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mutT protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"mutT" - Mutator mutT 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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[Homology]
Score
mutTMutator mutT protein; Identified by similarity to SP-P08337; match to protein family HMM PF00293; Belongs to the Nudix hydrolase family (129 aa)    
Predicted Functional Partners:
DVU_3052
ABC transporter, ATP-binding protein; Identified by similarity to SP-P45535; match to protein family HMM PF00005 (659 aa)
 
      0.919
mutM
Formamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3’- and 5’-phosphates (365 aa)
         
  0.857
ung
Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine (245 aa)
   
   
  0.798
DVU_2843
Very short patch repair endonuclease; May nick specific sequences that contain T-G mispairs resulting from m5C-deamination (136 aa)
       
  0.778
nnrD
Multifunctional fusion protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Belongs to the NnrD/CARKD family (574 aa)
   
 
  0.764
coaD
Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4’- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate; Belongs to the bacterial CoaD family (186 aa)
            0.743
rpsG
30S ribosomal protein S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA (156 aa)
   
      0.741
polA
DNA polymerase I; Identified by similarity to SP-P00582; match to protein family HMM PF00476; match to protein family HMM PF01367; match to protein family HMM PF02739; match to protein family HMM TIGR00593 (1015 aa)
   
   
  0.721
DVU_1653
Identified by similarity to SP-P42977; match to protein family HMM PF00571; match to protein family HMM PF01368; match to protein family HMM PF01743; match to protein family HMM PF02272 (904 aa)
   
   
  0.712
dnaN
DNA polymerase III, beta subunit; Identified by match to protein family HMM PF00712; match to protein family HMM PF02768; match to protein family HMM TIGR00663 (384 aa)
   
     
  0.691
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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