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histone H3-like centromeric protein CENH3 isoform X1 [Vitis vinifera]
histone H3 family protein( domain architecture ID 19223538)
histone H3 family protein similar to histone H3-like centromeric protein that is specifically found in centromeric nucleosomes
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
HFD_H3 | cd22911 | histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ... |
60-153 | 8.44e-54 | |||
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: 165.02 E-value: 8.44e-54
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Name | Accession | Description | Interval | E-value | |||
HFD_H3 | cd22911 | histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ... |
60-153 | 8.44e-54 | |||
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: 165.02 E-value: 8.44e-54
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PLN00161 | PLN00161 | histone H3; Provisional |
35-153 | 3.79e-48 | |||
histone H3; Provisional Pssm-ID: 215082 [Multi-domain] Cd Length: 135 Bit Score: 152.08 E-value: 3.79e-48
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H3 | smart00428 | Histone H3; |
54-153 | 4.31e-43 | |||
Histone H3; Pssm-ID: 128705 [Multi-domain] Cd Length: 105 Bit Score: 138.35 E-value: 4.31e-43
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Histone | pfam00125 | Core histone H2A/H2B/H3/H4; |
33-151 | 4.56e-37 | |||
Core histone H2A/H2B/H3/H4; Pssm-ID: 459682 [Multi-domain] Cd Length: 126 Bit Score: 123.70 E-value: 4.56e-37
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HHT1 | COG2036 | Archaeal histone H3/H4 [Chromatin structure and dynamics]; |
82-151 | 1.22e-03 | |||
Archaeal histone H3/H4 [Chromatin structure and dynamics]; Pssm-ID: 441639 Cd Length: 67 Bit Score: 35.58 E-value: 1.22e-03
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Name | Accession | Description | Interval | E-value | |||
HFD_H3 | cd22911 | histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ... |
60-153 | 8.44e-54 | |||
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: 165.02 E-value: 8.44e-54
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PLN00161 | PLN00161 | histone H3; Provisional |
35-153 | 3.79e-48 | |||
histone H3; Provisional Pssm-ID: 215082 [Multi-domain] Cd Length: 135 Bit Score: 152.08 E-value: 3.79e-48
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H3 | smart00428 | Histone H3; |
54-153 | 4.31e-43 | |||
Histone H3; Pssm-ID: 128705 [Multi-domain] Cd Length: 105 Bit Score: 138.35 E-value: 4.31e-43
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PTZ00018 | PTZ00018 | histone H3; Provisional |
1-154 | 5.60e-42 | |||
histone H3; Provisional Pssm-ID: 185400 [Multi-domain] Cd Length: 136 Bit Score: 136.57 E-value: 5.60e-42
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PLN00121 | PLN00121 | histone H3; Provisional |
1-154 | 1.24e-37 | |||
histone H3; Provisional Pssm-ID: 177733 [Multi-domain] Cd Length: 136 Bit Score: 125.55 E-value: 1.24e-37
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Histone | pfam00125 | Core histone H2A/H2B/H3/H4; |
33-151 | 4.56e-37 | |||
Core histone H2A/H2B/H3/H4; Pssm-ID: 459682 [Multi-domain] Cd Length: 126 Bit Score: 123.70 E-value: 4.56e-37
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PLN00160 | PLN00160 | histone H3; Provisional |
62-153 | 1.81e-30 | |||
histone H3; Provisional Pssm-ID: 165727 Cd Length: 97 Bit Score: 105.90 E-value: 1.81e-30
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HFD_archaea_histone-like | cd22909 | histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ... |
82-150 | 3.94e-05 | |||
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: 39.45 E-value: 3.94e-05
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HFD_SF | cd00076 | histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ... |
102-148 | 1.73e-04 | |||
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: 37.97 E-value: 1.73e-04
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HHT1 | COG2036 | Archaeal histone H3/H4 [Chromatin structure and dynamics]; |
82-151 | 1.22e-03 | |||
Archaeal histone H3/H4 [Chromatin structure and dynamics]; Pssm-ID: 441639 Cd Length: 67 Bit Score: 35.58 E-value: 1.22e-03
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HFD_POLE4-like | cd22929 | histone-fold domain found in DNA polymerase epsilon subunit 4 (POLE4) and similar proteins; ... |
100-150 | 4.58e-03 | |||
histone-fold domain found in DNA polymerase epsilon subunit 4 (POLE4) and similar proteins; POLE4, also called DNA polymerase II subunit 4, or DNA polymerase epsilon subunit p12, may participate in DNA repair and in chromosomal DNA replication. It is an accessory component of the DNA polymerase epsilon complex that consists of four subunits: the catalytic subunit POLE and the accessory subunits POLE2, POLE3 and POLE4. POLE4 forms a complex with POLE3. The POLE3-POLE4 is a histone chaperone that promotes tetrasome formation and DNA supercoiling in vitro. Interaction with POLE3 is a prerequisite for further binding with POLE and POLE2. In fungi, POLE4 has been named as DNA polymerase epsilon subunit C (DPB3, also known as DNA polymerase II subunit C). It is an accessory component of the DNA polymerase epsilon (DNA polymerase II) that participates in chromosomal DNA replication. DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4. DPB3 is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair. This subfamily also includes protein DLS1 (DPB3-like subunit of ISW2 complex 1). It functions as a component of the ISW2 complex, which at least consists of ISW2, ITC1, DLS1 and DPB4, and acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex. DLS1 is partially required for the ISW2 complex chromatin remodeling activity and is not required for its interaction with chromatin. Pssm-ID: 467054 [Multi-domain] Cd Length: 79 Bit Score: 34.41 E-value: 4.58e-03
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Blast search parameters | ||||
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