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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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adaAmethylphosphotriester-DNA alkyltransferase and transcriptional regulator (AraC/XylS family); Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the methylphosphotriester lesions in DNA by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. (211 aa)    
Predicted Functional Partners:
adaB
O6-methylguanine-DNA methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
  
 0.999
alkA
DNA-3-methyladenine glycosylase; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine and 7- methylguanine from the damaged DNA polymer formed by alkylation lesions.
  
 0.997
ogt
O6-alkylguanine DNA alkyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
  
 0.986
aag
3-alkylated purines and hypoxanthine DNA glycosidase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the DNA glycosylase MPG family.
  
  
 0.893
ydfE
Putative flavoprotein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
    0.659
yfjP
Putative DNA-modified purine glycosidase; Hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions; Belongs to the alkylbase DNA glycosidase AlkA family.
  
 0.628
ydeC
Putative transcriptional regulator (AraC/XylS family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator.
 
    0.536
comEC
DNA channel for uptake in competent cells; The comE operon is required for the binding and uptake of transforming DNA. ComEC is required for internalization but is dispensable for DNA binding; To H.influenzae REC2, N.gonorrhoeae ComA and E.coli YcaI.
     
 0.504
yisR
Putative transcriptional regulator (AraC/XylS family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator.
 
  
0.448
cinA
Competence-damage inducible regulator; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; regulator; Belongs to the CinA family.
     
 0.447
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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