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
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[Homology]
Score
rlmN50S rRNA 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. (404 aa)    
Predicted Functional Partners:
miaB
(dimethylallyl)adenosine tRNA methylthiotransferase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
 
  
 0.798
hisS
histidyl-tRNA synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.745
KKB61611.1
Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
 
   
 0.739
KKB64626.1
16S rRNA methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
  
 0.733
KKB62548.1
SAM-dependent methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
  
  
 0.733
ndk
Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family.
  
    0.720
nusB
Antitermination protein NusB; Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
 
  
 0.677
KKB63861.1
Diaminohydroxyphosphoribosylaminopyrimidine deaminase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.646
KKB64089.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the pseudouridine synthase RsuA family.
 
  
 0.611
KKB63058.1
YggS family pyridoxal phosphate enzyme; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
 
     0.610
Your Current Organism:
Robbsia andropogonis
NCBI taxonomy Id: 28092
Other names: ATCC 19311 [[Pseudomonas woodsii]], ATCC 23061, Aplanobacter stizolobii, Bacterium andropogoni, Bacterium woodsii, Burkholderia andropogonis, CCUG 32772, CFBP 2421, CIP 105771, DSM 9511, DSM 9884 [[Pseudomonas woodsii]], IBSBF 199, ICMP 2807, ICMP 3967 [[Pseudomonas woodsii]], JCM 10487, LMG 2129, LMG 2362 [[Pseudomonas woodsii]], LMG:2129, LMG:2362 [[Pseudomonas woodsii]], NCPPB 934, NCPPB 968 [[Pseudomonas woodsii]], NRRL B-14296, Paraburkholderia andropogonis, Pseudomonas andropogonis, Pseudomonas stizolobii, Pseudomonas woodsii, R. andropogonis, strain PW 102 [[Pseudomonas woodsii]]
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