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
EJG07937.1TIGRFAM: anaerobic ribonucleoside-triphosphate reductase; COGs: COG1328 Oxygen-sensitive ribonucleoside-triphosphate reductase; InterPro IPR012833; KEGG: mem:Memar_0320 anaerobic ribonucleoside-triphosphate reductase; SPTR: Anaerobic ribonucleoside-triphosphate reductase; TIGRFAM: Ribonucleoside-triphosphate reductase, anaerobic. (725 aa)    
Predicted Functional Partners:
EJG06406.1
PFAM: dUTPase; TIGRFAM: deoxycytidine triphosphate deaminase; COGs: COG0717 Deoxycytidine deaminase; InterPro IPR011962:IPR008180; KEGG: mpl:Mpal_0292 deoxycytidine triphosphate deaminase; PFAM: DeoxyUTP pyrophosphatase domain; SPTR: Deoxycytidine triphosphate deaminase; TIGRFAM: Deoxycytidine triphosphate deaminase.
    
 0.989
dcd
Deoxycytidine triphosphate deaminase; Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
    
 0.989
ndk
Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
     
 0.982
pyrG
CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
     
 0.981
moaA
Molybdenum cofactor biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate; Belongs to the radical SAM superfamily. MoaA family.
  
  
 0.974
mptA
Protein of unknown function DUF198; Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin.
  
  
  0.972
EJG07938.1
Glutaredoxin; KEGG: mbn:Mboo_1708 glutaredoxin; SPTR: Glutaredoxin.
    
 0.925
EJG06298.1
PFAM: HD domain; TIGRFAM: deoxyguanosinetriphosphate triphosphohydrolase, putative; COGs: COG0232 dGTP triphosphohydrolase; InterPro IPR006261:IPR006674:IPR003607; KEGG: mem:Memar_0447 metal-dependent phosphohydrolase; PFAM: Metal-dependent phosphohydrolase, HD region, subdomain; SMART: Metal-dependent phosphohydrolase, HD region; SPTR: Metal-dependent phosphohydrolase, HD sub domain; TIGRFAM: Deoxyguanosinetriphosphate triphosphohydrolase.
    
  0.923
EJG07274.1
PFAM: HD domain; TIGRFAM: deoxyguanosinetriphosphate triphosphohydrolase, putative; COGs: COG0232 dGTP triphosphohydrolase; InterPro IPR006261:IPR003607:IPR006674; KEGG: toc:Toce_0512 deoxyguanosinetriphosphate triphosphohydrolase; PFAM: Metal-dependent phosphohydrolase, HD region, subdomain; SMART: Metal-dependent phosphohydrolase, HD region; SPTR: Deoxyguanosinetriphosphate triphosphohydrolase-like protein 1; TIGRFAM: Deoxyguanosinetriphosphate triphosphohydrolase.
    
  0.923
queE
Radical SAM domain protein; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
  
 
 0.913
Your Current Organism:
Methanofollis liminatans
NCBI taxonomy Id: 28892
Other names: M. liminatans DSM 4140, Methanofollis liminatans DSM 4140, Methanofollis liminatans GKZPZ, Methanofollis liminatans str. DSM 4140, Methanofollis liminatans strain DSM 4140, Methanogenium liminatans (DSM 4140), Methanogenium liminatans DSM 4140
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