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.
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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
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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
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[Homology]
Score
mucD2Probable serine protease MucD. Homology to mucD of P. aruginosa of 47% (trembl|Q57155) InterPro: Serine proteases trypsin family (IPR001254); PDZ domain (also known as DHR or GLGF) (IPR001478); Chymotrypsin serin protease family (S1) (IPR001314); HtrA/DegQ protease family (IPR001940) Pfam: Trypsin; PDZ domain (also known as DHR or GLGF) signal peptide no TMHs ahpD_dom: alkylhydroperoxidase AhpD fam; High confidence in function and specificity; Belongs to the peptidase S1C family. (472 aa)    
Predicted Functional Partners:
rseA
Putative sigma-E factor, negative regulatory protein,; High confidence in function and specificity.
  
 
 0.929
glpK
Probable glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family.
   
 0.828
rseC
Putative sigma-E factor regulatory protein RseC,; High confidence in function and specificity.
  
  
 0.806
rseB
Putative sigma factor regulatory protein,; High confidence in function and specificity.
  
  
 0.789
azo1635
Thioredoxin-disulfide reductase; Conserved hypothetical thioredoxin. Homology to a putative thioredoxin of N. menigitidis (NMA0966) of 50%. Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. no signal peptide no TMHs; Function unclear.
   
   0.786
algU
RNA polymerase sigma factor, Myxococcus xanthus carQ; Alcaligenes eutrophus plasmid pMOL28-encoded cnrH; Escherichia coli fecI; Pseudomonas syringae hrpL; rpoE from Escherichia coli, Salmonella typhimurium and Haemophilus influenzae; Streptomyces coelicolor sigE; and Bacillus subtilis sigma factors sigV, sigX, sigY and sigZ; High confidence in function and specificity; Belongs to the sigma-70 factor family. ECF subfamily.
     
 0.767
lepB
LepB protein; Signal peptidase I (EC 3.4.21.89) (SPase I) (Leader peptidase I). SPase I is an integral membrane protein that is anchored in the cytoplasmic membrane by one or two N-terminal transmembrane domains, with the main part of the protein protuding in the periplasmic space. SPase I can cleave N-terminal leader sequences of nonlipoprotein that are exported by the SecYEG pathway or the twin arginine translocation (Tat) pathway. Pfam: Peptidase_S26 probable 2 TMH no signal peptide; High confidence in function and specificity.
 
  
 0.690
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 [...]
   
  0.686
ank1
Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% 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. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...]
   
  0.683
tnkS
Putative tankyrase type protein; Tankyrase 2 (EC 2.4.2.30) (TANK2) (Tankyrase II) (TNKS-2) (TRF1- interacting ankyrin-related ADP-ribose polymerase 2) (Tankyrase-like protein) (Tankyrase-related protein). May regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Has PARP activity and can modify TRF1 and thereby contribute to the regulation of telomere length. TREMBL:Q800E0:34%; Q8YTG9:36% identity. InterPro: Ankyrin-repeat Mop: molybdenum-pterin binding domain Presence of signal peptide (SignalP) but absence of transmembrane helices; Function [...]
    
  0.680
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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