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dusB protein (Sideroxydans lithotrophicus) - STRING interaction network
"dusB" - TIM-barrel protein, nifR3 family in Sideroxydans lithotrophicus
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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
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Score
dusBTIM-barrel protein, nifR3 family; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines (335 aa)    
Predicted Functional Partners:
Slit_0292
Fis family transcriptional regulator (84 aa)
   
        0.771
Slit_1032
Sulfite reductase (ferredoxin) (676 aa)
       
      0.694
purH
Phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase (520 aa)
   
        0.651
Slit_0290
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family (384 aa)
              0.644
proS
prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction- proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as ’pretransfer’ editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated ’posttransfer’ editing and involves dea [...] (566 aa)
     
    0.595
Slit_0289
Disulfide bond isomerase, DsbC/G-like protein (236 aa)
              0.592
gltX
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction- glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (468 aa)
   
    0.585
gluQ
glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5- dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon (304 aa)
   
    0.580
glnS
glutaminyl-tRNA synthetase (559 aa)
   
    0.580
purD
Phosphoribosylamine/glycine ligase (423 aa)
   
        0.578
Your Current Organism:
Sideroxydans lithotrophicus
NCBI taxonomy Id: 580332
Other names: S. lithotrophicus, S. lithotrophicus ES-1, Siderooxidans, Siderooxidans lithoautotrophicus, Sideroxydans, Sideroxydans lithotrophicus, Sideroxydans lithotrophicus ES-1, Sideroxydans lithotrophicus str. ES-1, Sideroxydans lithotrophicus strain ES-1, iron-oxidizing lithotroph ES-1
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