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
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[Homology]
Score
tiaStRNA(Ile2) 2-agmatinylcytidine synthetase TiaS; ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA. (429 aa)    
Predicted Functional Partners:
truB
Putative tRNA pseudouridine synthase B; Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 2 subfamily.
      
 0.748
thiI
Putative tRNA sulfurtransferase; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
      
 0.745
ribK
Riboflavin kinase; Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN); Belongs to the archaeal riboflavin kinase family.
  
     0.656
MCBB_1950
tRNA (cytidine(56)-2'-O)-methyltransferase; Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs; Belongs to the aTrm56 family.
  
     0.656
nob1
Endoribonuclease Nob1; Toxic component of a toxin-antitoxin (TA) module. Processes pre-16S-rRNA at its 3' end (the D-site) to yield the mature 3' end (By similarity). Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; PINc domain which binds Mn(2+), rRNA substrate and probably has endoribonuclease activity, and the C-terminal zinc ribbon domain which also binds rRNA substrate. Rule:MF_00265}; sp|O27890|NOB1_METTH;evalue=1e-041; PctID=48.10; score=168.
 
     0.653
MCBB_1199
Nicotinamide-nucleotide adenylyltransferase; sp|O26253|NADM_METTH;evalue=6e-075; PctID=75.72; score=279.
  
     0.640
MCBB_1627
UPF0218 protein; Catalyzes the GTP-dependent phosphorylation of the 3'- hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
 
     0.621
pfdB
Prefoldin subunit beta; Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.
  
     0.603
MCBB_1888
Putative HTH-type transcriptional regulatory protein MTH_967; sp|O27048|Y967_METTH;evalue=3e-091; PctID=54.21; score=335; {ECO:0000255|HAMAP-Rule:MF_00584}.
 
     0.582
MCBB_0501
Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway. phosphopantoate. Kinetic parameters: KM=0.47 mM for ATP; KM=1.2 mM for (R)-pantoate; KM=1.3 mM for (R)-pantothenate; Vmax=2870 nmol/min/mg enzyme with (R)-pantoate as substrate; Vmax=390 nmol/min/mg enzyme with (R)-pantothenate as substrate; phosphopantothenate; sp|Q5JHF1|POK_THEKO;evalue=5e-034; PctID=36.68; score=145.
 
     0.576
Your Current Organism:
Methanobacterium congolense
NCBI taxonomy Id: 118062
Other names: DSM 7095, M. congolense, Methanobacterium congolense Cuzin et al. 2001, OCM 786, strain C
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