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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ruvCCrossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. (182 aa)    
Predicted Functional Partners:
ruvA
ATP-dependent DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
 
 0.999
ruvB
ATP-dependent DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
 
 0.994
OOQ53664.1
Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.829
OOQ48749.1
Mg chelatase-like protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.744
OOQ53660.1
Preprotein translocase, YajC subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.743
secF
Preprotein translocase subunit SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
 
     0.702
pdxT
Glutamine amidotransferase; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
       0.699
pdxS
Pyridoxal biosynthesis lyase PdxS; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family.
       0.699
secD
Preprotein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
 
     0.687
recX
Recombinase RecX; Modulates RecA activity; Belongs to the RecX family.
  
  
 0.685
Your Current Organism:
Streptomyces antibioticus
NCBI taxonomy Id: 1890
Other names: ATCC 23879, ATCC 8663, Actinomyces antibioticus, BCRC 12164, CBS 478.48, CBS 659.68, CCM 3159, CCRC 12164, CCRC:12164, CECT 3225, DSM 40234, IFO 12838, IMET 40227, ISP 5234, JCM 4620, KCTC 9688, LMG 5966, LMG:5966, NBRC 12838, NCIMB 8504, NRRL B-2770, NRRL-ISP 5234, S. antibioticus, Streptomyces antibioticus subsp. antibioticus, VKM Ac-964
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