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
SDF08895.1Bifunctional non-homologous end joining protein LigD. (808 aa)    
Predicted Functional Partners:
SDE22245.1
DNA polymerase-3 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 re [...]
   
 0.990
ku
DNA end-binding protein Ku; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family.
 
  
 0.988
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
  
 0.975
SDE95658.1
CarboxypepD_reg-like domain-containing protein.
   
 0.898
SDD59896.1
DNA ligase-1.
 
  
 0.896
SDD72701.1
DNA polymerase-3 subunit delta'.
   
 0.893
SDE12894.1
Exonuclease SbcC.
   
 0.886
hisB
Imidazoleglycerol-phosphate dehydratase; In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.
   
 0.853
ligA
DNA ligase (NAD+); DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
    
 0.827
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.
  
 0.818
Your Current Organism:
Pricia antarctica
NCBI taxonomy Id: 641691
Other names: DSM 23421, JCM 17291, Maribacter sp. ZS1-8, P. antarctica, Pricia antarctica Yu et al. 2012, strain ZS1-8
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.