STRINGSTRING
STRING protein interaction network
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
polADNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. (880 aa)    
Predicted Functional Partners:
mutM
5-hydroxymethyluracil DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
  
  
 0.984
dnaN
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 [...]
 
 0.983
recA
Recombinase 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.
 
 0.970
AJF84306.1
Metallophosphoesterase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.964
sbcD
Nuclease SbcCD 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.
  
 0.964
AJF85525.1
DNA polymerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
0.958
dinG
DNA polymerase III subunit epsilon; 3'-5' exonuclease.
  
 0.947
ligD
ATP-dependent DNA ligase; Catalyzes the ATP-dependent formation of a phosphodiester at the site of a single-strand break in duplex DNA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.942
mutS
DNA mismatch repair protein MutS; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
   
 0.934
AJF86966.1
Restriction endonuclease subunit R; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.926
Your Current Organism:
Bacillus atrophaeus
NCBI taxonomy Id: 1452
Other names: ATCC 49337, B. atrophaeus, Bacillus atriphaeus, Bacillus sp. S2 BC-2, Bacillus subtilis DSM 2277, Bacillus subtilis DSM 675, CCUG 28524, CIP 107159, DSM 7264, IFO 15539, JCM 9070, LMG 16797, LMG:16797, NBRC 15539, NRRL NRS-213
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