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
Srot_0211DEAD/DEAH box helicase domain protein; KEGG: rop:ROP_64170 putative ATP-dependent RNA helicase; PFAM: DEAD/DEAH box helicase domain protein; helicase domain protein; SMART: DEAD-like helicase; helicase domain protein; Belongs to the DEAD box helicase family. (495 aa)    
Predicted Functional Partners:
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 [...]
   
 0.842
nnrD
Carbohydrate kinase, YjeF related 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. In the C-terminal section; belongs to the NnrD/CARKD family.
  
 0.834
pnp
Guanosine pentaphosphate synthetase I/polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
 
 0.805
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.
  
 0.802
Srot_0210
KEGG: rha:RHA1_ro06355 hypothetical protein.
  
    0.796
Srot_0662
PFAM: RNA binding S1 domain protein; KEGG: msm:MSMEG_3833 30S ribosomal protein S1.
   
 0.778
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.
   
 0.778
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.
   
 0.764
rplC
50S ribosomal protein L3; 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.
   
 
 0.727
Srot_0209
PFAM: Phosphoglycerate mutase; KEGG: mab:MAB_3534 acid phosphatase.
   
   0.704
Your Current Organism:
Segniliparus rotundus
NCBI taxonomy Id: 640132
Other names: S. rotundus DSM 44985, Segniliparus rotundus ATCC BAA-972, Segniliparus rotundus CIP 108378, Segniliparus rotundus DSM 44985, Segniliparus rotundus JCM 13578, Segniliparus rotundus str. DSM 44985, Segniliparus rotundus strain DSM 44985
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.