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
Srot_0441HhH-GPD family protein; KEGG: fal:FRAAL6530 A/G-specific adenine glycosylase; PFAM: HhH-GPD family protein; SMART: HhH-GPD family protein. (315 aa)    
Predicted Functional Partners:
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.
  
  
 0.830
Srot_1356
KEGG: rop:ROP_18940 putative exodeoxyribonuclease III; TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; PFAM: Endonuclease/exonuclease/phosphatase.
    
 0.786
Srot_2781
TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; KEGG: rop:ROP_62990 exodeoxyribonuclease; PFAM: Endonuclease/exonuclease/phosphatase.
    
 0.786
Srot_0440
PFAM: TspO/MBR family protein; KEGG: mva:Mvan_0268 TspO and MBR like proteins.
       0.779
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.
 
  
0.708
Srot_0442
KEGG: gbr:Gbro_0965 hypothetical protein.
       0.661
uvrB
Excinuclease ABC, B subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...]
     
 0.621
rlmN
Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family.
  
   
 0.619
Srot_1494
PFAM: UvrD/REP helicase; KEGG: rer:RER_44320 ATP-dependent DNA helicase UvrD1.
      
 0.614
recO
DNA repair protein RecO; Involved in DNA repair and RecF pathway recombination.
     
 0.600
Your Current Organism:
Segniliparus rotundus
NCBI taxonomy Id: 640132
Other names: S. rotundus DSM 44985, Segniliparus rotundus ATCC BAA-972, Segniliparus rotundus CIP 108378, Segniliparus rotundus DSM 44985, Segniliparus rotundus JCM 13578, Segniliparus rotundus str. DSM 44985, Segniliparus rotundus strain DSM 44985
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.