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DVU_0298 protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"DVU_0298" - 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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Score
DVU_0298Uncharacterized protein; Identified by Glimmer2; putative (261 aa)    
Predicted Functional Partners:
DVU_1382
HesB family selenoprotein; Selenoprotein; identified by match to protein family HMM PF01521; Belongs to the HesB/IscA family (107 aa)
 
 
  0.824
DVU_3276
Identified by similarity to SP-P08813; match to protein family HMM PF00037 (62 aa)
 
          0.778
dsvD
Protein DsvD; May play an essential role in dissimilatory sulfite reduction (78 aa)
   
          0.774
DVU_3274
Uncharacterized protein; Identified by Glimmer2; putative (222 aa)
 
     
  0.773
DVU_0359
annotation not available (108 aa)
 
 
  0.771
DVU_3273
Uncharacterized protein; Identified by similarity to GP-944973 (130 aa)
 
          0.754
DVU_1460
Uncharacterized protein; Identified by Glimmer2; putative (111 aa)
   
          0.745
DVU_0849
Heterodisulfide reductase, iron-sulfur-binding subunit, putative; Identified by match to protein family HMM PF00037; match to protein family HMM PF02662 (758 aa)
 
     
  0.742
dsvA
Sulfite reductase, dissimilatory-type subunit alpha; Part of the complex that catalyzes the reduction of sulfite to sulfide. The alpha and beta subunits may have arisen by gene duplication. They both bind 2 iron-sulfur clusters, but the alpha subunit seems to be catalytically inactive, due to substitutions along the putative substrate access channel, and because it binds sirohydrochlorin (the dematallated form of siroheme) instead of siroheme (437 aa)
   
          0.742
dvsB
Sulfite reductase, dissimilatory-type subunit beta; Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration, a process catalyzed by the sulfate-reducing bacteria (381 aa)
   
          0.735
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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