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
CAZ96251.1Deacetylase. Belongs to the histone deacetylase family; Specificity unclear. (300 aa)    
Predicted Functional Partners:
CAZ95265.1
FAD-dependent amine oxidoreductase of unknown substrate specificity; Belongs to the amine oxydase family; Localized in the cytoplasm; Specificity unclear.
   
 0.936
htpG
Chaperone protein htpG; Molecular chaperone. Has ATPase activity.
   
 0.742
udk
Uridine kinase (pyrimidine ribonucleoside kinase) is the rate-limiting enzyme in the pyrimidine salvage pathway. It catalyzes the reactions: ATP + uridine = ADP + UMP and ATP + cytidine = ADP + CMP. It forms a homotetramer and binds a ATP per subunit as cofactor. Localized in the cytoplasm; High confidence in function and specificity.
   
 0.697
npdA
NAD-dependent deacetylase activates the enzyme acetyl-CoA synthetase by deacetylating its catalytic Lysine in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. It binds one zinc ion as a cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the sirtuin family. Class III subfamily.
    
 
 0.585
CAZ96252.1
Putative protein.
       0.527
rplF
Ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
    
  0.525
katA2
Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.
   
 0.506
ppiB
Peptidyl-prolyl cis-trans isomerase, or PPIase or rotamase, accelerates the folding of proteins. It catalyzes the peptidyl-prolyl isomerisation during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilised in the cis conformation in oligopeptides; Contains a N-terminal Cyclophilin type PPIase/CLD and a C-terminal FKBP-type peptidyl-prolyl cis- trans isomerase; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.505
ppiA
Peptidyl-prolyl cis-trans isomerase, or PPIase or rotamase, accelerates the folding of proteins. It catalyzes the peptidyl-prolyl isomerisation during which the peptide bond preceding proline is stabilised in the cis conformation in oligopeptides; Contains a N-terminal Cyclophilin type PPIase/CLD domain and a C-terminal FKBP-type peptidyl-prolyl cis-trans isomerase domain; Signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; High confidence in function and specificity.
  
 0.505
CAZ96250.1
This enzyme belongs to the Acid phosphatase / vanadium-dependent haloperoxidase family protein; Features a signal peptide cleaved between residues 18 and 19; Localized in the periplasmic space; Family membership.
   
 0.500
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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