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.
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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
prfBBacterial peptide chain release factor 2 (bRF-2); Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. (365 aa)    
Predicted Functional Partners:
rplU
LSU ribosomal protein L21P; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
   
  0.975
rpsP
COGs: COG0228 Ribosomal protein S16; InterPro IPR000307; KEGG: aac:Aaci_1352 ribosomal protein S16; PFAM: ribosomal protein S16; SPTR: Ribosomal protein S16; TIGRFAM: ribosomal protein S16; PFAM: Ribosomal protein S16; TIGRFAM: ribosomal protein S16; Belongs to the bacterial ribosomal protein bS16 family.
 
 
 0.961
rplT
LSU ribosomal protein L20P; 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.
  
 0.958
rpsG
SSU ribosomal protein S7P; 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.
 
 
 0.951
rplQ
COGs: COG0203 Ribosomal protein L17; InterPro IPR000456; KEGG: tit:Thit_1943 ribosomal protein L17; PFAM: ribosomal protein L17; SPTR: Ribosomal protein L17; TIGRFAM: ribosomal protein L17; PFAM: Ribosomal protein L17; TIGRFAM: ribosomal protein L17.
  
  0.950
rpmA
COGs: COG0211 Ribosomal protein L27; InterPro IPR001684:IPR018261; KEGG: tpd:Teth39_1433 50S ribosomal protein L27; PFAM: ribosomal protein L27; SPTR: Ribosomal protein L27; TIGRFAM: ribosomal protein L27; PFAM: Ribosomal L27 protein; TIGRFAM: ribosomal protein L27; Belongs to the bacterial ribosomal protein bL27 family.
  
 
 0.949
rsfS
Iojap-like protein; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
 
 0.937
rpmF
COGs: COG0333 Ribosomal protein L32; InterPro IPR002677; KEGG: cce:Ccel_2134 ribosomal protein L32; PFAM: ribosomal L32p protein; SPTR: Ribosomal protein L32; TIGRFAM: ribosomal protein L32; PFAM: Ribosomal L32p protein family; TIGRFAM: ribosomal protein L32; Belongs to the bacterial ribosomal protein bL32 family.
  
 0.937
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.
  
 0.936
rplM
LSU ribosomal protein L13P; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
  
 
 0.934
Your Current Organism:
Thermosediminibacter oceani
NCBI taxonomy Id: 555079
Other names: T. oceani DSM 16646, Thermosediminibacter oceani DSM 16646, Thermosediminibacter oceani JW/IW-1228P, Thermosediminibacter oceani str. DSM 16646, Thermosediminibacter oceani strain DSM 16646
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