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
rimORibosomal protein S12 methylthiotransferase RimO; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (467 aa)    
Predicted Functional Partners:
dusA
tRNA-dihydrouridine synthase A; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs; Belongs to the Dus family. DusA subfamily.
 
  
 0.547
KPN63642.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S26 family.
  
    0.542
KPN63988.1
Signal peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S26 family.
  
    0.542
prfA
Peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
   
  
 0.538
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
    
   0.483
mnmE
tRNA modification GTPase TrmE; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
   
  
 0.480
KPN63716.1
Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.476
truB
Pseudouridine synthase; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
  
  
 0.470
rlmN
23S rRNA (adenine(2503)-C2)-methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family.
 
  
 0.463
KPN63715.1
GcrA cell cycle regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
    0.426
Your Current Organism:
Aliiroseovarius crassostreae
NCBI taxonomy Id: 154981
Other names: A. crassostreae, Aliiroseovarius crassostreae (Boettcher et al. 2005) Park et al. 2015, CVSP bacterium CV919-312, Crassostrea virginica symbiont, DSM 16950, Pseudoroseovarius crassostreae, Pseudoroseovarius crassostreae (Boettcher et al. 2005) Sun et al. 2015, Roseovarius crassostreae, Roseovarius crassostreae Boettcher et al. 2005, strain CV919-312
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