DFR1 protein (Powellomyces hirtus) - STRING interaction network

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DFR1

Dihydrofolate reductase. (2385 aa)

Predicted Functional Partners:

A0A507EA38

0.854

A0A507DQD9

0.842

A0A507DRR1

0.785

A0A507EDZ1

0.759

A0A507DYM6

0.750

A0A507E7R6

0.723

A0A507E6Y0

0.720

A0A507EAI9

0.719

A0A507EFS0

0.718

A0A507DXQ3

0.717

Your Current Organism:

Powellomyces hirtus

NCBI taxonomy Id: 109895
Other names: P. hirtus

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
A0A507DQD9	A0A507DRR1	A0A507DQD9	A0A507DRR1	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 [...]	DNA-directed RNA polymerase.	0.954
A0A507DQD9	A0A507DYM6	A0A507DQD9	A0A507DYM6	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 [...]	Uncharacterized protein.	0.999
A0A507DQD9	A0A507E6Y0	A0A507DQD9	A0A507E6Y0	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 [...]	DNA-directed RNA polymerase.	0.931
A0A507DQD9	A0A507E7R6	A0A507DQD9	A0A507E7R6	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 [...]	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.	0.980
A0A507DQD9	A0A507EA38	A0A507DQD9	A0A507EA38	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 [...]	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.	0.947
A0A507DQD9	A0A507EAI9	A0A507DQD9	A0A507EAI9	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 [...]	Uncharacterized protein.	0.929
A0A507DQD9	A0A507EFS0	A0A507DQD9	A0A507EFS0	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 [...]	RPOL4c domain-containing protein.	0.942
A0A507DQD9	DFR1	A0A507DQD9	A0A507DP47	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 [...]	Dihydrofolate reductase.	0.842
A0A507DRR1	A0A507DQD9	A0A507DRR1	A0A507DQD9	DNA-directed RNA polymerase.	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 [...]	0.954
A0A507DRR1	A0A507DXQ3	A0A507DRR1	A0A507DXQ3	DNA-directed RNA polymerase.	Uncharacterized protein.	0.624
A0A507DRR1	A0A507DYM6	A0A507DRR1	A0A507DYM6	DNA-directed RNA polymerase.	Uncharacterized protein.	0.979
A0A507DRR1	A0A507E6Y0	A0A507DRR1	A0A507E6Y0	DNA-directed RNA polymerase.	DNA-directed RNA polymerase.	0.999
A0A507DRR1	A0A507E7R6	A0A507DRR1	A0A507E7R6	DNA-directed RNA polymerase.	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.	0.995
A0A507DRR1	A0A507EA38	A0A507DRR1	A0A507EA38	DNA-directed RNA polymerase.	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.	0.951
A0A507DRR1	A0A507EAI9	A0A507DRR1	A0A507EAI9	DNA-directed RNA polymerase.	Uncharacterized protein.	0.999
A0A507DRR1	A0A507EFS0	A0A507DRR1	A0A507EFS0	DNA-directed RNA polymerase.	RPOL4c domain-containing protein.	0.999
A0A507DRR1	DFR1	A0A507DRR1	A0A507DP47	DNA-directed RNA polymerase.	Dihydrofolate reductase.	0.785
A0A507DXQ3	A0A507DRR1	A0A507DXQ3	A0A507DRR1	Uncharacterized protein.	DNA-directed RNA polymerase.	0.624
A0A507DXQ3	A0A507E6Y0	A0A507DXQ3	A0A507E6Y0	Uncharacterized protein.	DNA-directed RNA polymerase.	0.619
A0A507DXQ3	A0A507EA38	A0A507DXQ3	A0A507EA38	Uncharacterized 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.	0.793