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_0912PFAM: beta-lactamase domain protein; KEGG: bcb:BCB4264_A4375 metallo-beta-lactamase family protein. (200 aa)    
Predicted Functional Partners:
Apre_1676
PFAM: pyridine nucleotide-disulphide oxidoreductase dimerisation region; FAD-dependent pyridine nucleotide- disulphide oxidoreductase; Rhodanese domain protein; SMART: Rhodanese domain protein; KEGG: ftn:FTN_1391 uncharacterized NAD(FAD)- dependent dehydrogenase.
  
 0.941
Apre_0364
PFAM: Glyoxalase/bleomycin resistance protein/dioxygenase; KEGG: bph:Bphy_4478 glyoxalase/bleomycin resistance protein/dioxygenase.
 
  
 0.940
Apre_1605
KEGG: gsu:GSU3295 hypothetical protein.
     
  0.900
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.
 
     0.828
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.
  
    0.811
Apre_0909
TIGRFAM: 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.
  
    0.810
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.
     
 0.807
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.
  
    0.803
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.
  
  
 0.795
Apre_0914
PFAM: Positive regulator of sigma(E) RseC/MucC; KEGG: hiq:CGSHiGG_07760 positive regulator of sigma E.
       0.794
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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