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
PH0445219aa long hypothetical protein; Similar to PIR:A64441 percent identity: 42.458 in 187aa. motif=protein kinases signatures and profile. (219 aa)    
Predicted Functional Partners:
PH1987
324aa long hypothetical O-sialoglycoprotein endopeptidase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity.
   
 0.982
PH0770
154aa long hypothetical protein; Motif=mitochondrial energy transfer proteins signature.
    
 
 0.937
PH0993
723aa long hypothetical methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
    
 0.743
PH0435
340aa long hypothetical protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
  
  
 0.655
PH0058
158aa long hypothetical 40S ribosomal protein S13; Similar to Swiss_Prot:P54012 percent identity: 70.667 in 157aa; Swiss_Prot:Q05761 percent identity: 50.000 in 157aa; Swiss_Prot:P49203 percent identity: 48.649 in 155aa. motif=ribosomal protein S15 signature.
 
   
 0.578
PH1262
617aa long hypothetical prolyl endopeptidase; Similar to PIR:JC4084 percent identity: 85.552 in 616aa; Swiss_Prot:Q06903 percent identity: 48.971 in 256aa; owl:MTCI429A percent identity: 42.982 in 235aa.
      
 0.574
PH1544
397aa long hypothetical DNA-directed RNA polymerase subunit A'; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 0.529
PH1545
907aa long hypothetical DNA-directed RNA polymerase subunit A; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 0.528
PH1694
445aa long hypothetical signal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily.
 
   
 0.499
PH1095
1044aa long hypothetical translation initiation factor IF-2; Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity).
 
  
 0.486
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
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