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_1110Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 30.00; identified by sequence similarity; putative. (486 aa)    
Predicted Functional Partners:
cca
tRNA nucleotidyltransferase (cca); Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.
  
    0.936
MJ_1113
N-acetylglucosamine-1-phosphate transferase; Similar to GB:D28748 SP:P39465 PID:506372 percent identity: 28.00; identified by sequence similarity; putative.
       0.577
cobD
Cobalamin biosynthesis protein B (cbiB); Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
  
    0.551
fucA
Fuculose-1-phosphate aldolase (fucA); Involved in the biosynthesis of the coenzyme F420 which requires phospholactate produced via the aldol cleavage of L-fuculose 1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde. Catalyzes the reversible cleavage of L-fuculose 1- phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S- lactaldehyde (Ref.2,. FucA possesses a high specificity for the dihydroxyacetone phosphate (DHAP), but accepts a great variety of different aldehydes such as DL-glyceraldehyde and glycolaldehyde.
   
    0.463
top6A
DNA topoisomerase VI, subunit A (top6A); Relaxes both positive and negative superturns and exhibits a strong decatenase activity; Belongs to the TOP6A family.
       0.431
MJ_0443
Conserved hypothetical protein; Similar to GB:X59720 SP:P25586 PID:5300 percent identity: 27.78; identified by sequence similarity; putative.
       0.431
rio1
Conserved hypothetical protein; Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity).
       0.431
eIF1A
Translation initiation factor aIF-1A; Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity).
       0.431
mptA
Conserved hypothetical protein; Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin. It is also able to utilize a variety of GTP analogs as substrates, including GDP, beta,gamma-methylene-GTP and GTP-[gamma- thio]; Belongs to the GTP cyclohydrolase IV family.
       0.431
top6B
DNA topoisomerase VI, subunit B (top6B); Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
       0.431
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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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.