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
CAZ97865.1Conserved hypothetical protein; Signal peptide cleaved between the residues 27 and 28; Putatively localized in the outer membrane (PSORT result). (2927 aa)    
Predicted Functional Partners:
CAZ97042.1
Conserved hypothetical protein; Contains several Single hybrid motifs found in biotinyl/lipoyl-carrier proteins and domains, where the biotin and lipoic acid moieties act as covalently attached coenzyme in various enzymes; Signal peptide cleaved between the residues 23 and 24; Putatively localized in the cytoplasmic membrane.
  
  
  0.967
CAZ95459.1
Conserved hypothetical membrane protein; Contains an uncleavable signal sequence; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
  
  
 
0.930
CAZ95759.1
Conserved hypothetical protein; Putatively contains a B_ant_repeat domain (DUF 11) and a Concanavalin A-like lectin/glucanase domain in the N-terminal region; Contains also at least four BNR/Asp-box repeats (bacterial neuraminidase repeat) found in many glycoside hydrolases and in other extracellular proteins of unknown function; Signal peptide cleaved between the residues 23 and 24; Probably localized in the outer membrane.
  
  
 
0.928
CAZ96570.1
Protein that contains in the N-terminal part, one cadherin like domain and in its C-terminal part, five PKD repeats. The PKD domains are present in the extracellular parts of proteins involved in interactions with other proteins or polysaccharides; Signal peptide cleaved between the residues 19 and 20; Putatively localized in the outer membrane.
     
  0.900
CAZ97785.1
Hypothetical protein; Would contain ten type-3 Thrombospondin repeats; Signal peptide cleaved between the residues 24 and 25; Putatively localized in the outer membrane.
     
  0.900
CAZ95761.1
Conserved hypothetical periplasmic protein; Contains a central Ig-like domain (residues 511-592); Signal peptide cleaved between the residues 26 and 27; Localized in the periplasmic space; Conserved hypothetical protein.
  
   
 0.768
CAZ95760.1
Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein.
  
     0.766
CAZ98769.1
Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 28 and 29; Localized in the periplasmic space; Conserved hypothetical protein.
  
     0.764
CAZ98882.1
Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space; Conserved hypothetical protein.
  
     0.764
CAZ95455.1
Hypothetical protein. Putatively localized in the cytoplasm.
  
    0.763
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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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.