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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
SKC75870.1Putative hydrolase of the HAD superfamily. (210 aa)    
Predicted Functional Partners:
recC
DNA helicase/exodeoxyribonuclease V, gamma subunit; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recomb [...]
       0.773
recB
Exodeoxyribonuclease V beta subunit; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and rep [...]
       0.773
recD
DNA helicase/exodeoxyribonuclease V, alpha subunit; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recomb [...]
       0.773
SKC68984.1
Polyphosphate glucokinase.
   
 
  0.766
glgC
Glucose-1-phosphate adenylyltransferase; Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
   
 
  0.704
SKC75875.1
Luciferase family oxidoreductase, group 1.
       0.671
SKC72957.1
Glucokinase.
   
 
  0.634
SKC80554.1
Glucokinase.
   
 
  0.634
SKC70797.1
Diaminohydroxyphosphoribosylaminopyrimidine deaminase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
    
 0.630
SKC48587.1
Polyphosphate glucokinase.
   
 
  0.622
Your Current Organism:
Krasilnikoviella flava
NCBI taxonomy Id: 526729
Other names: CC 0387, CC0387, CCTCC AA208024, DSM 21481, JCM 16551, K. flava, Krasilnikoviella flava (Jiang et al. 2009) Nishijima et al. 2017, Promicromonospora flava, Promicromonospora flava Jiang et al. 2009, Promicromonospora sp. CC 0387
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