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
CAZ98234.1Thiol-disulfide oxidoreductase catalyzes the formation of disulfide bond in various substrates. Its exact specificity is not known; Contains a N-terminal transmembrane helix; Belongs to the thioredoxin family; Localized in the cytoplasmic membrane; Specificity unclear. (188 aa)    
Predicted Functional Partners:
CAZ94109.1
Conserved hypothetical membrane protein; Contains six transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
   
 0.684
CAZ98233.1
Conserved hypothetical protein; Localized in the cytoplasm.
       0.523
CAZ98187.1
Conserved protein belonging to the thioredoxin family. Thioredoxins are small proteins of approximately one hundred amino-acid residues which participate in various redox reactions via the reversible oxidation of an active center disulfide bond; Signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space; Family membership.
  
 
 0.520
dsbD
Thiol:disulfide interchange protein; DsbD, also known as protein-disulfide reductase, is required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps; Uses NAD(P) as cofactor; Contains eight transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity.
  
 
 0.520
CAZ98097.1
Conserved protein belonging to the DUF179 family. Localized in the cytoplasm; Family membership.
   
 
 0.515
CAZ96021.1
Conserved hypothetical membrane protein; Protein that consists of a SCO1/SenC domain; Contains a N-terminal transmembrane segment; Belongs to the SCO2/SenC family; Localized in the cytoplasmic membrane; Family membership.
 
 
 0.489
CAZ94457.1
Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity unclear.
   
 
 0.484
nrfI
NrfI may play a role in cytochrome c biogenesis and may be required for maturation of the NrfA protein, involved in nitrite reduction; Contains 12 transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity.
  
  
 0.475
CAZ96539.1
Conserved hypothetical membrane protein; Protein that consists of a SCO1/SenC domain; Belongs to the SCO2/SenC family; Contains a N-terminal transmembrane segment; Localized in the cytoplasmic membrane; Family membership.
 
 
 0.473
CAZ96982.1
Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear.
  
 0.466
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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