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
DIP0829Putative endonuclease; Similar to Streptomyces coelicolor putative endonuclease VIII Nei or SC7C7.15c SW:END8_STRCO (O86820) (276 aa) fasta scores: E(): 2.5e-39, 40.87% id in 274 aa, and to Escherichia coli endonuclease VIII Nei or B0714 SW:END8_ECOLI (P50465) (262 aa) fasta scores: E(): 4.6e-14, 28.88% id in 277 aa. (268 aa)    
Predicted Functional Partners:
DIP0827
Similar to Escherichia coli probable ATP-dependent helicase Lhr or RhlF or B1653 SW:LHR_ECOLI (P30015) (1538 aa) fasta scores: E(): 1.4e-134, 46.42% id in 1579 aa.
 
  
 0.900
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
  
  
 0.884
rnc
Ribonuclease III; Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
     
 0.843
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; Belongs to the RecA family.
  
  
 0.819
nth
Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate.
   
  
 0.664
DIP0828
Putative DNA repair protein; Similar to Streptomyces coelicolor G/U mismatch-specific DNA glycosylase Mug TR:Q9K3I5 (EMBL:AL390188) (160 aa) fasta scores: E(): 1.6e-21, 46.49% id in 157 aa, and to Escherichia coli G/U mismatch-specific DNA glycosylase Mug or B3068 SW:MUG_ECOLI (P43342) (168 aa) fasta scores: E(): 1.1e-15, 36.84% id in 171 aa.
 
   
 0.628
DIP1980
Putative DNA repair protein; Similar to Mycobacterium leprae probable DNA glycosylase ML1920 TR:Q9CBJ0 (EMBL:AL583923) (297 aa) fasta scores: E(): 5.3e-52, 51.86% id in 295 aa. N-terminus is similar to the N-terminal region of Escherichia coli A/G-specific adenine glycosylase MutY SW:MUTY_ECOLI (P17802) (350 aa) fasta scores: E(): 2.9e-23, 40.48% id in 205 aa.
  
  
 0.611
coaE
dephospho-CoA kinase; Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A; Belongs to the CoaE family.
  
  
 0.482
Your Current Organism:
Corynebacterium diphtheriae
NCBI taxonomy Id: 257309
Other names: C. diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC13129
Server load: high (86%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.