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
CAZ94911.1The transcriptional regulators with the Rrf2-type HTH domain control a variety of operons that encode iron-sulfur-containing proteins as well as other proteins involved in electron transport. Other rrf2-type HTH proteins are repressors of genes involved in nitrite or iron metabolism; The C-terminal part of the rrf2-type HTH domain contains 3 conserved cysteine residues that may bind an Fe-S cluster; Contains a DNA-binding, winged helix-turn-helix (wHTH) domain; Localized in the cytoplasm; Family membership. (136 aa)    
Predicted Functional Partners:
iscS
Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules as thio-nucleosides in tRNA, thiamine, biotin, lipoate, molybdopterin and Fe-S cluster; Uses the Pyridoxal phosphate as prosthetic group linked to a lysine residue; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.
  
  
 0.724
cysH
The 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase called also PAPS sulfotransferase catalyses the reduction of activated sulfate into sulfite; The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP); Belongs to the PAPS reductase family; Localized in the cytoplasm; High confidence in function and specificity.
 
  
 0.649
ccoNO
Fusion of the subunits CcoN and CcoO of the Cytochrome cbb3 oxidase. Converts the ferrocytochrome to ferricytochrome. Belongs to the ccoNOQP operon. Contains 13 transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity.
  
  
 0.566
sirA
Sulfite reductase catalyses the six-electron reduction reactions of sulfite to sulfide; Contains a Fe(4)S(4) cluster coupled to a siroheme through a cysteine bridge; Would contains a C-terminal HEPN domain of unknown function; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family; Localized in the cytoplasm; High confidence in function and specificity.
 
    0.558
CAZ94910.1
Conserved hypothetical membrane protein; Contains a C-terminal transmembrane segment; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
       0.495
CAZ94912.1
Conserved hypothetical membrane protein; Contains six transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
       0.488
cysD
The sulfate adenylyltransferase (ATP sulfurylase) catalyses the activation of sulfate with ATP to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. ATP sulfurylase is a heterodimer composed of cysD, the smaller subunit, and cysN; Belongs to the PAPS reductase family; Localized in the cytoplasm; High confidence in function and specificity.
  
  
 0.439
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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