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.
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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[Homology]
Score
rnrRibonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. (695 aa)    
Predicted Functional Partners:
rph
Ribonuclease 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.
   
 0.946
ACZ07644.1
Metal dependent phosphohydrolase; KEGG: similar to Dauer Up-Regulated family member (dur-1); TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase HD sub domain; SMART: metal-dependent phosphohydrolase HD region.
 
    0.857
ACZ07642.1
KEGG: pca:Pcar_1511 N-acetylmuramoyl-L-alanine amidase; PFAM: cell wall hydrolase/autolysin; SMART: cell wall hydrolase/autolysin.
 
     0.815
smpB
SsrA-binding protein; Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to [...]
     
 0.805
ACZ09056.1
TIGRFAM: metal dependent phophohydrolase; PFAM: Polynucleotide adenylyltransferase region; metal-dependent phosphohydrolase HD sub domain; NUDIX hydrolase; KEGG: scl:sce1090 hypothetical protein; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
  
 0.790
ACZ07643.1
Hypothetical protein.
       0.781
rpsR
Ribosomal protein S18; Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit; Belongs to the bacterial ribosomal protein bS18 family.
  
 
 0.760
rpsQ
Ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
  
 
 0.746
rpsG
Ribosomal protein S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
   
 
 0.746
rpsO
Ribosomal protein S15; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
  
 
 0.739
Your Current Organism:
Sebaldella termitidis
NCBI taxonomy Id: 526218
Other names: S. termitidis ATCC 33386, Sebaldella termitidis ATCC 33386, Sebaldella termitidis NCTC 11300, Sebaldella termitidis str. ATCC 33386, Sebaldella termitidis strain ATCC 33386
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.