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HX89_12505 protein (Dermacoccus nishinomiyaensis) - STRING interaction network
"HX89_12505" - Uncharacterized protein in Dermacoccus nishinomiyaensis
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
HX89_12505Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (326 aa)    
Predicted Functional Partners:
HX89_12510
ATP-dependent DNA ligase; Derived by automated computational analysis using gene prediction method- Protein Homology (292 aa)
   
  0.999
HX89_06610
ATP-dependent DNA ligase; Derived by automated computational analysis using gene prediction method- Protein Homology (347 aa)
     
  0.979
ku
Non-homologous end joining protein Ku; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5’- and 3’- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD (264 aa)
 
   
  0.949
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (889 aa)
   
 
  0.821
HX89_00670
Beta sliding clamp; 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 replication as [...] (376 aa)
     
 
  0.675
HX89_05810
Vitamin B12-dependent ribonucleotide reductase; Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen (975 aa)
     
        0.659
HX89_03235
Exodeoxyribonuclease III; Derived by automated computational analysis using gene prediction method- Protein Homology (262 aa)
 
   
  0.651
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2’-deoxyuridine- 5’-monophosphate (dUMP) to 2’-deoxythymidine-5’-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis (264 aa)
     
   
  0.521
sbcD
Nuclease SbcCD subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity (397 aa)
     
 
  0.504
HX89_07320
5’-3’ exonuclease; Derived by automated computational analysis using gene prediction method- Protein Homology (308 aa)
   
 
  0.483
Your Current Organism:
Dermacoccus nishinomiyaensis
NCBI taxonomy Id: 1274
Other names: ATCC 29093, CCM 2140, CCUG 33028, CIP 81.71, D. nishinomiyaensis, DSM 20448, Dermacoccus nishinomiyaensis, Dermacoccus nishinomiyensis, Dermatococcus nishinomiyaensis, Dermatococcus nishinomiyensis, IEGM 393, IFO 15356, JCM 11613, LMG 14222, Micrococcus nishinomiyaensis, Micrococcus nishinomyaensis, NBRC 15356, NCTC 11039
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