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
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
rphRibonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. (241 aa)    
Predicted Functional Partners:
EHA59357.1
3'-5' exonuclease; KEGG: pmt:PMT1703 putative ribonuclease D; PFAM: 3'-5' exonuclease; SMART: 3'-5' exonuclease.
   
 0.966
EHA63332.1
Ribonuclease II; KEGG: pmf:P9303_14471 putative acetazolamide conferring resistance protein Zam; PFAM: Ribonuclease II/R; Ribonuclease B, N-terminal OB domain; Ribosomal protein S1, RNA-binding domain; SMART: Ribonuclease II/R; Cold shock protein; RNA-binding domain, S1; Belongs to the RNR ribonuclease family.
   
 0.952
EHA63372.1
Ribonuclease II; KEGG: pmf:P9303_14771 ribonuclease II; PFAM: Ribonuclease II/R; SMART: Ribonuclease II/R.
   
 0.952
EHA62283.1
Nucleoside-triphosphatase rdgB; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
 
 
  0.952
EHA64167.1
Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; TIGRFAM: Ham1-like protein; KEGG: pmf:P9303_08051 HAM1 family protein; PFAM: Ham1-like protein.
 
 
  0.949
dnaG
DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
    
 0.939
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
 
 0.917
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
   
 
 0.879
rpsD
Ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
  
  0.877
EHA64296.1
Ribonuclease P; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
   
 
 0.875
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
Server load: medium (44%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.