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
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tusASulfur transfer protein SirA; Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthesis of molybdopterin. (83 aa)    
Predicted Functional Partners:
iscS
Cysteine desulfurase; 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.
   
 0.993
tusD
Sulfur transfer complex subunit TusD; Part of a sulfur-relay system required for 2-thiolation of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE.
 
 
 0.989
ychN
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.789
moaD
Molybdopterin synthase small subunit; Catalyzes the conversion of molybdopterin precursor Z into molybdopterin; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 
 0.786
moaC
Molybdenum cofactor biosynthesis protein MoaC; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP); Belongs to the MoaC family.
     
 0.747
moaE
Molybdopterin guanine dinucleotide biosynthesis protein MoaE; Catalyzes the conversion of molybdopterin precursor Z into molybdopterin; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.713
AKA38202.1
Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.574
AKA38203.1
YeeE/YedE; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.574
thiI
tRNA s(4)U8 sulfurtransferase; 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.
  
 
 0.566
moeA
Molybdopterin biosynthesis protein MoeA; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family.
     
 0.534
Your Current Organism:
Yersinia ruckeri
NCBI taxonomy Id: 29486
Other names: ATCC 29473, CCM 6093, CCUG 14190, CDC 2396-61, CIP 82.80, DSM 18506, JCM 15110, JCM 2429, NCIB 2194, NCIMB 2194, NCTC 12986, Y. ruckeri
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