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
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fmtmethionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. (320 aa)    
Predicted Functional Partners:
Rmag_0209
16S rRNA m(5)C-967 methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
  
 0.991
purN
Phosphoribosylglycinamide formyltransferase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
 
  
0.929
metG
methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
     
 0.919
purH
KEGG: tcx:Tcr_0439 phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; TIGRFAM: phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PFAM: AICARFT/IMPCHase bienzyme; MGS domain protein.
     
 0.919
def
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
 
 0.914
Rmag_0686
PFAM: protein kinase; protein phosphatase 2C domain protein; SMART: tyrosine protein kinase; serine/threonine protein kinase; KEGG: hch:HCH_05817 serine/threonine protein kinase.
  
   0.849
folD
5,10-methylenetetrahydrofolate dehydrogenase (NADP+) / methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
 
  
 0.820
argH
TIGRFAM: argininosuccinate lyase; PFAM: fumarate lyase; KEGG: sde:Sde_3670 response regulator receiver domain protein (CheY-like).
       0.783
priA
Primosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily.
  
    0.667
nusB
NusB antitermination factor; Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
  
  
 0.645
Your Current Organism:
Ruthia magnifica
NCBI taxonomy Id: 413404
Other names: C. Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica strain Cm (Calyptogena magnifica), Ruthia magnifica str. Cm (Calyptogena magnifica)
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