A0A096P9P7 protein (Ostreococcus tauri) - STRING interaction network

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Score

A0A096P9P7

EF-Hand 1, calcium-binding site; Belongs to the calmodulin family. (163 aa)

Predicted Functional Partners:

A0A090M449

0.936

A0A090M8K5

0.818

A0A090N334

0.802

A0A096P9D2

0.759

A0A096P7K8

0.741

A0A090MC42

0.735

A0A090LXF3

0.727

A0A096PA50

0.727

Q012U8_OSTTA

0.727

Q01CC1_OSTTA

0.727

Your Current Organism:

Ostreococcus tauri

NCBI taxonomy Id: 70448
Other names: O. tauri

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
A0A090LXF3	A0A090M449	A0A090LXF3	A0A090M449	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).	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	0.727
A0A090LXF3	A0A090M8K5	A0A090LXF3	A0A090M8K5	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).	Small ubiquitin-related modifier.	0.728
A0A090LXF3	A0A090N334	A0A090LXF3	A0A090N334	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).	Cullin repeat-like-containing domain; Belongs to the cullin family.	0.719
A0A090LXF3	A0A096P9P7	A0A090LXF3	A0A096P9P7	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).	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	0.727
A0A090M449	A0A090LXF3	A0A090M449	A0A090LXF3	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	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).	0.727
A0A090M449	A0A090M8K5	A0A090M449	A0A090M8K5	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	Small ubiquitin-related modifier.	0.818
A0A090M449	A0A090MC42	A0A090M449	A0A090MC42	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	Serine/threonine-protein kinase, active site.	0.735
A0A090M449	A0A090N334	A0A090M449	A0A090N334	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	Cullin repeat-like-containing domain; Belongs to the cullin family.	0.802
A0A090M449	A0A096P7K8	A0A090M449	A0A096P7K8	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	Concanavalin A-like lectin/glucanase, subgroup.	0.741
A0A090M449	A0A096P9D2	A0A090M449	A0A096P9D2	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	Serine/threonine-protein kinase, active site.	0.759
A0A090M449	A0A096P9P7	A0A090M449	A0A096P9P7	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	0.936
A0A090M449	A0A096PA50	A0A090M449	A0A096PA50	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	Heat shock transcription factor family.	0.727
A0A090M449	Q012U8_OSTTA	A0A090M449	Q012U8	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	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).	0.727
A0A090M449	Q01CC1_OSTTA	A0A090M449	Q01CC1	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	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).	0.727
A0A090M8K5	A0A090LXF3	A0A090M8K5	A0A090LXF3	Small ubiquitin-related modifier.	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).	0.728
A0A090M8K5	A0A090M449	A0A090M8K5	A0A090M449	Small ubiquitin-related modifier.	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	0.818
A0A090M8K5	A0A090N334	A0A090M8K5	A0A090N334	Small ubiquitin-related modifier.	Cullin repeat-like-containing domain; Belongs to the cullin family.	0.920
A0A090M8K5	A0A096P7K8	A0A090M8K5	A0A096P7K8	Small ubiquitin-related modifier.	Concanavalin A-like lectin/glucanase, subgroup.	0.545
A0A090M8K5	A0A096P9P7	A0A090M8K5	A0A096P9P7	Small ubiquitin-related modifier.	EF-Hand 1, calcium-binding site; Belongs to the calmodulin family.	0.818
A0A090M8K5	Q012U8_OSTTA	A0A090M8K5	Q012U8	Small ubiquitin-related modifier.	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).	0.728