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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Co-occurrence
Co-expression
Experiments
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[Homology]
Score
ORB40736.1ATP-binding protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. (380 aa)    
Predicted Functional Partners:
hflX
GTPase HflX; GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. HflX GTPase family.
     
 0.707
miaB
Hypothetical protein; 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.
  
   
 0.702
ORB40737.1
Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.692
bioD
Dethiobiotin synthase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring.
      
 0.678
ORB41828.1
Dihydrofolate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.671
ORB44853.1
Septum formation inhibitor Maf; Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
  
 
   0.664
nuoI
NADH-quinone oxidoreductase subunit I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
 
 
 0.663
nuoD
NADH dehydrogenase subunit D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family.
  
  
 0.640
ORB35140.1
Peroxiredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.630
nuoC
NADH-quinone oxidoreductase subunit C; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family.
  
  
 0.621
Your Current Organism:
Mycolicibacterium porcinum
NCBI taxonomy Id: 39693
Other names: ATCC 33776, CCUG 37674, CIP 105392, DSM 44242, JCM 6378, M. porcinum, Mycobacterium porcinum, strain E10241-1
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