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
gatCaspartyl/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. (96 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.
 
 0.999
gatA
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).
 
 0.998
AFZ59724.1
PFAM: Amidase; TIGRFAM: amidohydrolase, AtzE family; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120:IPR014087; KEGG: ana:alr1018 amidase; PFAM: Amidase; SPTR: Glu-tRNA(Gln) amidotransferase subunit A; TIGRFAM: Amidohydrolase, AtzE type.
 
 0.990
AFZ57550.1
PFAM: Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: naz:Aazo_0334 amidase; PFAM: Amidase; SPTR: Amidase; Belongs to the amidase family.
 
 
 0.981
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; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: naz:Aazo_3649 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb.
   
 0.961
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.
  
 
 0.884
dapA
Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
  
  
 0.787
rpsN
SSU ribosomal protein S14P; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family.
   
    0.779
atpH
ATP synthase F1 subcomplex delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
  
    0.776
AFZ57943.1
PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II; COGs: COG0069 Glutamate synthase domain 2; InterPro IPR000583:IPR006982:IPR002932:IPR002489; KEGG: naz:Aazo_0653 glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal; PRIAM: Glutamate synthase (ferredoxin); SPTR: Glutamate synthase (Ferredoxin).
   
 
 0.690
Your Current Organism:
Anabaena cylindrica
NCBI taxonomy Id: 272123
Other names: A. cylindrica PCC 7122, Anabaena cylindrica IAM M-1, Anabaena cylindrica NIES-19, Anabaena cylindrica PCC 7122, Anabaena cylindrica UTEX B 629, Anabaena sp. ATCC 27899, Anabaena sp. PCC 7122
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.