STRINGSTRING
EFTS-2 EFTS-2 A0A0D3F2J8 A0A0D3F2J8 A0A0D3F748 A0A0D3F748 A0A0D3FEJ0 A0A0D3FEJ0 A0A0D3FJN1 A0A0D3FJN1 A0A0D3FKH0 A0A0D3FKH0 A0A0D3FRE9 A0A0D3FRE9 A0A0D3FYE6 A0A0D3FYE6 A0A0D3GI13 A0A0D3GI13 A0A0D3GTH3 A0A0D3GTH3 A0A0D3GUM1 A0A0D3GUM1 EFTS EFTS
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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EFTS-2Elongation factor Ts, mitochondrial; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family. (1123 aa)
A0A0D3F2J8Uncharacterized protein. (476 aa)
A0A0D3F748Elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (467 aa)
A0A0D3FEJ0Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (447 aa)
A0A0D3FJN1EF1_GNE domain-containing protein; Belongs to the EF-1-beta/EF-1-delta family. (224 aa)
A0A0D3FKH0Elongation 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. (770 aa)
A0A0D3FRE9Elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (453 aa)
A0A0D3FYE6Elongation factor G, chloroplastic; Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. 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. (702 aa)
A0A0D3GI13Uncharacterized protein. (419 aa)
A0A0D3GTH3EF1_GNE domain-containing protein; Belongs to the EF-1-beta/EF-1-delta family. (251 aa)
A0A0D3GUM1EF1_GNE domain-containing protein; Belongs to the EF-1-beta/EF-1-delta family. (224 aa)
EFTSElongation factor Ts, mitochondrial; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family. (482 aa)
Your Current Organism:
Oryza barthii
NCBI taxonomy Id: 65489
Other names: African wild rice, O. barthii, Oryza barthii A.Chev., Oryza breviligulata, Oryza breviligulata A.Chev. & Roehr.
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