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
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
polADNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. (878 aa)    
Predicted Functional Partners:
AGA67581.1
DNA polymerase III, beta subunit; 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 [...]
 
 0.988
recA
Protein RecA; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
 
 0.978
sbcD
Exodeoxyribonuclease I subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family.
  
 0.972
AGA69459.1
ATP-dependent DNA helicase, RecQ-like protein; PFAM: Helicase conserved C-terminal domain; RQC domain; HRDC domain; DEAD/DEAH box helicase; TIGRFAM: ATP-dependent DNA helicase RecQ; ATP-dependent DNA helicase, RecQ family.
  
 0.956
AGA70099.1
ATP-dependent DNA ligase LigD polymerase module; PFAM: ATP dependent DNA ligase domain; Eukaryotic and archaeal DNA primase small subunit; ATP dependent DNA ligase C terminal region; ATP-dependent DNA ligase LigD phosphoesterase module.
  
 0.926
AGA68089.1
ATPase involved in DNA repair.
  
 0.915
dinG
DnaQ family exonuclease/DinG family helicase, putative; 3'-5' exonuclease.
  
 0.900
AGA70565.1
DNA/RNA helicase, superfamily II, SNF2 family; PFAM: SNF2 Helicase protein; Helicase conserved C-terminal domain; SNF2 family N-terminal domain.
  
 0.898
mutL
DNA mismatch repair protein MutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
   
 0.892
AGA67603.1
Hypothetical protein.
  
 0.886
Your Current Organism:
Desulfitobacterium dichloroeliminans
NCBI taxonomy Id: 871963
Other names: D. dichloroeliminans LMG P-21439, Desulfitobacterium dichloroeliminans DCA1, Desulfitobacterium dichloroeliminans LMG P-21439, Desulfitobacterium dichloroeliminans LMG P21439, Desulfitobacterium dichloroeliminans str. LMG P-21439, Desulfitobacterium dichloroeliminans strain LMG P-21439
Server load: low (26%) [HD]