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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
cmkCytidylate kinase (cmk); Similar to GB:L77117 SP:Q58071 PID:1591369 percent identity: 48.59; identified by sequence similarity; putative. (180 aa)    
Predicted Functional Partners:
rpl24
LSU ribosomal protein L24P (rpl24P); 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.
  
    0.985
rpl22
LSU ribosomal protein L22P (rpl22P); This protein binds specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
  
    0.985
rpl4
LSU ribosomal protein L4P (rpl4P); 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.
  
    0.985
rps4e
SSU ribosomal protein S4E (rps4E); Similar to GB:L77117 SP:P54039 PID:1591170 percent identity: 48.92; identified by sequence similarity; putative; Belongs to the eukaryotic ribosomal protein eS4 family.
  
    0.984
rpl14
LSU ribosomal protein L14P (rpl14P); Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family.
  
    0.984
rpl5
LSU ribosomal protein L5P (rpl5P); 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.
  
    0.983
rps3
SSU ribosomal protein S3P (rps3P); Binds the lower part of the 30S subunit head. Belongs to the universal ribosomal protein uS3 family.
 
    0.983
rpl2
LSU ribosomal protein L2P (rpl2P); 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.
  
    0.981
rpl32e
LSU ribosomal protein L32E (rpl32E); Similar to GB:L77117 SP:P54010 PID:1591174 percent identity: 51.22; identified by sequence similarity; putative; Belongs to the eukaryotic ribosomal protein eL32 family.
 
    0.980
rps17
SSU ribosomal protein S17P (rps17P); One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
  
    0.980
Your Current Organism:
Archaeoglobus fulgidus
NCBI taxonomy Id: 224325
Other names: A. fulgidus DSM 4304, Archaeoglobus fulgidus DSM 4304, Archaeoglobus fulgidus VC-16, Archaeoglobus fulgidus str. DSM 4304, Archaeoglobus fulgidus strain DSM 4304
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.