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
EHA64152.1Endoribonuclease L-PSP; KEGG: pmf:P9303_08201 putative translation initiation inhibitor, YjgF family protein; TIGRFAM: YjgF-like protein; PFAM: Endoribonuclease L-PSP. (132 aa)    
Predicted Functional Partners:
fusA
Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]
    
 0.870
ilvA
Threonine dehydratase, biosynthetic; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
 
 0.868
EHA63257.1
PFAM: Phosphoribosyltransferase; KEGG: pmt:PMT0810 adenine phosphoribosyltransferase.
 
 
 0.850
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
  
 
 0.803
EHA63015.1
TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT.
    
  0.732
EHA64196.1
TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: pmf:P9303_07681 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
    
  0.732
EHA64006.1
KEGG: cbu:CBU_1204 succinate-semialdehyde dehydrogenase; PFAM: Aldehyde dehydrogenase domain.
   
 0.636
EHA60241.1
PFAM: Aldehyde dehydrogenase domain; KEGG: pmt:PMT0191 putative aldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family.
   
 0.636
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
    
 0.592
EHA64151.1
Fe(3+)-transporting ATPase; PFAM: ABC transporter-like; KEGG: pmf:P9303_17671 ABC transporter ATP-binding protein; SMART: ATPase, AAA+ type, core.
       0.579
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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