close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
Rmag_0088TIGRFAM: adenylylsulfate reductase, alpha subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; KEGG: tbd:Tbd_2282 adenylylsulfate reductase, alpha subunit. (627 aa)    
Predicted Functional Partners:
Rmag_0087
TIGRFAM: adenylylsulfate reductase, beta subunit; PFAM: 4Fe-4S ferredoxin, iron-sulfur binding domain protein; KEGG: tbd:Tbd_2283 adenylylsulfate reductase, beta subunit.
 
 
 0.997
sat
KEGG: tbd:Tbd_0874 ATP-sulfurylase; TIGRFAM: sulfate adenylyltransferase; PFAM: ATP-sulfurylase; Belongs to the sulfate adenylyltransferase family.
 
 
 0.981
Rmag_0793
Fumarase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
  
 0.977
Rmag_0869
KEGG: tbd:Tbd_2484 sulfite reductase, dissimilatory-type beta subunit; TIGRFAM: sulfite reductase, dissimilatory-type beta subunit; PFAM: 4Fe-4S ferredoxin, iron-sulfur binding domain protein; nitrite/sulfite reductase, hemoprotein beta-component, ferrodoxin domain protein; nitrite and sulphite reductase 4Fe-4S region.
 
 
 0.964
Rmag_0870
KEGG: tbd:Tbd_2485 sulfite reductase, dissimilatory-type alpha subunit; TIGRFAM: sulfite reductase, dissimilatory-type alpha subunit; PFAM: nitrite and sulphite reductase 4Fe-4S region.
 
 
 0.964
Rmag_0086
KEGG: tbd:Tbd_2284 hypothetical protein.
 
     0.926
nuoD
NADH dehydrogenase subunit D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family.
   
 
 0.922
cysQ
3'(2'),5'-bisphosphate nucleotidase; Converts adenosine-3',5'-bisphosphate (PAP) to AMP. Belongs to the inositol monophosphatase superfamily. CysQ family.
   
  0.912
Rmag_0242
NADH dehydrogenase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
 
 0.910
Rmag_0089
KEGG: tbd:Tbd_2281 hypothetical protein.
 
     0.900
Your Current Organism:
Ruthia magnifica
NCBI taxonomy Id: 413404
Other names: C. Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica strain Cm (Calyptogena magnifica), Ruthia magnifica str. Cm (Calyptogena magnifica)
Server load: low (32%) [HD]