A0A178AQB4 protein (Stagonospora sp. SRC1lsM3a)

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Score

A0A178AQB4

Uncharacterized protein. (98 aa)

Predicted Functional Partners:

A0A178AL64

0.754

IQ06DRAFT_2455

0.697

A0A178BBM9

0.692

A0A178A9B9

0.611

A0A178AZP5

0.604

A0A178ALG7

0.601

A0A178BAS5

0.569

A0A178AVN9

0.548

A0A178AUE5

0.542

A0A178AVK8

0.542

Your Current Organism:

Stagonospora sp. SRC1lsM3a

NCBI taxonomy Id: 765868
Other names: S. sp. SRC1lsM3a

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
A0A178A9B9	A0A178AQB4	A0A178A9B9	A0A178AQB4	Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones.	Uncharacterized protein.	0.611
A0A178A9B9	A0A178AUE5	A0A178A9B9	A0A178AUE5	Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones.	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.	0.865
A0A178A9B9	A0A178AVK8	A0A178A9B9	A0A178AVK8	Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones.	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.	0.865
A0A178A9B9	A0A178AVN9	A0A178A9B9	A0A178AVN9	Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones.	Uncharacterized protein; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.	0.993
A0A178A9B9	A0A178AZP5	A0A178A9B9	A0A178AZP5	Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones.	SET domain-containing protein.	0.771
A0A178A9B9	A0A178BAS5	A0A178A9B9	A0A178BAS5	Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones.	Eukaryotic translation initiation factor-like protein 2 subunit gamma.	0.743
A0A178A9B9	IQ06DRAFT_2455	A0A178A9B9	A0A178B982	Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones.	Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.	0.997
A0A178AL64	A0A178AQB4	A0A178AL64	A0A178AQB4	Uncharacterized protein.	Uncharacterized protein.	0.754
A0A178AL64	A0A178AVN9	A0A178AL64	A0A178AVN9	Uncharacterized protein.	Uncharacterized protein; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.	0.509
A0A178AL64	A0A178BAS5	A0A178AL64	A0A178BAS5	Uncharacterized protein.	Eukaryotic translation initiation factor-like protein 2 subunit gamma.	0.992
A0A178AL64	IQ06DRAFT_2455	A0A178AL64	A0A178B982	Uncharacterized protein.	Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.	0.608
A0A178ALG7	A0A178AQB4	A0A178ALG7	A0A178AQB4	Tryptophan synthase.	Uncharacterized protein.	0.601
A0A178AQB4	A0A178A9B9	A0A178AQB4	A0A178A9B9	Uncharacterized protein.	Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones.	0.611
A0A178AQB4	A0A178AL64	A0A178AQB4	A0A178AL64	Uncharacterized protein.	Uncharacterized protein.	0.754
A0A178AQB4	A0A178ALG7	A0A178AQB4	A0A178ALG7	Uncharacterized protein.	Tryptophan synthase.	0.601
A0A178AQB4	A0A178AUE5	A0A178AQB4	A0A178AUE5	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.	0.542
A0A178AQB4	A0A178AVK8	A0A178AQB4	A0A178AVK8	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.	0.542
A0A178AQB4	A0A178AVN9	A0A178AQB4	A0A178AVN9	Uncharacterized protein.	Uncharacterized protein; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.	0.548
A0A178AQB4	A0A178AZP5	A0A178AQB4	A0A178AZP5	Uncharacterized protein.	SET domain-containing protein.	0.604
A0A178AQB4	A0A178BAS5	A0A178AQB4	A0A178BAS5	Uncharacterized protein.	Eukaryotic translation initiation factor-like protein 2 subunit gamma.	0.569