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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Arch_0569COGs: COG1837 RNA-binding protein (contains KH domain); InterPro IPR004088:IPR009019; KEGG: xce:Xcel_1168 RNA-binding protein (KH domain); SPTR: D0WR64 KH domain protein; PFAM: KH domain; Belongs to the UPF0109 family. (78 aa)    
Predicted Functional Partners:
rpsP
COGs: COG0228 Ribosomal protein S16; InterPro IPR000307:IPR020592; KEGG: bad:BAD_0209 30S ribosomal protein S16; PFAM: ribosomal protein S16; SPTR: A0ZZV7 30S ribosomal protein S16; TIGRFAM: ribosomal protein S16; PFAM: Ribosomal protein S16; TIGRFAM: ribosomal protein S16; Belongs to the bacterial ribosomal protein bS16 family.
  
  
 0.986
Arch_1817
COGs: COG1847 RNA-binding protein; InterPro IPR001374; KEGG: bcv:Bcav_4221 single-stranded nucleic acid binding R3H domain protein; PFAM: single-stranded nucleic acid binding R3H domain protein; SMART: single-stranded nucleic acid binding R3H domain protein; SPTR: D0WL15 R3H domain-containing protein; PFAM: R3H domain.
  
 
 0.945
rplS
Ribosomal protein L19; 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.
  
    0.890
rimM
16S rRNA processing protein RimM; An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes; Belongs to the RimM family.
  
  
 0.881
rpsI
COGs: COG0103 Ribosomal protein S9; InterPro IPR000754:IPR014721:IPR020568:IPR020574; KEGG: xce:Xcel_0662 ribosomal protein S9; PFAM: ribosomal protein S9; SPTR: A7B9L2 30S ribosomal protein S9; PFAM: Ribosomal protein S9/S16; Belongs to the universal ribosomal protein uS9 family.
  
    0.773
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.
  
    0.763
rpsO
Ribosomal protein S15; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
  
    0.762
rplT
Ribosomal protein L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
  
    0.759
trmD
tRNA (guanine-N1)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family.
 
    0.756
rpsT
Ribosomal protein S20; Binds directly to 16S ribosomal RNA.
   
    0.700
Your Current Organism:
Arcanobacterium haemolyticum
NCBI taxonomy Id: 644284
Other names: A. haemolyticum DSM 20595, Arcanobacterium haemolyticum ATCC 9345, Arcanobacterium haemolyticum CIP 103370, Arcanobacterium haemolyticum DSM 20595, Arcanobacterium haemolyticum str. DSM 20595, Arcanobacterium haemolyticum strain DSM 20595
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.