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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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
MMP1217Conserved hypothetical archaeal protein. (219 aa)    
Predicted Functional Partners:
MMP1218
Conserved hypothetical protein.
  
    0.973
sepS
Phenylalanyl-tRNA synthetase alpha subunit; Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).
   
 
 0.964
MMP1240
Conserved hypothetical protein; Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L- cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)); Belongs to the SepCysS family.
   
 
 0.950
2pgk
2-phosphoglycerate kinase; Citation: Mol. Gen. Genet. 242 (2), 163-168 (1994); FEBS Lett. 272:94-98.
  
    0.854
pheS
Phenylalanyl-tRNA synthetase alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
    
   0.683
hisC
Histidinol-phosphate aminotransferase; Citation: Conover RK, Doolittle WF. (1990) J Bacteriol 172:3244-9.
  
    0.666
cobQ
Cobyrinic acid a,c-diamide synthase:Cobyric acid synthase CobQ; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.
  
    0.514
MMP1219
Putative dinG ATP-dependent helicase; Citation: J Biol Chem. 2003 279: 29294-28293.
       0.474
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).
   
  
 0.474
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
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