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
AEB85246.1TIGRFAM: Diguanylate cyclase, predicted; PFAM: Diguanylate cyclase, predicted; KEGG: dia:Dtpsy_1780 diguanylate cyclase; SMART: Diguanylate cyclase, predicted. (334 aa)    
Predicted Functional Partners:
AEB86400.1
KEGG: dac:Daci_0737 metal dependent phosphohydrolase; PFAM: Metal-dependent phosphohydrolase, HD subdomain; SMART: Metal-dependent phosphohydrolase, HD domain.
  
 0.864
trmB
tRNA (guanine-N(7)-)-methyltransferase; Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
     
 0.780
AEB85243.1
PFAM: Amine oxidase; KEGG: ajs:Ajs_1983 FAD dependent oxidoreductase.
       0.771
gluQ
Glutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.
       0.764
AEB84961.1
PFAM: Metal-dependent phosphohydrolase, HD subdomain; KEGG: ajs:Ajs_1963 metal dependent phosphohydrolase.
 
 
 0.664
AEB86683.1
Metal dependent phosphohydrolase; TIGRFAM: Uncharacterised protein family HDIG; PFAM: Metal-dependent phosphohydrolase, HD subdomain; KEGG: dia:Dtpsy_0366 metal dependent phosphohydrolase; SMART: Metal-dependent phosphohydrolase, HD domain.
 
 0.656
AEB83535.1
Metal dependent phosphohydrolase; TIGRFAM: Uncharacterised protein family HDIG; PFAM: Metal-dependent phosphohydrolase, HD subdomain; KEGG: aav:Aave_1533 metal dependent phosphohydrolase; SMART: Metal-dependent phosphohydrolase, HD domain.
 
 
 0.645
AEB86480.1
TIGRFAM: Diguanylate cyclase, predicted; PFAM: Diguanylate phosphodiesterase, EAL domain; Diguanylate cyclase, predicted; KEGG: rfr:Rfer_2485 diguanylate cyclase/phosphodiesterase; SMART: Diguanylate phosphodiesterase, EAL domain; Diguanylate cyclase, predicted.
 
 
0.623
AEB82555.1
Diguanylate cyclase/phosphodiesterase with PAS/PAC sensor(s); TIGRFAM: Diguanylate cyclase, predicted; PAS; PFAM: Diguanylate phosphodiesterase, EAL domain; Diguanylate cyclase, predicted; PAS fold; PAS fold-4; KEGG: ajs:Ajs_0088 diguanylate cyclase/phosphodiesterase with PAS/PAC sensor(s); SMART: Diguanylate phosphodiesterase, EAL domain; Diguanylate cyclase, predicted; PAC motif; PAS.
 
0.620
AEB86773.1
Diguanylate cyclase/phosphodiesterase with PAS/PAC and GAF sensor(s); TIGRFAM: Diguanylate cyclase, predicted; PAS; PFAM: Diguanylate cyclase, predicted; PAS fold; GAF; Diguanylate phosphodiesterase, EAL domain; KEGG: bxe:Bxe_C0015 diguanylate cyclase/phosphodiesterase with PAS/PAC sensor(s); SMART: Diguanylate phosphodiesterase, EAL domain; Diguanylate cyclase, predicted; PAS; PAC motif; GAF.
 
0.608
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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