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
gatBglutamyl-tRNA(Gln) amidotransferase, B subunit; 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. (497 aa)    
Predicted Functional Partners:
gatC
glutamyl-tRNA(Gln) amidotransferase, C subunit; 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.
  
 0.999
gatA
glutamyl-tRNA(Gln) amidotransferase, A subunit; 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).
 
 0.999
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.
 
 0.985
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
 
 0.953
pheT
COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR020825:IPR005121:IPR016027:IPR009061:IPR 004532:IPR002547:IPR012340:IPR005147:IPR005146; KEGG: jde:Jden_1109 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: D0WN31 Phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synt [...]
  
  
 0.793
gluSR
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.
  
 
 0.779
Arch_0178
Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain protein; COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterPro IPR020058:IPR014729:IPR020060:IPR001412; KEGG: mgi:Mflv_1233 glutamyl-Q tRNA(Asp) synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; SPTR: D0WLH0 Glutamate--tRNA ligase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.715
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
   
  
 0.686
Arch_0418
Phospholipase D/Transphosphatidylase; COGs: COG1502 Phosphatidylserine/phosphatidylglycerophosphate/ cardiolipin synthase; InterPro IPR001736; KEGG: xce:Xcel_1743 phospholipase D/transphosphatidylase; PFAM: phospholipase D/Transphosphatidylase; SMART: phospholipase D/Transphosphatidylase; SPTR: D0WS38 Cardiolipin synthetase; PFAM: Phospholipase D Active site motif.
       0.623
Arch_0422
Malic protein NAD-binding protein; COGs: COG0281 Malic enzyme; InterPro IPR016040:IPR015884:IPR012301:IPR012302; KEGG: nca:Noca_2034 malate dehydrogenase; PFAM: malic protein NAD-binding; malic protein domain protein; SPTR: D0WL78 NADP-dependent malic enzyme; PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain.
  
    0.615
Your Current Organism:
Arcanobacterium haemolyticum
NCBI taxonomy Id: 644284
Other names: A. haemolyticum DSM 20595, Arcanobacterium haemolyticum ATCC 9345, Arcanobacterium haemolyticum CIP 103370, Arcanobacterium haemolyticum DSM 20595, Arcanobacterium haemolyticum str. DSM 20595, Arcanobacterium haemolyticum strain DSM 20595
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