STRINGSTRING
dinP protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"dinP" - DNA polymerase IV 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
dinPDNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3’-5’ exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (386 aa)    
Predicted Functional Partners:
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)
   
 
  0.835
umuD
UmuD protein; Identified by similarity to SP-P04153; match to protein family HMM PF00717; Belongs to the peptidase S24 family (164 aa)
 
  0.824
recA
Protein RecA; Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (357 aa)
   
 
  0.799
nth
Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N- glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3’ to the AP site by a beta-elimination, leaving a 3’-terminal unsaturated sugar and a product with a terminal 5’-phosphate (285 aa)
   
 
  0.798
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)
   
   
  0.777
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)
     
 
  0.677
DVU_0256
ATP-dependent RNA helicase, DEAD/DEAH box family; Identified by match to protein family HMM PF00270; match to protein family HMM PF00271 (1121 aa)
   
 
  0.637
groEL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (547 aa)
       
 
  0.572
rpmB
50S ribosomal protein L28; Identified by match to protein family HMM PF00830; match to protein family HMM TIGR00009; Belongs to the bacterial ribosomal protein bL28 family (69 aa)
           
  0.552
nusA
Transcription termination/antitermination protein NusA; Participates in both transcription termination and antitermination (428 aa)
       
 
  0.547
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 (24%) [HD]