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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
KXB74322.1KEGG: phe:Phep_1011 6.7e-84 DEAD/DEAH box helicase; K05591 ATP-independent RNA helicase DbpA; Psort location: Cytoplasmic, score: 9.97. (438 aa)    
Predicted Functional Partners:
nnrD
YjeF domain protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epim [...]
   
 0.956
KXB77642.1
30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.
   
 0.945
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.
  
 0.944
rpsE
Ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family.
   
 0.937
rpsK
30S ribosomal protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family.
   
 0.933
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
 
 
 0.889
KXB81933.1
KEGG: ddf:DEFDS_1775 1.3e-110 translation elongation factor G K02355; Psort location: Cytoplasmic, score: 9.97.
   
 0.876
fusA
Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]
   
 0.876
KXB77264.1
Putative translation elongation factor G; KEGG: bnm:BALAC2494_01437 4.4e-64 Protein-synthesizing GTPase; Psort location: Cytoplasmic, score: 9.97.
   
 0.876
KXB74321.1
Hypothetical protein; Psort location: Cytoplasmic, score: 8.96.
       0.849
Your Current Organism:
Prevotella amnii
NCBI taxonomy Id: 419005
Other names: CCUG 53648, DSM 23384, JCM 14753, P. amnii, Prevotella amnii Lawson et al. 2008 emend. Hahnke et al. 2016
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.