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
ANQ23121.1DNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. (278 aa)    
Predicted Functional Partners:
ANQ20148.1
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 [...]
   
 0.968
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.
  
 0.931
ligA
DNA ligase (NAD(+)) LigA; This protein 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; essential for DNA replication and repair of damaged DNA; similar to ligase LigB; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.927
xni
Flap endonuclease Xni; Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment.
  
 0.829
ANQ21978.1
Has polymerase, DNA-binding and 3'-5' exonuclease activities. In Aeropyrum pernix this protein is sensitive to aphidicolin and stable at 95#C; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.814
ANQ22065.1
DNA polymerase III subunit delta; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.801
ANQ21130.1
Exodeoxyribonuclease III; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.794
ANQ24135.1
Exonuclease SbcC; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.770
sbcD
Exonuclease 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.
  
 0.764
hisB
Bifunctional imidazole glycerol-phosphate dehydratase/histidinol phosphatase; Catalyzes the formation of 3-(imidazol-4-yl)-2-oxopropyl phosphate from D-ethythro-1-(imidazol-4-yl)glycerol 3-phosphate and histidinol from histidinol phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the histidinol- phosphatase family.
   
 0.725
Your Current Organism:
Vibrio natriegens
NCBI taxonomy Id: 691
Other names: ATCC 14048, Beneckea natriegens, CAIM 12, CCUG 16371, CCUG 4980 A, CIP 103193, DSM 759, IFO 15636, LMG 10935, LMG:10935, NBRC 15636, NCCB 73019, NCMB 857, NCMB:857, NCTC 11319, Pseudomonas natriegens, V. natriegens
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