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
gatBaspartyl/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. (546 aa)    
Predicted Functional Partners:
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).
 0.999
AEB07537.1
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.
 
 0.999
asnS
COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR002312:IPR004522:IPR006195:IPR004365:IPR 004364; KEGG: apv:Apar_0370 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Putative uncharacterized protein; TIGRFAM: asparaginyl-tRNA synthetase; IMG reference gene:2503576180; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase.
 
 0.997
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.
 
 0.968
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
 
 0.930
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.
  
 
 0.829
AEB06595.1
Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain protein; COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterPro IPR020058:IPR001412:IPR020060; KEGG: apv:Apar_1332 glutamate--tRNA ligase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; SPTR: Putative uncharacterized protein; IMG reference gene:2503575259; PFAM: tRNA synthetases class I (E and Q), catalytic domain; TIGRFAM: glutamyl-queuosine tRNA(Asp) synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.795
pheT
COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR004532:IPR002547:IPR005121:IPR005146:IPR 005147; KEGG: apv:Apar_1054 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Putative uncharacterized protein; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; IMG reference gene:2503576306; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta su [...]
  
  
 0.728
rpoC
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
  
 0.706
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.
  
  
 0.656
Your Current Organism:
Coriobacterium glomerans
NCBI taxonomy Id: 700015
Other names: C. glomerans PW2, Coriobacterium glomerans DSM 20642, Coriobacterium glomerans PW2, Coriobacterium glomerans str. PW2, Coriobacterium glomerans strain PW2
Server load: low (10%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.