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
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 [...] (665 aa)    
Predicted Functional Partners:
uvrA
Excinuclease ABC subunit 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.
 
 0.999
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.
 0.998
all1616
ORF_ID:all1616; hypothetical protein.
  
 
 0.975
all3439
ORF_ID:all3439; unknown protein.
  
 
 0.937
alr1263
UV DNA damage endonuclease; Component in a DNA repair pathway. Removal of UV LIGHT damaged nucleotides. Recognizes pyrimidine dimers and cleave a phosphodiester bond immediately 5' to the lesion (By similarity).
      
 0.901
all4495
DNA helicase II; ORF_ID:all4495.
 
 
 0.876
recA
Recombination protein; 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; Belongs to the RecA family.
 
  
 0.810
alr0165
DNA helicase; ORF_ID:alr0165; hypothetical protein.
  
 
 0.781
alr1674
ORF_ID:alr1674; hypothetical protein.
  
 
 0.781
alr4908
SOS function regulatory protein, LexA repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
  
  
 0.751
Your Current Organism:
Nostoc sp. PCC7120
NCBI taxonomy Id: 103690
Other names: Anabaena sp. (ATCC 27893), Anabaena sp. (PCC 7120), Anabaena sp. DCC D0672, Anabaena sp. PCC 7120, Anabaena sp. SAG 25.82, Anabaena sp. UTEX B 2576, Anabaena variabilis UTCC 387, N. sp. PCC 7120, Nostoc muscorum ISU, Nostoc sp. AKM24, Nostoc sp. ATCC 27347, Nostoc sp. ATCC 72893, Nostoc sp. DSM 107007, Nostoc sp. Ind43, Nostoc sp. PCC 7120, Nostoc sp. SAG 25.82
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.