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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene co-occurrence
gene fusions
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[Homology]
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pyrGCTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. (552 aa)    
Predicted Functional Partners:
ndk
Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family.
  
 
 0.946
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
 
 
 0.944
rpoB
DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 
 0.930
MCA0046
MazG family protein; Identified by similarity to OMNI:CC1747; match to protein family HMM PF03819; match to protein family HMM TIGR00444.
    
  0.920
maf-1
Maf protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
    
  0.905
rpsB
Ribosomal protein S2; Identified by similarity to SP:P02351; match to protein family HMM PF00318; match to protein family HMM TIGR01011; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.888
lepA
GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
  
  
 0.864
ileS
isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.
  
  
 0.852
leuS
leucyl-tRNA synthetase; Identified by match to protein family HMM PF00133; match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.845
rplB
Ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
   
 
 0.833
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
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