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
PH0183318aa long hypothetical protein. (318 aa)    
Predicted Functional Partners:
PH0182
257aa long hypothetical NH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
  
   0.785
PH0456
314aa long hypothetical protein; Similar to owl:ECAE0002042 percent identity:33.645 in 223aa.
  
 
 0.668
PH0184
149aa long hypothetical molybdopterinconverting factor, subunit; Similar to owl:MTCY16429 percent identity: 38.525 in 122aa; owl:ATAC00233312 percent identity: 34.752 in 141aa; Swiss_Prot:P30749 percent identity: 40.171 in 117aa. motif=tonB-dependent receptor proteins signatures.
  
    0.621
PH1637
261aa long hypothetical DNA-directed RNA polymerase subunit D; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoD/eukaryotic RPB3 RNA polymerase subunit family.
  
 0.597
PH1546
1117aa long hypothetical DNA-directed RNA polymerase subunit B; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 0.588
PH1804
441aa long hypothetical protein; Similar to owl:AB002406 percent identity: 49.883 in 443aa; PIR:S52698 percent identity: 48.219 in 435aa; PIR:S61029 percent identity: 45.564 in 431aa. motif=ATP/GTP-binding site motif A (P-loop).
   
 0.565
PHS044
82aa long hypothetical DNA-directed RNA polymerase subunit Hprotein; 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.
   
 0.556
PH0108
216aa long hypothetical alanyl-tRNA synthetase; Functions in trans to edit the amino acid moiety from mischarged charged Gly-tRNA(Ala) and Ser-tRNA(Ala). Belongs to the class-II aminoacyl-tRNA synthetase family. Editing domain AlaX-M subfamily.
   
 0.533
PH0297
915aa long hypothetical alanyl-tRNA synthetase; 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). Edits incorrectly charged Ser-tRNA(Ala). Incorrectly charged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Gly and Ser) in the charging step. Belongs to the class-II aminoacyl-tRNA synthetase family.
   
 0.533
PHS056
77aa long hypothetical DNA-directed RNA polymerase; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoP/eukaryotic RPC10 RNA polymerase subunit family.
  
 0.533
Your Current Organism:
Pyrococcus horikoshii
NCBI taxonomy Id: 70601
Other names: P. horikoshii OT3, Pyrococcus horikoshii OT-3, Pyrococcus horikoshii OT3, Pyrococcus horikoshii str. OT3, Pyrococcus shinkaii OT3, Pyrococcus sp. OT3
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.