 163.46 E-value: 1.18e-53
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PLN00158 | PLN00158 | histone H2B; Provisional |
17-122 | 8.95e-53 | |||
histone H2B; Provisional Pssm-ID: 215081 Cd Length: 116 Bit Score: 161.78 E-value: 8.95e-53
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PTZ00463 | PTZ00463 | histone H2B; Provisional |
21-121 | 4.33e-39 | |||
histone H2B; Provisional Pssm-ID: 185642 Cd Length: 117 Bit Score: 127.21 E-value: 4.33e-39
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Histone | pfam00125 | Core histone H2A/H2B/H3/H4; |
33-99 | 3.14e-20 | |||
Core histone H2A/H2B/H3/H4; Pssm-ID: 459682 [Multi-domain] Cd Length: 126 Bit Score: 79.40 E-value: 3.14e-20
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HFD_SF | cd00076 | histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ... |
37-97 | 1.83e-06 | |||
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: 42.20 E-value: 1.83e-06
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HFD_TAF12 | cd07981 | histone-fold domain found in transcription initiation factor TFIID subunit 12 (TAF12) and ... |
43-93 | 2.99e-04 | |||
histone-fold domain found in transcription initiation factor TFIID subunit 12 (TAF12) and similar proteins; TAF12, also called TATA Binding Protein (TBP) associated factor 12, transcription initiation factor TFIID 20/15 kDa subunits, TAFII-20/TAFII-15, or TAFII20/TAFII15, is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC. TAFs are essential for mediating regulation of RNA polymerase transcription. TAF12 interacts with TAF4 and makes a novel histone-like heterodimer that binds DNA and has a core promoter function of a subset of genes. It is important for RAS-induced transformation properties of human colorectal cancer cells; its levels are increased in the cells harboring the RAS mutation. Also, TAF12 interacts with activating transcription factor 7 (ATF7) and contributes to the hypersensitivity of osteoclast (OCL) precursors to 1,25-dihydroxyvitamin D2 (1,25-(OH)2D3; also known as calcitriol) in Paget's disease (PD), a disorder of the bone remodeling process, in which the body absorbs old bone and forms abnormal new bone. Pssm-ID: 467025 [Multi-domain] Cd Length: 74 Bit Score: 36.74 E-value: 2.99e-04
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HFD_archaea_histone-like | cd22909 | histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ... |
39-97 | 3.88e-03 | |||
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription regulators and similar proteins; The family includes many archaeal histone-fold proteins and histone-like transcription regulators, which may bind and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. They can increase the resistance of DNA to thermal denaturation. Pssm-ID: 467034 Cd Length: 64 Bit Score: 33.67 E-value: 3.88e-03
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