close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
cpdB2', 3'-cyclic nucleotide 2'-phosphodiesterase; In Escherichia coli this is a periplasmic enzyme while in gram positive organisms it may be anchored at the cell surface; this protein appears to consist of a dimer fusion; functions during ribonucleic acid degradation; 2',3'-cyclic nucleotides are first converted to 3'-nucleotide and then cleaved to yield a ribonucleotide and a phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology. (1402 aa)    
Predicted Functional Partners:
cinA
Damage-inducible protein CinA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CinA family.
   
 
  0.757
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
     
 0.752
guaB
Inosine-5-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
    
 0.749
deoA
Thymidine phosphorylase; Catalyzes the reversible phosphorolysis of thymidine, deoxyuridine and their analogues to their respective bases and 2-deoxyribose 1-phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
  0.724
KEZ53991.1
MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.711
KEZ49706.1
Hypoxanthine phosphoribosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the purine/pyrimidine phosphoribosyltransferase family.
  
  
 0.684
KEZ51747.1
Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family.
 
  
  0.678
KEZ47882.1
5'-nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the 5'-nucleotidase family.
  
  
 
0.678
deoD
Purine nucleoside phosphorylase DeoD-type; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
  0.667
KEZ51498.1
Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
  
 
 0.666
Your Current Organism:
Bacillus indicus
NCBI taxonomy Id: 246786
Other names: B. indicus, Bacillus cibi, Bacillus cibi Yoon et al. 2005, Bacillus indicus Suresh et al. 2004 emend. Stropko et al. 2014, Bacillus sp. KU12, Bacillus sp. KU14, DSM 15820, DSM 16189 [[Bacillus cibi]], JCM 12168, KCTC 3880 [[Bacillus cibi]], LMG 22858, LMG:22858, MTCC 4374, strain JG-30 [[Bacillus cibi]], strain Sd/3
Server load: low (34%) [HD]