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uvrB protein (Prevotella amnii) - STRING interaction network
"uvrB" - Excinuclease ABC subunit B in Prevotella amnii
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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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[Homology]
Score
uvrBExcinuclease 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 [...] (681 aa)    
Predicted Functional Partners:
HMPREF9018_2057
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 (944 aa)
 
  0.996
HMPREF9018_1979
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 (977 aa)
 
  0.996
uvrC
Excinuclease ABC subunit 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 (613 aa)
 
  0.996
HMPREF9018_0491
DNA helicase (845 aa)
 
  0.952
clpP
Endopeptidase Clp ; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (221 aa)
     
 
  0.847
HMPREF9018_0008
DNA helicase (892 aa)
   
  0.733
polA
DNA-directed DNA polymerase (945 aa)
         
  0.709
dnaA
Chromosomal replication initiator protein DnaA ; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box)- 5’-TTATC[CA]A[CA]A-3’. DnaA binds to ATP and to acidic phospholipids (467 aa)
   
   
  0.638
ligA
Polydeoxyribonucleotide 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 (676 aa)
   
 
  0.629
HMPREF9018_0770
Exodeoxyribonuclease 7 large subunit ; Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides (439 aa)
 
     
  0.603
Your Current Organism:
Prevotella amnii
NCBI taxonomy Id: 679191
Other names: P. amnii, P. amnii CRIS 21A-A, Prevotella amnii, Prevotella amnii CRIS 21A-A, Prevotella amnii Lawson et al. 2008, Prevotella amnii str. CRIS 21A-A, Prevotella amnii strain CRIS 21A-A
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