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
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
ARA76412.1methylated-DNA--protein-cysteine 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. (175 aa)    
Predicted Functional Partners:
ARA78313.1
DNA-3-methyladenine glycosidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.774
ARA76410.1
Universal stress protein UspE; With UspC and UspD is involved in resistance to UV irradiation; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.577
ARA77598.1
Bifunctional transcriptional regulator/O6-methylguanine-DNA methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
0.552
ARA74359.1
DNA polymerase III subunit beta; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]
  
 
 
 0.472
ARA76764.1
Recombination factor protein RarA; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.452
ARA77339.1
Methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.449
xerD
Site-specific tyrosine recombinase XerD; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerC binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. In the complex XerD specifical [...]
 
     0.449
ARA75944.1
Universal stress protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.445
ARA78350.1
Universal stress global response regulator UspA; Involved in resistance to DNA-damaging agents; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.445
polA
Hypothetical protein; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
 
 
 
 0.438
Your Current Organism:
Pectobacterium brasiliense
NCBI taxonomy Id: 180957
Other names: CFBP 6617, Erwinia carotovora subsp. brasiliensis, LMG 21371, LMG:21371, NCPPB 4609, P. brasiliense, Pectobacterium brasiliense Portier et al. 2019, Pectobacterium brasiliensis, Pectobacterium carotovorum subsp. brasiliense, Pectobacterium carotovorum subsp. brasiliensis, strain 212
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