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ligA protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"ligA" - DNA ligase in Desulfovibrio vulgaris Hildenborough
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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ligADNA ligase; 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 (799 aa)    
Predicted Functional Partners:
uvrB
UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] (677 aa)
 
 
  0.922
nadE
Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source (559 aa)
   
   
  0.832
DVU_1606
Potassium uptake protein, TrkA family; Identified by similarity to OMNI-NTL01SS00580; match to protein family HMM PF02080; match to protein family HMM PF02254 (350 aa)
   
        0.766
DVU_1607
Uncharacterized protein; Identified by Glimmer2; putative (248 aa)
              0.742
uvrA
UvrABC system protein A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (956 aa)
 
   
  0.737
mutY
A/G-specific adenine glycosylase; Identified by match to protein family HMM PF00293; match to protein family HMM PF00633; match to protein family HMM PF00730; match to protein family HMM TIGR01084 (373 aa)
   
   
  0.736
uvrC
UvrABC system protein C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5’ and 3’ sides of the lesion. The N-terminal half is responsible for the 3’ incision and the C-terminal half is responsible for the 5’ incision (702 aa)
 
 
  0.730
polA
DNA polymerase I; Identified by similarity to SP-P00582; match to protein family HMM PF00476; match to protein family HMM PF01367; match to protein family HMM PF02739; match to protein family HMM TIGR00593 (1015 aa)
   
 
  0.730
gyrB
DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner (798 aa)
   
 
  0.722
leuS
Leucine--tRNA ligase; Identified by similarity to SP-P07813; match to protein family HMM PF00133; match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family (829 aa)
   
 
  0.716
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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