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
SIQ36584.1Superfamily II DNA and RNA helicase; Belongs to the DEAD box helicase family. (383 aa)    
Predicted Functional Partners:
fusA
Translation elongation factor 2 (EF-2/EF-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. [...]
   
 0.956
nnrD
NAD(P)H-hydrate epimerase; 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 bot [...]
  
 0.955
rplC
LSU ribosomal protein L3P; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family.
   
 
 0.889
rpsD
SSU ribosomal protein S4P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
  
 0.887
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.
   
 0.882
SIR40636.1
SSU ribosomal protein S1P.
   
 0.877
rpsE
SSU ribosomal protein S5P; 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.
   
 0.874
SIR83132.1
Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
 
 0.870
SIQ39664.1
Peptidyl-prolyl cis-trans isomerase B (cyclophilin B).
 
 0.869
rplX
Large subunit ribosomal protein L24; One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
   
 
 0.866
Your Current Organism:
Mucilaginibacter lappiensis
NCBI taxonomy Id: 354630
Other names: LMG 25358, LMG:25358, M. lappiensis, Mucilaginibacter lappiensis Mannisto et al. 2010, Mucilaginibacter sp. ANJLI2, Mucilaginibacter sp. MP601, Mucilaginibacter sp. RA1BR4, Sphingobacteriaceae bacterium ANJLI2, strain ANJLI2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.