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DVU_1802 protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"DVU_1802" - Uncharacterized protein in Desulfovibrio vulgaris Hildenborough
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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
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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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DVU_1802Uncharacterized protein; Identified by similarity to OMNI-NTL01RS2082 (286 aa)    
Predicted Functional Partners:
DVU_0038
Acyltransferase domain protein; Identified by match to protein family HMM PF01553 (616 aa)
   
 
  0.551
serS
Serine--tRNA ligase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (424 aa)
     
      0.521
DVU_1688
1-acyl-sn-glycerol-3-phosphate acyltransferase, putative; Identified by match to protein family HMM PF01553 (269 aa)
   
 
  0.518
DVU_1801
Uncharacterized protein; Identified by Glimmer2; putative (395 aa)
              0.517
ileS
Isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as ’pretransfer’ editing and involves the hydrolysis of activated Val-AMP. The other activity is designated ’posttransfer’ editing and involves deacylation of mischarged Val-tRNA(Ile) (938 aa)
   
      0.515
DVU_1834
Pyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second (1225 aa)
       
      0.504
rplC
50S ribosomal protein L3; 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 (209 aa)
     
      0.469
DVU_0742
Uncharacterized protein; Identified by Glimmer2; putative (278 aa)
   
          0.430
ispD
Bifunctional enzyme IspD/IspF; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl- D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2- phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4- cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF); In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily (395 aa)
   
        0.415
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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