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nfo protein (Nitrosopumilus maritimus) - STRING interaction network
"nfo" - Probable endonuclease 4 in Nitrosopumilus maritimus
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
nfoProbable endonuclease 4; 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 (279 aa)    
Predicted Functional Partners:
Nmar_0063
KEGG- tpe-Tpen_0288 glycyl-tRNA synthetase; TIGRFAM- glycyl-tRNA synthetase; PFAM- tRNA synthetase class II (G H P and S); Anticodon-binding domain protein (485 aa)
              0.779
priS
DNA primase small subunit PriS; Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthe [...] (373 aa)
   
        0.710
priL
DNA primase large subunit PriL; Regulatory subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Stabilizes and modulates the activity of the small subunit, increasing the rate of DNA synthesis, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair (341 aa)
   
        0.660
lig
DNA ligase; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair (588 aa)
     
   
  0.600
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 (218 aa)
   
 
  0.600
dbh
DNA 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 (364 aa)
 
 
  0.597
fen
Flap endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. Binds the unpaired 3’-DNA end and kinks the DNA to facilitate 5’ cleavage specificity. Cleaves one nucleotide into the double- stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. A [...] (340 aa)
   
 
  0.537
Nmar_0067
KEGG- sun-SUN_1015 hypothetical protein (953 aa)
   
        0.527
Nmar_0924
PFAM- CDP-alcohol phosphatidyltransferase; KEGG- pfu-PF0462 CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family (190 aa)
   
        0.521
Nmar_0068
PFAM- glutamine amidotransferase class-I; KEGG- pto-PTO1342 GMP synthase subunit A (180 aa)
              0.518
Your Current Organism:
Nitrosopumilus maritimus
NCBI taxonomy Id: 436308
Other names: N. maritimus SCM1, Nitrosopumilus maritimus, Nitrosopumilus maritimus SCM1, Nitrosopumilus maritimus str. SCM1, Nitrosopumilus maritimus strain SCM1, Seattle Aquarium strain SCM1
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