node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BK809_0000118 | BK809_0000839 | A0A1S8BGT3 | A0A1S8BCA6 | Protein sum2. | GH131_N domain-containing protein. | 0.726 |
BK809_0000118 | BK809_0002774 | A0A1S8BGT3 | A0A0G2DXA1 | Protein sum2. | Putative atp-dependent rna helicase dhh1; Belongs to the DEAD box helicase family. | 0.993 |
BK809_0000839 | BK809_0000118 | A0A1S8BCA6 | A0A1S8BGT3 | GH131_N domain-containing protein. | Protein sum2. | 0.726 |
BK809_0000839 | BK809_0001366 | A0A1S8BCA6 | A0A1S8B8T5 | GH131_N domain-containing protein. | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact 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. | 0.779 |
BK809_0000839 | BK809_0001783 | A0A1S8BCA6 | A0A1S8BAX7 | GH131_N domain-containing protein. | DNA-directed RNA polymerase II subunit RPB3. | 0.766 |
BK809_0000839 | BK809_0002711 | A0A1S8BCA6 | A0A1S8B2C4 | GH131_N domain-containing protein. | Transcription elongation factor SPT5; The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene. | 0.651 |
BK809_0000839 | BK809_0002774 | A0A1S8BCA6 | A0A0G2DXA1 | GH131_N domain-containing protein. | Putative atp-dependent rna helicase dhh1; Belongs to the DEAD box helicase family. | 0.699 |
BK809_0000839 | BK809_0004081 | A0A1S8BCA6 | A0A0G2HKC6 | GH131_N domain-containing protein. | RuvB-like helicase; DNA helicase participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. | 0.659 |
BK809_0000839 | BK809_0004301 | A0A1S8BCA6 | A0A1S8BDM2 | GH131_N domain-containing protein. | DNA ligase 4. | 0.679 |
BK809_0000839 | BK809_0004899 | A0A1S8BCA6 | A0A1S8B818 | GH131_N domain-containing protein. | Imitation switch two complex protein 1. | 0.676 |
BK809_0000839 | BK809_0005647 | A0A1S8BCA6 | A0A1S8BN73 | GH131_N domain-containing protein. | FACT complex subunit spt16. | 0.678 |
BK809_0000839 | BK809_0006603 | A0A1S8BCA6 | A0A0G2FXF6 | GH131_N domain-containing protein. | FACT complex subunit POB3; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of [...] | 0.742 |
BK809_0001366 | BK809_0000839 | A0A1S8B8T5 | A0A1S8BCA6 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact 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. | GH131_N domain-containing protein. | 0.779 |
BK809_0001366 | BK809_0001783 | A0A1S8B8T5 | A0A1S8BAX7 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact 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. | DNA-directed RNA polymerase II subunit RPB3. | 0.966 |
BK809_0001366 | BK809_0002711 | A0A1S8B8T5 | A0A1S8B2C4 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact 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. | Transcription elongation factor SPT5; The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene. | 0.912 |
BK809_0001366 | BK809_0004081 | A0A1S8B8T5 | A0A0G2HKC6 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact 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. | RuvB-like helicase; DNA helicase participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. | 0.951 |
BK809_0001366 | BK809_0004301 | A0A1S8B8T5 | A0A1S8BDM2 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact 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. | DNA ligase 4. | 0.689 |
BK809_0001366 | BK809_0004899 | A0A1S8B8T5 | A0A1S8B818 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact 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. | Imitation switch two complex protein 1. | 0.835 |
BK809_0001366 | BK809_0005647 | A0A1S8B8T5 | A0A1S8BN73 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact 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. | FACT complex subunit spt16. | 0.957 |
BK809_0001366 | BK809_0006603 | A0A1S8B8T5 | A0A0G2FXF6 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact 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. | FACT complex subunit POB3; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of [...] | 0.956 |