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
azo1211Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. (357 aa)    
Predicted Functional Partners:
alaS
AlaS protein; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
   
 0.975
azo0443
Beta-lactamase; Conserved Hypothetical protein(Metallo-beta-lactamase superfamily). Has PF00753, Metallo-beta-lactamase superfamily; IPR001279, Blactmase-like;These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor; Family membership.
    
 0.950
azo3288
Putative exonuclease of the beta-lactamase fold involved in RNA processing, N-terminal fragment; Family membership.
    
 0.950
azo3289
Putative exonuclease of the beta-lactamase fold involved in RNA processing, C-terminal fragment; Family membership.
    
 0.950
azo0839
SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear.
   
 0.940
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.
  
 
 0.927
azo1210
Putative GTPase; TREMBLnew:CAE26305: 46% identity, 65% similarity. sprot:YJIA_ECOLI, 33% identity, 55% similarity Hypothetical protein. Pfam:cobW: Cobalmine synthesis protein; ABC_tran TIGRFAM: MMR_HSR1- GTPASE of unknown function InterPro: Cobalamin synthesis protein/P47K mobB: molybdopterin-guanine dinucleotid; Conserved hypothetical protein.
 
   
 0.918
azo1095
Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient protein superfamily, TREMBL:Q7VZF1 (58% identity); TREMBL:Q7NRU4 (57% identity). InterPro (IPR000286): Histone deacetylase family Pfam (PF00850): Histone deacetylase domain; Family membership.
    
 0.917
azo1601
Histone deacetylases catalyse the removal of the acetyl group from histones. Histone deacetylase, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of an ancient family, TREMBL:Q7NVL6 (58% identity); TREMBL:Q8XZ00 (57% identity). InterPro (IPR000286): Histone deacetylase superfamily Pfam (PF00850): Histone deacetylase domain; Family membership.
    
 0.917
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 [...]
    
 0.916
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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