A9V5N7_MONBE protein (Monosiga brevicollis) - STRING interaction network

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Score

A9V5N7_MONBE

Predicted protein. (1075 aa)

Predicted Functional Partners:

A9UY63_MONBE

0.995

A9UNN8_MONBE

0.969

A9V6F4_MONBE

0.822

A9UYK2_MONBE

0.802

A9V921_MONBE

0.802

A9V840_MONBE

0.641

A9UPU3_MONBE

0.640

A9UZC6_MONBE

0.640

A9VBV8_MONBE

0.640

A9UQQ5_MONBE

0.536

Your Current Organism:

Monosiga brevicollis

NCBI taxonomy Id: 81824
Other names: M. brevicollis

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
A9UNN8_MONBE	A9UPU3_MONBE	A9UNN8	A9UPU3	CSL zinc finger domain-containing protein.	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	0.549
A9UNN8_MONBE	A9UY63_MONBE	A9UNN8	A9UY63	CSL zinc finger domain-containing protein.	2-(3-amino-3-carboxypropyl)histidine synthase subunit 1; Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.	0.965
A9UNN8_MONBE	A9UYK2_MONBE	A9UNN8	A9UYK2	CSL zinc finger domain-containing protein.	Predicted protein.	0.742
A9UNN8_MONBE	A9UZC6_MONBE	A9UNN8	A9UZC6	CSL zinc finger domain-containing protein.	Predicted protein.	0.549
A9UNN8_MONBE	A9V5N7_MONBE	A9UNN8	A9V5N7	CSL zinc finger domain-containing protein.	Predicted protein.	0.969
A9UNN8_MONBE	A9V6F4_MONBE	A9UNN8	A9V6F4	CSL zinc finger domain-containing protein.	Predicted protein.	0.504
A9UNN8_MONBE	A9V921_MONBE	A9UNN8	A9V921	CSL zinc finger domain-containing protein.	Predicted protein.	0.742
A9UNN8_MONBE	A9VBV8_MONBE	A9UNN8	A9VBV8	CSL zinc finger domain-containing protein.	Predicted protein.	0.549
A9UPU3_MONBE	A9UNN8_MONBE	A9UPU3	A9UNN8	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	CSL zinc finger domain-containing protein.	0.549
A9UPU3_MONBE	A9UQQ5_MONBE	A9UPU3	A9UQQ5	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	Uncharacterized protein.	0.406
A9UPU3_MONBE	A9UY63_MONBE	A9UPU3	A9UY63	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	2-(3-amino-3-carboxypropyl)histidine synthase subunit 1; Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.	0.640
A9UPU3_MONBE	A9V5N7_MONBE	A9UPU3	A9V5N7	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	Predicted protein.	0.640
A9UPU3_MONBE	A9V6F4_MONBE	A9UPU3	A9V6F4	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	Predicted protein.	0.605
A9UPU3_MONBE	A9V840_MONBE	A9UPU3	A9V840	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	RNA helicase.	0.443
A9UQQ5_MONBE	A9UPU3_MONBE	A9UQQ5	A9UPU3	Uncharacterized protein.	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	0.406
A9UQQ5_MONBE	A9UY63_MONBE	A9UQQ5	A9UY63	Uncharacterized protein.	2-(3-amino-3-carboxypropyl)histidine synthase subunit 1; Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.	0.485
A9UQQ5_MONBE	A9V5N7_MONBE	A9UQQ5	A9V5N7	Uncharacterized protein.	Predicted protein.	0.536
A9UQQ5_MONBE	A9V840_MONBE	A9UQQ5	A9V840	Uncharacterized protein.	RNA helicase.	0.858
A9UY63_MONBE	A9UNN8_MONBE	A9UY63	A9UNN8	2-(3-amino-3-carboxypropyl)histidine synthase subunit 1; Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.	CSL zinc finger domain-containing protein.	0.965
A9UY63_MONBE	A9UPU3_MONBE	A9UY63	A9UPU3	2-(3-amino-3-carboxypropyl)histidine synthase subunit 1; Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	0.640