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
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Co-expression
Experiments
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[Homology]
Score
azo3289Putative exonuclease of the beta-lactamase fold involved in RNA processing, C-terminal fragment; Family membership. (216 aa)    
Predicted Functional Partners:
azo3288
Putative exonuclease of the beta-lactamase fold involved in RNA processing, N-terminal fragment; Family membership.
     0.991
azo1211
Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs.
    
 0.902
azo0839
SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear.
    
 0.759
dnaL
DNA ligase (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]). CATALYZES EFFICIENT STRAND JOINING ON A SINGLE NICKED DNA. InterPro: ATP-dependent DNA ligase; Specificity unclear.
 
 
 0.759
azo3907
Conserved hypothetical protein. Homology to xac4125 of X. axonopodis of 42% (trembl|Q8PF60). Domain structure: 5 x TRP, 50 aa - 83 aa; 84 aa - 117 aa; 118 aa - 151 aa; 152 aa - 182 aa; 186 aa - 219 aa. InterPro: TPR repeat (IPR001440); SAM (and some other nucleotide) binding motif (IPR000051). Pfam: TPR daomian. no signal peptide. no TMHs.
   
  0.708
azo1741
Putative DNA-ligase like protein Rv0938/MT0965. dnl1: DNA ligase I ATP-dependent; Specificity unclear; ORF4.
   
 0.707
lig2
DNA ligase (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]). This protein seals during DNA replication DNA recombination and DNA repair nicks in double-stranded DNA (By similarity); High confidence in function and specificity.
   
 0.698
azo2784
Conserved hypothetical monoamine oxidase. Homology to rsp0431 of R. solanacearum of 34% (trembl|Q8XSN6). In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. InterPro: Amine oxidase (IPR002937). Pfam: Flavin containing amine oxidase. probable signal peptide. no TMH; Family membership.
    
  0.695
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.
   
 
  0.686
azo0531
Conserved hypothetical secreted protein. Homology to PA2778 of P.aeruginosa of 39% (trembl|Q9I065(SRS)) Has Signal Peptide. No TMH present. Has PF03412:Peptidase C39 family;Lantibiotic and non-lantibiotic bacteriocins are synthesised as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 an [...]
   
  0.664
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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