A0A4Y7STM1 protein (Coprinellus micaceus) - STRING interaction network

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A0A4Y7STM1

DHS-like NAD/FAD-binding domain-containing protein. (620 aa)

Predicted Functional Partners:

A0A4Y7T8J8

0.888

A0A4Y7TG56

0.875

A0A4Y7TUE3

0.863

A0A4Y7SV94

0.849

A0A4Y7TX48

0.846

A0A4Y7TU21

0.828

A0A4Y7T7U4

0.827

A0A4Y7T4L6

0.816

A0A4Y7T4M6

0.816

A0A4Y7T6U6

0.816

Your Current Organism:

Coprinellus micaceus

NCBI taxonomy Id: 71717
Other names: C. micaceus, Coprinus micaceus

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Browse interactions in tabular form:

node1	node2	node1 annotation	node2 annotation	score
A0A4Y7STM1	A0A4Y7SV94	DHS-like NAD/FAD-binding domain-containing protein.	Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.	0.849
A0A4Y7STM1	A0A4Y7T4L6	DHS-like NAD/FAD-binding domain-containing protein.	F-box domain-containing protein.	0.816
A0A4Y7STM1	A0A4Y7T4M6	DHS-like NAD/FAD-binding 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.	0.816
A0A4Y7STM1	A0A4Y7T6U6	DHS-like NAD/FAD-binding 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.	0.816
A0A4Y7STM1	A0A4Y7T7U4	DHS-like NAD/FAD-binding domain-containing protein.	Uridine nucleosidase.	0.827
A0A4Y7STM1	A0A4Y7T8J8	DHS-like NAD/FAD-binding domain-containing protein.	Nicotinamide-nucleotide adenylyltransferase; Belongs to the eukaryotic NMN adenylyltransferase family.	0.888
A0A4Y7STM1	A0A4Y7TG56	DHS-like NAD/FAD-binding domain-containing protein.	Glutamine-dependent NAD(+) synthetase; In the C-terminal section; belongs to the NAD synthetase family.	0.875
A0A4Y7STM1	A0A4Y7TU21	DHS-like NAD/FAD-binding domain-containing protein.	Nudix hydrolase domain-containing protein.	0.828
A0A4Y7STM1	A0A4Y7TUE3	DHS-like NAD/FAD-binding domain-containing protein.	ATP-NAD kinase.	0.863
A0A4Y7STM1	A0A4Y7TX48	DHS-like NAD/FAD-binding domain-containing protein.	Pyrazinamidase/nicotinamidase.	0.846
A0A4Y7SV94	A0A4Y7STM1	Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.	DHS-like NAD/FAD-binding domain-containing protein.	0.849
A0A4Y7SV94	A0A4Y7T7U4	Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.	Uridine nucleosidase.	0.945
A0A4Y7SV94	A0A4Y7T8J8	Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.	Nicotinamide-nucleotide adenylyltransferase; Belongs to the eukaryotic NMN adenylyltransferase family.	0.830
A0A4Y7SV94	A0A4Y7TG56	Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.	Glutamine-dependent NAD(+) synthetase; In the C-terminal section; belongs to the NAD synthetase family.	0.468
A0A4Y7SV94	A0A4Y7TX48	Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.	Pyrazinamidase/nicotinamidase.	0.827
A0A4Y7T4L6	A0A4Y7STM1	F-box domain-containing protein.	DHS-like NAD/FAD-binding domain-containing protein.	0.816
A0A4Y7T4M6	A0A4Y7STM1	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.	DHS-like NAD/FAD-binding domain-containing protein.	0.816
A0A4Y7T6U6	A0A4Y7STM1	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.	DHS-like NAD/FAD-binding domain-containing protein.	0.816
A0A4Y7T7U4	A0A4Y7STM1	Uridine nucleosidase.	DHS-like NAD/FAD-binding domain-containing protein.	0.827
A0A4Y7T7U4	A0A4Y7SV94	Uridine nucleosidase.	Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.	0.945