STRINGSTRING
DVU_1968 protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"DVU_1968" - annotation not available in Desulfovibrio vulgaris Hildenborough
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
DVU_1968annotation not available (413 aa)    
Predicted Functional Partners:
cysK
Cysteine synthase; Identified by match to protein family HMM PF00291; match to protein family HMM TIGR01136; match to protein family HMM TIGR01139; Belongs to the cysteine synthase/cystathionine beta- synthase family (308 aa)
       
  0.907
DVU_0173
Thiosulfate reductase, putative; Identified by similarity to SP-P37600; match to protein family HMM PF00384; match to protein family HMM PF01568; match to protein family HMM PF04879 (733 aa)
         
  0.904
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)
       
    0.901
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)
       
    0.901
DVU_1969
Uncharacterized protein; Identified by Glimmer2; putative (231 aa)
              0.863
DVU_1970
Response regulator; Identified by match to protein family HMM PF00072 (135 aa)
              0.813
DVU_1967
Transcriptional regulator, rrf2 protein, putative; Identified by similarity to SP-P33395; match to protein family HMM PF02082; match to protein family HMM TIGR00738 (173 aa)
              0.806
DVU_1368
Rhodanese-like domain protein; Identified by match to protein family HMM PF00581 (540 aa)
 
 
  0.754
DVU_0253
Oxidoreductase, FAD/iron-sulfur cluster-binding domain protein; Identified by match to protein family HMM PF00037; match to protein family HMM PF01565; match to protein family HMM PF02913 (941 aa)
 
   
  0.715
DVU_0283
AhpF family protein/thioredoxin reductase; Identified by similarity to SP-P80880; match to protein family HMM PF00070; match to protein family HMM TIGR01292; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family (661 aa)
   
 
  0.669
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
Server load: low (18%) [HD]