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_0480Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 27.49; identified by sequence similarity; putative. (198 aa)    
Predicted Functional Partners:
adkA
Adenylate kinase (adk); Similar to PID:1086550 PID:1591182 percent identity: 100.00; identified by sequence similarity; putative; Belongs to the archaeal adenylate kinase family.
 
    0.957
MJ_0606
Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 32.18; identified by sequence similarity; putative.
   
  
 0.887
secY
Protein translocase, subunit SEC61 alpha (secY); The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
 
    0.878
srp54
Signal recognition particle, subunit SRP54; 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.
     
 0.690
aglB
Putative transmembrane oligosaccharyl transferase; Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcGlc-2,3-diNAcAGlcNAc in Methanococci) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins.
  
     0.616
rpl15
LSU ribosomal protein L15P (rplO); Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
 
    0.606
rpl24
LSU ribosomal protein L24P (rplX); One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
 
     0.588
rps5
SSU ribosomal protein S5P (rpsE); With S4 and S12 plays an important role in translational accuracy.
  
    0.568
rps3
SSU ribosomal protein S3P (rpsC); Binds the lower part of the 30S subunit head. Belongs to the universal ribosomal protein uS3 family.
  
    0.562
MJ_0597
Conserved hypothetical protein; Similar to PID:747640 GB:AE000666 percent identity: 24.23; identified by sequence similarity; putative.
  
     0.556
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.