A0A1J7JPW6 protein (Coniochaeta ligniaria) - STRING interaction network

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Score

A0A1J7JPW6

CobW-domain-containing protein. (372 aa)

Predicted Functional Partners:

A0A1J7JQI0

0.700

A0A1J7IUZ5

0.698

A0A1J7IK09

0.697

A0A1J7J6Y3

0.599

A0A1J7J4A8

0.577

A0A1J7JC94

0.577

A0A1J7JFZ4

0.577

A0A1J7JKE3

0.476

A0A1J7I435

0.432

Your Current Organism:

Coniochaeta ligniaria

NCBI taxonomy Id: 1408157
Other names: C. ligniaria NRRL 30616, Coniochaeta ligniaria NRRL 30616

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Browse interactions in tabular form:

node1	node2	node1 annotation	node2 annotation	score
A0A1J7I435	A0A1J7J4A8	Histidine biosynthesis trifunctional protein.	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	0.613
A0A1J7I435	A0A1J7JC94	Histidine biosynthesis trifunctional protein.	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	0.613
A0A1J7I435	A0A1J7JFZ4	Histidine biosynthesis trifunctional protein.	Uncharacterized protein.	0.613
A0A1J7I435	A0A1J7JKE3	Histidine biosynthesis trifunctional protein.	tRNA-synt_1e domain-containing protein.	0.632
A0A1J7I435	A0A1J7JPW6	Histidine biosynthesis trifunctional protein.	CobW-domain-containing protein.	0.432
A0A1J7IK09	A0A1J7IUZ5	Uncharacterized protein.	Glucocorticoid receptor-like (DNA-binding domain).	0.993
A0A1J7IK09	A0A1J7J4A8	Uncharacterized protein.	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	0.416
A0A1J7IK09	A0A1J7J6Y3	Uncharacterized protein.	Uncharacterized protein.	0.999
A0A1J7IK09	A0A1J7JC94	Uncharacterized protein.	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	0.416
A0A1J7IK09	A0A1J7JFZ4	Uncharacterized protein.	Uncharacterized protein.	0.416
A0A1J7IK09	A0A1J7JPW6	Uncharacterized protein.	CobW-domain-containing protein.	0.697
A0A1J7IK09	A0A1J7JQI0	Uncharacterized protein.	Ribosomal protein S14.	0.993
A0A1J7IUZ5	A0A1J7IK09	Glucocorticoid receptor-like (DNA-binding domain).	Uncharacterized protein.	0.993
A0A1J7IUZ5	A0A1J7J4A8	Glucocorticoid receptor-like (DNA-binding domain).	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	0.786
A0A1J7IUZ5	A0A1J7J6Y3	Glucocorticoid receptor-like (DNA-binding domain).	Uncharacterized protein.	0.997
A0A1J7IUZ5	A0A1J7JC94	Glucocorticoid receptor-like (DNA-binding domain).	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	0.786
A0A1J7IUZ5	A0A1J7JFZ4	Glucocorticoid receptor-like (DNA-binding domain).	Uncharacterized protein.	0.786
A0A1J7IUZ5	A0A1J7JPW6	Glucocorticoid receptor-like (DNA-binding domain).	CobW-domain-containing protein.	0.698
A0A1J7J4A8	A0A1J7I435	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	Histidine biosynthesis trifunctional protein.	0.613
A0A1J7J4A8	A0A1J7IK09	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	Uncharacterized protein.	0.416