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
Pisl_2010Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. (211 aa)    
Predicted Functional Partners:
rps17
SSU ribosomal protein S17P; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
  
 
 0.990
rpl13
LSU ribosomal protein L13P; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
  
 
 0.977
rpl15
LSU ribosomal protein L15P; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
 
 0.976
rpl3
LSU ribosomal protein L3P; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family.
  
 
 0.976
thiI
Thiamine biosynthesis/tRNA modification protein ThiI; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
  
 
 0.963
rpl11
LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors; Belongs to the universal ribosomal protein uL11 family.
  
   0.947
rpl14
LSU ribosomal protein L14P; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family.
  
 
 0.925
rpl2
LSU ribosomal protein L2P; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
  
   0.912
sucD
succinyl-CoA synthetase (ADP-forming) alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
  
 
 0.907
Pisl_1583
Aconitase; TIGRFAM: aconitate hydratase 1; PFAM: aconitate hydratase domain protein; KEGG: pai:PAE1499 aconitate hydratase.
   
 
 0.907
Your Current Organism:
Pyrobaculum islandicum
NCBI taxonomy Id: 384616
Other names: P. islandicum DSM 4184, Pyrobaculum islandicum DSM 4184, Pyrobaculum islandicum str. DSM 4184, Pyrobaculum islandicum strain DSM 4184
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.