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DVU_3276 protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"DVU_3276" - Identified by similarity to SP:P08813 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
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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[Homology]
Score
DVU_3276Identified by similarity to SP-P08813; match to protein family HMM PF00037 (62 aa)    
Predicted Functional Partners:
DVU_3273
Uncharacterized protein; Identified by similarity to GP-944973 (130 aa)
 
          0.813
DVU_3274
Uncharacterized protein; Identified by Glimmer2; putative (222 aa)
 
          0.806
DVU_0298
Uncharacterized protein; Identified by Glimmer2; putative (261 aa)
 
          0.778
DVU_0305
Ferredoxin II; Identified by similarity to SP-P10624; match to protein family HMM PF00037 (64 aa)
           
  0.736
DVU_3272
TPR domain protein; Identified by match to protein family HMM PF00515 (207 aa)
 
          0.736
dsvD
Protein DsvD; May play an essential role in dissimilatory sulfite reduction (78 aa)
   
          0.722
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)
   
          0.719
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)
 
     
  0.701
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)
   
     
  0.694
DVU_0848
Heterodisulfide reductase, putative; Identified by similarity to GP-1890204 (412 aa)
   
          0.683
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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