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
ABI66645.1PFAM: glutamyl-tRNA synthetase, class Ic; KEGG: ccr:CC2205 glutamyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (278 aa)    
Predicted Functional Partners:
rplW
LSU ribosomal protein L23P; One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome; Belongs to the universal ribosomal protein uL23 family.
   
 0.927
rplM
LSU ribosomal protein L13P; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
  
 0.925
rplF
LSU ribosomal protein L6P; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
   
 0.921
rplD
LSU ribosomal protein L4P; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
  
 0.920
rplR
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.
   
 0.919
rplO
LSU ribosomal protein L15P; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
   
 0.915
rplN
LSU ribosomal protein L14P; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family.
   
 0.913
rplB
LSU ribosomal protein L2P; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
  
 0.911
rplX
LSU ribosomal protein L24P; One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
   
 0.909
rplV
LSU ribosomal protein L22P; This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).
   
 0.909
Your Current Organism:
Maricaulis maris
NCBI taxonomy Id: 394221
Other names: M. maris MCS10, Maricaulis maris MCS10, Maricaulis maris str. MCS10, Maricaulis maris strain MCS10
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.