STRINGSTRING
RSAG_02201 protein (Ruminococcus sp. 5139BFAA) - STRING interaction network
"RSAG_02201" - Uncharacterized protein in Ruminococcus sp. 5139BFAA
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
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Gene Fusion
Cooccurence
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[Homology]
Score
RSAG_02201Uncharacterized protein (103 aa)    
Predicted Functional Partners:
RSAG_01331
Uncharacterized protein (1053 aa)
       
      0.860
RSAG_00685
Uncharacterized protein (831 aa)
       
      0.860
RSAG_02939
Uncharacterized protein (384 aa)
   
  0.713
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 (394 aa)
   
  0.713
dapL
LL-diaminopimelate aminotransferase ; Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate, a reaction that requires three enzymes in E.coli (404 aa)
 
 
    0.667
RSAG_01570
Thiazole biosynthesis adenylyltransferase ThiF (278 aa)
   
 
  0.655
RSAG_02352
Cysteine synthase (309 aa)
   
 
  0.650
pyrK
Dihydroorotate oxidase B, electron transfer subunit ; Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+) (262 aa)
     
    0.646
RSAG_00640
Uncharacterized protein (295 aa)
     
    0.646
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 (259 aa)
       
  0.633
Your Current Organism:
Ruminococcus sp. 5139BFAA
NCBI taxonomy Id: 457412
Other names: R. sp. 5_1_39BFAA, Ruminococcus 5_1_39BFAA, Ruminococcus sp. 5139BFAA, Ruminococcus sp. 5_1_39BFAA
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