STRINGSTRING
STRING protein interaction network
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:
a 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 to 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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
unguracil-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. (225 aa)    
Predicted Functional Partners:
thiL
Thiamine-phosphate kinase; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1; Belongs to the thiamine-monophosphate kinase family.
  
    0.820
Mvan_0002
DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]
  
 
 0.743
Mvan_0730
TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase; KEGG: mmc:Mmcs_0567 exodeoxyribonuclease III (xth).
  
 0.718
Mvan_1556
KEGG: mmc:Mmcs_1211 exodeoxyribonuclease III (xth); TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase.
  
 0.718
Mvan_4057
Membrane alanyl aminopeptidase, Metallo peptidase, MEROPS family M01; TIGRFAM: aminopeptidase N; PFAM: peptidase M1, membrane alanine aminopeptidase; KEGG: mmc:Mmcs_3605 peptidase M1, aminopeptidase N actinomycete-type.
 
   
 0.631
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.
  
 
 0.616
Mvan_2149
KEGG: mmc:Mmcs_1930 putative conserved secreted protein.
       0.613
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
  
  
 0.601
Mvan_2150
PFAM: regulatory protein, AsnC/Lrp family; KEGG: mmc:Mmcs_1931 putative transcriptional regulator, AsnC family.
       0.531
trpD
Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA).
      0.529
Your Current Organism:
Mycolicibacterium vanbaalenii
NCBI taxonomy Id: 350058
Other names: M. vanbaalenii PYR-1, Mycobacterium sp. PYR-1, Mycobacterium vanbaalenii DSM 7251, Mycobacterium vanbaalenii PYR-1, Mycolicibacterium vanbaalenii DSM 7251, Mycolicibacterium vanbaalenii PYR-1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.