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
APO91285.1ATP-dependent DNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. (534 aa)    
Predicted Functional Partners:
APO91283.1
DNA ligase-associated DEXH box helicase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.997
APO91287.1
Phosphoesterase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.961
APO91286.1
DNA ligase-associated DEXH box helicase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
    0.951
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 [...]
   
 0.936
ligA
DNA ligase (NAD(+)) LigA; 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.
    
 0.916
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.
  
 0.855
APO91284.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.773
exo
Exodeoxyribonuclease IX; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.697
holB
DNA polymerase III subunit delta; Catalyzes the DNA-template-directed extension of the 3'-end of a DNA strand; the delta' subunit seems to interact with the gamma subunit to transfer the beta subunit on the DNA; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.674
ku
Ku protein; 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.
 
  
 0.670
Your Current Organism:
Xanthomonas euvesicatoria
NCBI taxonomy Id: 456327
Other names: ATCC 11633, Bacterium vesicatorium, DSM 19128, ICMP 109, ICMP 98, NCPPB 2968, X. euvesicatoria, Xanthomonas campestris (pv. vesicatoria), Xanthomonas campestris pv. Vesicatoria type A, Xanthomonas campestris pv. vesicatoria, Xanthomonas euvesicatoria Jones et al. 2006 emend. Constantin et al. 2016
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.