STRINGSTRING
A0A0D3F3Q5 A0A0D3F3Q5 A0A0D3ETH6 A0A0D3ETH6 A0A0D3ETV3 A0A0D3ETV3 A0A0D3F0Y1 A0A0D3F0Y1 A0A0D3F4U3 A0A0D3F4U3 A0A0D3F5Q7 A0A0D3F5Q7 A0A0D3F660 A0A0D3F660 A0A0D3F748 A0A0D3F748 A0A0D3FEJ0 A0A0D3FEJ0 A0A0D3FEJ1 A0A0D3FEJ1 A0A0D3FKH0 A0A0D3FKH0 A0A0D3FRE9 A0A0D3FRE9 A0A0D3FS13 A0A0D3FS13 A0A0D3FTK2 A0A0D3FTK2 A0A0D3FYE6 A0A0D3FYE6 A0A0D3GBK4 A0A0D3GBK4 A0A0D3GIJ2 A0A0D3GIJ2 A0A0D3HS05 A0A0D3HS05 A0A0D3HUT5 A0A0D3HUT5 A0A0D3HWK4 A0A0D3HWK4
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
A0A0D3F3Q5Tr-type G domain-containing protein. (711 aa)
A0A0D3ETH6Tr-type G domain-containing protein. (853 aa)
A0A0D3ETV3Tr-type G domain-containing protein. (841 aa)
A0A0D3F0Y1Translation factor GUF1 homolog, mitochondrial; Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner. (596 aa)
A0A0D3F4U3Tr-type G domain-containing protein. (469 aa)
A0A0D3F5Q7Tr-type G domain-containing protein. (843 aa)
A0A0D3F660EFG_C domain-containing protein. (757 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)
A0A0D3FEJ1Uncharacterized protein. (918 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)
A0A0D3FS13Tr-type G domain-containing protein. (843 aa)
A0A0D3FTK2Tr-type G domain-containing protein. (548 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)
A0A0D3GBK4Tr-type G domain-containing protein. (1208 aa)
A0A0D3GIJ2Tr-type G domain-containing protein. (898 aa)
A0A0D3HS05Tr-type G domain-containing protein. (464 aa)
A0A0D3HUT5Tr-type G domain-containing protein. (847 aa)
A0A0D3HWK4Tr-type G domain-containing protein. (464 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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