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
ADE85010.1Sporulation domain protein. (304 aa)    
Predicted Functional Partners:
holB
DNA polymerase III, delta' subunit.
 
     0.866
tmk
Thymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis; Belongs to the thymidylate kinase family.
       0.839
dacC2
D-alanyl-D-alanine carboxypeptidase-2; Belongs to the peptidase S11 family.
       0.839
ADE85004.1
Membrane transport family protein.
       0.817
ADE85005.1
Metallo-beta-lactamase family protein.
       0.817
ADE85006.1
TatD-related deoxyribonuclease family protein.
       0.817
ADE84275.1
Peptidase, subfamily A24A, prepilin type IV.
 
     0.778
ADE85554.1
Membrane protein, putative.
  
     0.768
ADE84274.1
TPR repeat domain protein.
 
     0.767
ADE84273.1
TPR repeat domain protein.
 
     0.756
Your Current Organism:
Rhodobacter capsulatus
NCBI taxonomy Id: 272942
Other names: R. capsulatus SB 1003, Rhodobacter capsulatus SB 1003
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.