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_0541Conserved hypothetical protein; Similar to GP:1001812 percent identity: 32.62; identified by sequence similarity; putative; Belongs to the archaeal NMN adenylyltransferase family. (168 aa)    
Predicted Functional Partners:
nadE
NH(3)-dependent NAD+ synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
    
 0.966
nadC
Nicotinate-nucleotide pyrophosphorylase (nadC); Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family.
    
 0.953
MJ_0540
Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ0540.
       0.940
MJ_0917
Conserved hypothetical protein; Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as phosphoryl donors, however poly(P) is not considered to be the phys [...]
    
 0.924
surE
surE stationary-phase survival protein SurE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family.
     
  0.900
ppsA
Phosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
 
     0.639
MJ_1385
Conserved hypothetical protein; Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs; Belongs to the aTrm56 family.
 
     0.622
tiaS
Conserved hypothetical protein; 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.
  
     0.619
ribK
Conserved hypothetical protein; Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN). Can also utilize UTP as the phosphate donor, although less efficiently, and it is unclear if ATP and GTP can also serve as substrates or not.
 
     0.601
nadA
Quinolinate synthetase (nadA); Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
     
 0.563
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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