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
rimNtRNA threonylcarbamoyladenosine biosynthesis protein RimN; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. (189 aa)    
Predicted Functional Partners:
APR71683.1
DNA protecting protein DprA; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.811
APR71682.1
Peptidoglycan-binding protein LysM; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.803
def_1
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
  
    0.715
APR71680.1
DUF2946 domain-containing protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.448
rlmL
23S rRNA (guanine(2445)-N(2))/(guanine(2069)-N(7))- methyltransferase; Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. Belongs to the methyltransferase superfamily. RlmKL family.
 
   
 0.439
tsaD
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family.
 
  
 0.425
ksgA
16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))- dimethyltransferase; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
 
    0.406
Your Current Organism:
Acinetobacter haemolyticus
NCBI taxonomy Id: 29430
Other names: A. haemolyticus, ATCC 17906, Achromobacter haemolyticus, Acinetobacter genomosp. 4, Acinetobacter genomospecies 4, Acinetobacter haematolyticus, CCUG 888, CIP 64.3, DSM 6962, LMG 996, LMG:996, NCCB 85026, NCTC 12155, NCTC:12155, strain B40, strain Mannheim 2446/60
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