STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
tufTranslation elongation factor EF-1, subunit alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. (428 aa)    
Predicted Functional Partners:
rps10
SSU ribosomal protein S10P (rpsJ); Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
 
 0.995
ef1b
Hypothetical protein; Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus allowing the regeneration of EF-1-alpha/GTP that could then be used to form the ternary complex EF-1-alpha/GTP/AAtRNA.
   
 0.995
fusA
Translation elongation factor EF-2; 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 (By similarity); Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase [...]
0.985
rps3ae
SSU ribosomal protein S3AE; Similar to GP:469248 percent identity: 29.17; identified by sequence similarity; putative; Belongs to the eukaryotic ribosomal protein eS1 family.
 
 0.983
rps3
SSU ribosomal protein S3P (rpsC); Binds the lower part of the 30S subunit head. Belongs to the universal ribosomal protein uS3 family.
 
 0.981
rps5
SSU ribosomal protein S5P (rpsE); With S4 and S12 plays an important role in translational accuracy.
 
 0.973
rpl18
LSU ribosomal protein L18P; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
 
 0.972
rpl30
LSU ribosomal protein L30P (rpmD); Similar to SP:P14035 PID:44769 percent identity: 71.43; identified by sequence similarity; putative.
 
 0.969
eif5a
Translation initiation factor aIF-5A; Functions by promoting the formation of the first peptide bond; Belongs to the eIF-5A family.
  
 
 0.966
rpl5
LSU ribosomal protein L5P (rplE); This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. May contact the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
 0.965
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.