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 [...] (711 aa)    
Predicted Functional Partners:
uvrA
ABC-ATPase UvrA; 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.
 
 0.999
KUO01582.1
Daunorubicin resistance protein DrrC; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.998
KUN95583.1
ABC transporter; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.998
KUN91171.1
Daunorubicin resistance protein DrrC; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.997
KUN93005.1
ATP-dependent DNA helicase PcrA; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.939
KUN98667.1
ATP-dependent DNA helicase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.866
recA
DNA recombination/repair protein RecA; 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.
 
  
 0.863
ruvB
ATP-dependent DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
 
   
 0.827
pheT
phenylalanine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
   
 0.790
Your Current Organism:
Streptomyces resistomycificus
NCBI taxonomy Id: 67356
Other names: ATCC 19804, BCRC 13755, CBS 556.68, CCRC 13755, CCRC:13755, DSM 40133, IFO 12814, ISP 5133, JCM 4409, NBRC 12814, NCIMB 9843, NRRL 2290, NRRL-ISP 5133, PCM 2296, S. resistomycificus, Streptomyces sp. USC032, UNIQEM 190
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