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 Ung; 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. (227 aa)    
Predicted Functional Partners:
MMAR_1738
Oxidoreductase; Thought to be involved in fatty acid degradation. FadB and FadA are the alpha and beta subunits of the multifunctional enzyme complex of the fatty acid degradation cycle.
  
    0.879
MMAR_1736
Conserved hypothetical protein.
       0.874
xthA
Exodeoxyribonuclease III protein XthA; Involved in base excision repair. apurinic- apyrimidinic endonuclease. supposed to remove the damaged DNA at cytosines and guanines by cleaving at the 3' side of the ap site by a beta-elimination reaction. possibly exhibites 3'-5'-exonuclease, 3'-phosphomonoesterase, 3'- repair diesterase and ribonuclease H activities [catalytic activity: degradation of double-stranded DNA. it acts progressively in a 3'- to 5'-direction, releasing 5'- phosphomononucleotides].
  
 0.869
thiL
Thiamine-monophosphate kinase ThiL; 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.
  
    0.846
MMAR_1734
Conserved hypothetical membrane protein.
       0.735
MMAR_1739
Nitroreductase; Function unknown; probably involved in cellular metabolism.
     
 0.685
dnaN
DNA polymerase III (beta chain) DnaN; 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 initiatio [...]
  
 
 0.633
lppK
Conserved lipoprotein, LppK.
  
 
 0.633
dnaN_1
Probably involved in phage genome replication. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. this DNA polymerase also exhibits 3' to 5' exonuclease activity. the beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA [catalytic activity: N deoxynucleoside triphosphate = N diphosphate + {DNA}n].
  
 
 0.633
nth
Endonuclease III Nth; 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.
  
 
 0.614
Your Current Organism:
Mycobacterium marinum
NCBI taxonomy Id: 216594
Other names: M. marinum M, Mycobacterium marinum M, Mycobacterium marinum str. M, Mycobacterium marinum strain M
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