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aEF-1 aEF-1 rpsJ rpsJ aEF-1-2 aEF-1-2 aEF-2 aEF-2 rps3ae rps3ae rpsC rpsC rps7 rps7 rpsL rpsL rpl18 rpl18 rpsE rpsE rplE rplE
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.
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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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
aEF-1Translation 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:
rpsJ
SSU ribosomal protein S10; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
 
 
 0.998
aEF-1-2
Translation elongation factor aEF-1 beta; 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.
   
 0.998
aEF-2
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; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF- [...]
 
0.996
rps3ae
SSU ribosomal protein S3AE; Belongs to the eukaryotic ribosomal protein eS1 family.
 
 0.995
rpsC
SSU ribosomal protein S3P; Binds the lower part of the 30S subunit head. Belongs to the universal ribosomal protein uS3 family.
 
 0.992
rps7
SSU ribosomal protein S7P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center; Belongs to the universal ribosomal protein uS7 family.
 
 
 0.991
rpsL
SSU ribosomal protein S12; With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits. Belongs to the universal ribosomal protein uS12 family.
  
 
 0.986
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.
 
 0.985
rpsE
SSU ribosomal protein S5P; With S4 and S12 plays an important role in translational accuracy.
 
 
 0.985
rplE
LSU ribosomal protein L5P; 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.
 0.984
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
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