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
nthEndonuclease 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. (220 aa)    
Predicted Functional Partners:
exoA_2
Exodeoxyribonuclease III; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.993
dnaD
DNA replication protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.940
nfo
Deoxyribonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin.
  
 
 0.823
ypoC
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.781
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
  
 
 0.728
mutM
DNA-formamidopyrimidine 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.
   
  
 0.717
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.
  
 
 0.705
recJ
single-stranded-DNA-specific exonuclease RecJ; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.677
asnC
asparagine--tRNA ligase; Catalyzes a two-step reaction, first charging an asparagine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.657
preA
Dihydropyrimidine dehydrogenase subunit B; NADH-dependent; catalyzes the conversion of pyrimidines to 5,6-dihydro compounds in pyrimidine degradation; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.626
Your Current Organism:
Lysinibacillus sphaericus
NCBI taxonomy Id: 1421
Other names: ATCC 14577, B-23268, BCRC 12825, Bacillus sp. G10(2009), Bacillus sphaericus, CCM 2120, CCRC 12825, CCRC:12825, CCUG 7428, CIP 65.30, DSM 28, IAM 13420, JCM 2502, KCTC 3346, L. sphaericus, LMG 7134, LMG:7134, NBRC 15095, NCCB 75018, NCIMB 9370, NCTC 10338, NRRL B-23268, VKM B-509
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