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
AFZ06238.1UPF0082 protein yeeN; PFAM: Domain of unknown function DUF28; TIGRFAM: DNA-binding regulatory protein, YebC/PmpR family; COGs: COG0217 conserved hypothetical protein; HAMAP: Protein of unknown function DUF28; InterPro IPR002876; KEGG: npu:Npun_R5651 hypothetical protein; PFAM: Protein of unknown function DUF28; SPTR: UPF0082 protein OSCI_3500001; TIGRFAM: Protein of unknown function DUF28. (255 aa)    
Predicted Functional Partners:
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
  
 0.807
tyrS
tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.
   0.641
tig
Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily.
 
  
 0.588
rplS
LSU ribosomal protein L19P; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
  
   0.552
rpmF
PFAM: Ribosomal L32p protein family; TIGRFAM: ribosomal protein L32; HAMAP: Ribosomal protein L32p; InterPro IPR002677; KEGG: cyj:Cyan7822_1212 50S ribosomal protein L32; PFAM: Ribosomal protein L32p; SPTR: 50S ribosomal protein L32; TIGRFAM: Ribosomal protein L32p; Belongs to the bacterial ribosomal protein bL32 family.
   
  
 0.517
AFZ06239.1
PFAM: Restriction endonuclease; COGs: COG1787 endonuclease distantly related to Holliday junction resolvase and Mrr-like restriction enzyme; InterPro IPR007560; KEGG: npu:Npun_F0096 hypothetical protein; PFAM: Restriction endonuclease, type IV-like, Mrr; SPTR: Putative uncharacterized protein.
       0.496
AFZ06240.1
Hypothetical protein.
       0.495
tsf
Elongation factor Ts; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family.
   
  
 0.494
AFZ06237.1
PFAM: Phosphoglycerate mutase family; COGs: COG0406 Fructose-2 6-bisphosphatase; InterPro IPR013078; KEGG: ter:Tery_2127 phosphoglycerate mutase; PFAM: Histidine phosphatase superfamily, clade-1; SMART: Histidine phosphatase superfamily, clade-1; SPTR: Putative phosphoglycerate mutase.
       0.479
ruvC
Holliday junction endonuclease 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.
 
  
 0.472
Your Current Organism:
Oscillatoria nigroviridis
NCBI taxonomy Id: 179408
Other names: O. nigro-viridis PCC 7112, Oscillatoria nigro-viridis PCC 7112, Oscillatoria sp. PCC 7112
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.