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
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
azo1261Conserved hypothetical membrane protein. Homology to Bll7266 of B. japonicum of 45% (trembel:Q89E21) InterPro:IPR007621; DUF477. Pfam:PF04536; DUF477 Signal peptide present (Signal P predicted). Presence of 2 transmembrane helices; Conserved hypothetical protein. (310 aa)    
Predicted Functional Partners:
lemA1
Conserved hypothetical LemA family protein; Putative lipoprotein [lemA],57 % identity (75% similarity) to TrEMBL;Q72TG3,TrEMBL;Q6N9H6(60% identity). No signl peptide or TMH present. Has PF04011:LemA family(IPR007156,lemA);The members of this family are related to the LemA protein. LemA contains an amino terminal predicted transmembrane helix. It has been predicted that the small amino terminus is extracellular [1]. The exact molecular function of this protein is uncertain; Conserved hypothetical protein.
 
  
 0.959
azo1260
Conserved hypothetical protein. Homology to RPA1575 of R.palustris of 41% (tremble:Q6N9H4). Has PF04536:(IPR007621)Domain of unknown function (DUF477);This is a family of uncharacterised proteins. They are found in both eukarya and eubacteria. No TMHs. No signal peptide.
 
     0.921
coxB
Conserved hypothetical cytochrome c oxidase,subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
    
   0.878
petB
Ubiquinol-cytochrome c reductase cytochrome b protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
    
   0.785
coxC
Cytochrome c oxidase polypeptide III Subunits I II and III form the functional core of the enzyme complex. InterPro: Cytochrome c oxidase subunit III; High confidence in function and specificity.
    
   0.744
lemA2
Conserved hypothetical lemA family protein; Putative cytoplasmic membrane protein, lemA, 41% identity(63% similarity) to TrEMBL;Q9FA50.TrEMBL;Q7CNK7(37% identity). Has PF04011,LemA family;IPR007156;The members of this family are related to the LemA protein P71452. LemA contains an amino terminal predicted transmembrane helix. It has been predicted that the small amino terminus is extracellular. The exact molecular function of this protein is uncertain; Conserved hypothetical protein.
 
  
 0.734
qoxA
Probable quinol oxidase, subunit I. Homology to qoxA of R. sphaeroides of 52% (trembl|Q9Z605). InterPro: Cytochrome c oxidase subunit III (IPR000298); Cytochrome coxidase, subunit I (IPR000883) Pfam: Cytochrom C and quinol oxidase poly polypeptide signal peptide 17 TMHs; Family membership; Belongs to the heme-copper respiratory oxidase family.
    
   0.733
coxA
Probable cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
    
   0.733
qoxB
Probable quniol oxidase, subunit II. Homology to qoxB of Rhodobacter sphaeroides of 41% (gi|4416093|gb|AAD20226.1|(NBCI ENTREZ)). InterPro: Cytochrome c oxidase subunit II (IPR002429); Cu(A) centre of cytochrome c oxidase, subunit II and nitrous oxide reductase (IPR001505). Pfam: Cytochrome c oxidase subunit II, periplasmic. no signal peptide. 2 TMHs; Family membership.
    
   0.727
azo1919
Probable oxidoreductase; Hypothetical protein MG039 homolog (D09_orf384). D-amino acid oxidase (EC: 1.4.3.3) (DAMOX or DAO) is an FAD flavoenzyme that catalyzes the oxidation of neutral and basic D-amino acids into their corresponding keto acids. DAOs have been characterized and sequenced in fungi and vertebrates where they are known to be located in the peroxisomes. InterPro: D-amino acid oxidase Putative conserved exported protein. TREMBL:Q7WG75: 55% identity,65% similarity. TREMBLnew:CAE29609. Pfam:NAD binding FAD dependent oxidoreductase. TIGRFAM:UDP-GALP mutase. Signal P predicted [...]
    
   0.683
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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