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ligA protein (Maritimibacter alkaliphilus) - STRING interaction network
"ligA" - Polydeoxyribonucleotide synthase [NAD(+)] in Maritimibacter alkaliphilus
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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ligAPolydeoxyribonucleotide synthase [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 (710 aa)    
Predicted Functional Partners:
RB2654_10393
DNA polymerase I (932 aa)
 
 
  0.937
RB2654_04099
ATP-dependent DNA helicase RecG (696 aa)
   
   
  0.908
recA
Recombinase A ; 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 (361 aa)
         
  0.898
rpsL
30S ribosomal protein S12 ; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (123 aa)
           
  0.895
RB2654_13394
DNA ligase (519 aa)
     
 
  0.863
uvrB
Excinuclease ABC subunit 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 [...] (721 aa)
 
 
  0.785
valS
Valyl-tRNA synthetase ; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner (1030 aa)
     
   
  0.756
hemE
Uroporphyrinogen decarboxylase ; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III (342 aa)
     
   
  0.722
leuS
Leucyl-tRNA synthetase (848 aa)
 
 
  0.717
ileS
Isoleucyl-tRNA synthetase ; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as ’pretransfer’ editing and involves the hydrolysis of activated Val-AMP. The other activity is designated ’posttransfer’ editing and involves deacylation of mischarged Val-tRNA(Ile) (996 aa)
   
 
  0.702
Your Current Organism:
Maritimibacter alkaliphilus
NCBI taxonomy Id: 314271
Other names: M. alkaliphilus, M. alkaliphilus HTCC2654, Maritimibacter, Maritimibacter Lee et al. 2007, Maritimibacter alkaliphilus, Maritimibacter alkaliphilus HTCC2654, Maritimibacter alkaliphilus Lee et al. 2007, Maritimibacter alkaliphilus str. HTCC2654, Maritimibacter alkaliphilus strain HTCC2654, Rhodobacterales bacterium HTCC2654
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