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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Co-occurrence
Co-expression
Experiments
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[Homology]
Score
recJKEGG: cbe:Cbei_4321 1.8e-138 single-stranded-DNA-specific exonuclease RecJ; K07462 single-stranded-DNA-specific exonuclease; Psort location: Cytoplasmic, score: 7.50. (596 aa)    
Predicted Functional Partners:
murE
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase; KEGG: faa:HMPREF0389_00596 1.8e-122 UDP-N-acetylmuramyl tripeptide synthetase; K01928 UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase; Psort location: Cytoplasmic, score: 9.97.
  
  
 0.842
relA
Putative GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
  
    0.828
dtd
D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.
       0.820
KXA30457.1
KEGG: sis:LS215_2402 9.0e-41 beta-lactamase domain-containing protein; Psort location: Cytoplasmic, score: 7.50.
  
    0.812
hemZ_1
Coproporphyrinogen dehydrogenase HemZ; KEGG: cce:Ccel_1948 2.3e-67 coproporphyrinogen III oxidase; K02495 oxygen-independent coproporphyrinogen III oxidase; Psort location: Cytoplasmic, score: 9.97.
  
    0.812
priA
Primosomal protein; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily.
 
     0.651
murB_3
UDP-N-acetylmuramate dehydrogenase; Cell wall formation.
 
  
 0.597
ydeM_3
six-Cys-in-45 modification radical SAM protein; KEGG: mcj:MCON_2732 6.5e-15 anaerobic sulfatase-maturating protein K06871; Psort location: Cytoplasmic, score: 7.50.
       0.587
aspS
aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
       0.570
ruvC
Crossover 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.
   
 
 0.553
Your Current Organism:
Peptoniphilus harei
NCBI taxonomy Id: 54005
Other names: ATCC BAA-601, CCUG 38491, CIP 105323, DSM 10020, NCTC 13076, P. harei, Peptostreptococcus harei, Schleiferella harei
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