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
OCH20952.1tRNA threonylcarbamoyladenosine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. (269 aa)    
Predicted Functional Partners:
thiI
tRNA 4-thiouridine(8) synthase 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.
  
 
 0.783
OCH18695.1
Thiamine biosynthesis protein ThiS; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  0.750
thiG
Thiazole synthase; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
 
 
  0.732
mnmC
tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC; Catalyzes the last two steps in the biosynthesis of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34; In the C-terminal section; belongs to the DAO family.
 
  
  0.728
iscS
Cysteine desulfurase IscS; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
    
 0.721
OCH22202.1
Molybdopterin synthase sulfur carrier subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.716
OCH18696.1
Molybdopterin-synthase adenylyltransferase MoeB; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
0.680
OCH17631.1
Molybdopterin-synthase adenylyltransferase MoeB; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
0.675
OCH22898.1
Cysteine desulfurase-like protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.601
OCH20950.1
Cysteine sulfinate desulfinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.
    
 0.601
Your Current Organism:
Aliivibrio logei
NCBI taxonomy Id: 688
Other names: A. logei, ATCC 29985, CCUG 20283, CIP 104991, LMG 21012, LMG:21012, NCIMB 2252, Photobacterium logei, Vibrio logei, strain 584
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.