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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Apre_0909TIGRFAM: single-stranded-DNA-specific exonuclease RecJ; PFAM: phosphoesterase RecJ domain protein; phosphoesterase DHHA1; KEGG: single-stranded-DNA-specific exonuclease RecJ; K07462 single-stranded-DNA-specific exonuclease. (576 aa)    
Predicted Functional Partners:
plsY
Protein of unknown function DUF205; Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
 
    0.843
Apre_0910
(p)ppGpp synthetase I, SpoT/RelA; 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.
  
    0.815
Apre_0912
PFAM: beta-lactamase domain protein; KEGG: bcb:BCB4264_A4375 metallo-beta-lactamase family protein.
  
    0.810
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.
       0.806
der
Small GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
  
  
 0.804
aspS
aspartyl-tRNA synthetase; 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.
       0.798
gpsA
PFAM: NAD-dependent glycerol-3-phosphate dehydrogenase domain protein; KEGG: bsu:BSU22830 NAD(P)H-dependent glycerol-3- phosphate dehydrogenase; Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
  
    0.796
Apre_0914
PFAM: Positive regulator of sigma(E) RseC/MucC; KEGG: hiq:CGSHiGG_07760 positive regulator of sigma E.
       0.794
glyA
Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
       0.788
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.
   
 
 0.749
Your Current Organism:
Anaerococcus prevotii DSM 20548
NCBI taxonomy Id: 525919
Other names: A. prevotii DSM 20548, Anaerococcus prevotii ATCC 9321, Anaerococcus prevotii CCUG 41932, Anaerococcus prevotii str. DSM 20548, Anaerococcus prevotii strain DSM 20548
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.