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
MJ_0670Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 37.37; identified by sequence similarity; putative. (356 aa)    
Predicted Functional Partners:
bioB
Biotin synthetase (bioB); Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.
   
    0.816
MJ_0486
Conserved hypothetical protein; Similar to SP:P45476 PID:606150 GB:U00096 PID:2367204 percent identity: 29.79; identified by sequence similarity; putative.
     0.815
tgtA
Queuine tRNA-ribosyltransferase (tgtA); Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs. Can also utilize guanine as substrate.
     
 0.801
arfC
Riboflavin-specific deaminase (ribG); Catalyzes an early step in riboflavin biosynthesis, the NAD(P)H-dependent reduction of the ribose side chain of 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6- ribitylamino-4(3H)-pyrimidinone 5'-phosphate. The beta anomer is the authentic substrate, and the alpha anomer can serve as substrate subsequent to spontaneous anomerization. NADPH and NADH function equally well as the reductants. Does not catalyze the reduction of 5- amino-6-(5-phospho-D-ribosylamino)uracil to 5-amino-6-(5-phospho-D- ribitylamino)uracil; [...]
       0.780
nadE
NH(3)-dependent NAD+ synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
 
  
 0.665
MJ_0669
ATP-dependent RNA helicase, DEAD-family (deaD); Similar to GB:L42023 SP:P44586 PID:1003361 PID:1222156 PID:1204489 percent identity: 43.17; identified by sequence similarity; putative; Belongs to the DEAD box helicase family.
       0.605
MJ_0672
Membrane bound transport protein, putative; Similar to GB:L42023 PID:1005433 PID:1220685 PID:1204859 SP:Q57486 percent identity: 40.00; identified by sequence similarity; putative.
       0.603
trm14
Conserved hypothetical protein; S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the guanosine nucleotide at position 6 (m2G6) in tRNA(Cys).
 
   
 0.560
cfbE
Conserved hypothetical protein; Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the activation the g-propionate side chain of 15,17(3)-seco-F430-17(3)-acid (seco-F430) for intramolecular C-C bond formation to yield the carbocyclic F ring of coenzyme F430. Belongs to the MurCDEF family.
  
    0.543
comB
Conserved hypothetical protein; Hydrolyzes both enantiomers of 2-phosphosulfolactate. Able to hydrolyze both enantiomers of 2-hydroxycarboxylic acids with pseudosymmetric centers of inversion. Specifically hydrolyzes (S)- phospholactate and (S)-phosphoglycerate.
 
    0.529
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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