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
AMF98484.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (132 aa)    
Predicted Functional Partners:
rnpA
Ribonuclease P protein component; 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.
  
  
 0.892
rpmH
50S ribosomal protein L34; In Escherichia coli transcription of this gene is enhanced by polyamines; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL34 family.
  
 
 0.887
rplB
50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
   
 
 0.870
secD
Preprotein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
   
 
 0.860
secD-2
Preprotein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
   
 
 0.860
secY
Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. Belongs to th [...]
   
 
 0.856
rpsS
30S ribosomal protein S19; Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
   
   0.847
rpsI
30S ribosomal protein S9; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uS9 family.
   
   0.845
rplQ
50S ribosomal protein L17; Is a component of the macrolide binding site in the peptidyl transferase center; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.844
rplD
50S ribosomal protein L4; Forms part of the polypeptide exit tunnel.
   
   0.840
Your Current Organism:
Vibrio harveyi
NCBI taxonomy Id: 669
Other names: ATCC 14126, Achromobacter harveyi, Beneckea harveyi, Beneckea neptuna, CAIM 513, CCUG 28584, CECT 525, CIP 103192, DSM 19623, IFO 15634, LMG 4044, LMG:4044, Lucibacterium harveyi, NBRC 15634, NCCB 80033, NCTC 12970, Photobacterium harveyi, Pseudomonas harveyi, V. harveyi, Vibrio carchariae, Vibrio sp. HENC-01, Vibrio sp. HENC-02, Vibrio sp. PG 001, Vibrio sp. PG 002, Vibrio sp. PG 006, Vibrio sp. PG 007, Vibrio trachuri
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