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
Dret_0017PFAM: protein of unknown function DUF116; KEGG: dvl:Dvul_0031 hypothetical protein. (298 aa)    
Predicted Functional Partners:
Dret_0018
PFAM: NusB/RsmB/TIM44; Fmu (Sun) domain protein; KEGG: dma:DMR_00320 rRNA (cytosine-C(5)-)- methyltransferase; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
       0.663
def
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
       0.600
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
       0.600
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
       0.572
Dret_0618
KEGG: dde:Dde_0419 hypothetical protein.
  
     0.559
Your Current Organism:
Desulfohalobium retbaense
NCBI taxonomy Id: 485915
Other names: D. retbaense DSM 5692, Desulfohalobium retbaense DSM 5692, Desulfohalobium retbaense str. DSM 5692, Desulfohalobium retbaense strain DSM 5692
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.