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_1428O-linked GlnNAc transferase; Similar to GB:AE000666 percent identity: 34.08; identified by sequence similarity; putative. (567 aa)    
Predicted Functional Partners:
MJ_1427
Hypothetical protein; Catalyzes the condensation of 4-aminobenzoate (pABA) with 5- phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta- ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P).
       0.926
MJ_1450
Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 37.27; identified by sequence similarity; putative.
 
 
 0.858
alaS
alanyl-tRNA synthetase (alaS); Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala) (By similarity). Also functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala), and maybe also from Gly-tRNA(Ala).
   
 0.847
rpoD
DNA-directed RNA polymerase, subunit D (rpoD); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 0.830
rpoH
DNA-directed RNA polymerase, subunit H (rpoH); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates; Belongs to the archaeal RpoH/eukaryotic RPB5 RNA polymerase subunit family.
  
 0.817
MJ_0920
GTP-binding protein homologue (yphC); Similar to PID:1146219 SP:P50743 GB:AL009126 percent identity: 26.99; identified by sequence similarity; putative.
  
 0.814
herA
Conserved hypothetical protein; Involved in DNA double-strand break (DSB) repair (By similarity). Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity (By similarity); Belongs to the HerA family.
 
   
 0.813
rpoB2
DNA-directed RNA polymerase, subunit B'' (rpoB2); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. The B (B''+B' and beta) subunits have been implicated in DNA promoter recognition and also in nucleotide binding.
  
 0.810
rpoB1
DNA-directed RNA polymerase, subunit B' (rpoB1); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. The B (B''+B' and beta) subunits have been implicated in DNA promoter recognition and also in nucleotide binding.
  
 0.810
rpoK
DNA-directed RNA polymerase, subunit K (rpoK); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoK/eukaryotic RPB6 RNA polymerase subunit family.
  
 0.808
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.