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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
nifF2Probable flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family. (178 aa)    
Predicted Functional Partners:
azo2279
Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...]
    
 0.590
azo2278
Conserved hypothetical protein. Homology to pa3943 of P. aeruginosa (TREMBL:Q9HX73). no domians predicted. weak evidence for signal peptide. no TMHs.
 
  
  0.560
azo2282
Conserved hypothetical protein. Identity to Daro_1071 of Dechloromonas aromatica of 41% (gi|71846331|gb|AAZ45827.1|). Pfam: CheW-like domain. CheW-like domain proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.
 
 
   0.560
azo2117
Hypothetical protein. Very bad homology with hits. Has No domains, repeats, motifs or features detected.
 
     0.557
azo2280
Hypothetical protein 25% Identity to TrEMBL;Q7U749. No domains, repeats, motifs or features present.
       0.539
azo1488
Conserved hypothetical protein. Homology to Daro03003756 of Dechloromonas aromatica of 53% (gi|41722684|ref|ZP_00149673.1|(NBCI ENTREZ)). No domains predicted. No signal peptide. No TMHs.
  
     0.490
azo0536
Conserved hypothetical protein. Homology to an orf of Pseudomonas stutzeri of 52% (tremble:Q9EVM9). No domains predicted. No TMHs. No signal peptide.
 
     0.470
azo1131
Conserved hypothetical protein. Homology to Daro03001685 of Dechloromonas aromatica of 46% (gi|41725028|ref|ZP_00151838.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide.
  
     0.460
nifY2
NifY-like protein. Homology to Daro03003760 of Dechloromonas aromatica of 65% (gi|46140358|ref|ZP_00203574.1|(NBCI ENTREZ)). Pfam: Dinitrogenase iron-molybdenum cofactor. This family contains several NIF (B, Y and X) proteins which are involved in the synthesis of an iron-molybdenum cofactors (FeMo-co) in the dinitrogenase enzyme which catalyses the reduction of dinitrogen to ammonium. No signal peptide predicted. No TMHs; Family membership.
 
   
 0.456
azo0564
Conserved hypothetical protein. Has PF05484:LRV protein FeS4 cluster(IPR008665);This Iron sulphur cluster is found at the N-terminus of some proteins containing LRV repeats. Has 6,(IPR004830) PF01816:Leucine rich repeat variant;The function of this repeat is unknown. It has an unusual structure of two helices. One is an alpha helix,the other is the much rarer 3-10 helix; Function unclear.
 
     0.440
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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