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
AFZ47459.1PFAM: Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: cyp:PCC8801_1372 amidase; PFAM: Amidase; SPTR: Amidase. (471 aa)    
Predicted Functional Partners:
gatB
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
 
 
 0.993
gatC
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
 
 
 0.990
AFZ46294.1
Hypothetical protein; COGs: COG1541 Coenzyme F390 synthetase; KEGG: ate:Athe_2035 coenzyme F390 synthetase-like protein; SPTR: Coenzyme F390 synthetase-like protein.
    
  0.903
AFZ46438.1
PFAM: Aldehyde dehydrogenase family; COGs: COG1012 NAD-dependent aldehyde dehydrogenase; InterPro IPR015590:IPR012394:IPR016160; KEGG: ava:Ava_3615 aldehyde dehydrogenase; PFAM: Aldehyde Dehydrogenase; SPTR: Aldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family.
    
 0.902
AFZ46488.1
KEGG: cyt:cce_0494 hypothetical protein; SPTR: Putative uncharacterized protein.
  
 
 0.714
asnS
PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase; COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR004522:IPR004365:IPR004364:IPR006195:IPR 002312; KEGG: cyc:PCC7424_2654 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase.
   
 
 0.714
gltX
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 
 0.714
AFZ46264.1
AMP-dependent synthetase and ligase; PFAM: AMP-binding enzyme; COGs: COG0318 Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; InterPro IPR020845:IPR000873; KEGG: cyc:PCC7424_1874 beta-ketoacyl synthase; PFAM: AMP-dependent synthetase and ligase; SPTR: Beta-ketoacyl synthase.
  
 
 0.696
AFZ46265.1
Beta-ketoacyl synthase; PFAM: Acyl transferase domain; Phosphopantetheine attachment site; KR domain; Beta-ketoacyl synthase, N-terminal domain; AMP-binding enzyme; Sulfotransferase domain; Beta-ketoacyl synthase, C-terminal domain; COGs: COG3321 Polyketide synthase modules and related protein; InterProIPR000639:IPR009081:IPR006162:IPR018201:IPR 000873:IPR006163:IPR014030:IPR014031:IPR014043:IPR013968:I PR000863:IPR000073; KEGG: cyc:PCC7424_1874 beta-ketoacyl synthase; PFAM: Beta-ketoacyl synthase; phosphopantetheine-binding; AMP-dependent synthetase and ligase; Acyl transferase; KR do [...]
  
 
 0.696
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
 
 0.649
Your Current Organism:
Cyanobacterium stanieri
NCBI taxonomy Id: 292563
Other names: C. stanieri PCC 7202, Cyanobacterium stanieri PCC 7202, Synechococcus cedrorum CCAP 14792a (no longer available), Synechococcus cedrorum CCAP 14792b (no longer available), Synechococcus cedrorum M137/1a, Synechococcus cedrorum SAG 88.79, Synechococcus sp. ATCC 29140, Synechococcus sp. PCC 7202
Server load: medium (42%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.