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
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
KDS86317.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (525 aa)    
Predicted Functional Partners:
pnp
Polynucleotide phosphorylase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
 
 
 0.914
KDS84198.1
Carbohydrate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.843
KDS87628.1
Cyclophilin; 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.
 
 
 0.828
KDS84537.1
Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.818
rpsA
30S ribosomal protein S1; In Escherichia coli this protein is involved in binding to the leader sequence of mRNAs and is itself bound to the 30S subunit; autoregulates expression via a C-terminal domain; in most gram negative organisms this protein is composed of 6 repeats of the S1 domain while in gram positive there are 4 repeats; the S1 nucleic acid-binding domain is found associated with other proteins; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.809
KDS86318.1
Cold-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.795
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.
   
 
 0.793
fusA
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 subfamily.
   
 0.767
KDS84703.1
Elongation factor G; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.767
KDS87629.1
Nosiheptide resistance regulatory protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.762
Your Current Organism:
Streptomyces fradiae
NCBI taxonomy Id: 1906
Other names: ATCC 10745, ATCC 19760, Actinomyces fradii, BCRC 12196, CBS 498.68, CCM 3174, CCRC 12196, CCRC:12196, CECT 3197, DSM 40063, HAMBI 965, HUT 6095, IFO 12773, IFO 3718, IMET 42051, IMI 061202, ISP 5063, JCM 4133, JCM 4579, JCM 4824 [[Streptomyces roseoflavus]], KCTC 9760, NBRC 12773, NBRC 13439 [[Streptomyces roseoflavus]], NBRC 3718, NCIMB 11005, NCIMB 8233, NRRL B-2789 [[Streptomyces roseoflavus]], NRRL-ISP 5063, PCM 2330, RIA 97, S. fradiae, Streptomyces fradiae subsp. fradiae, Streptomyces fradii, Streptomyces roseiflavus, Streptomyces roseoflavus, Streptomyces sp. NEAE-82, UNIQEM 146, VKM Ac-150, VKM Ac-151, VKM Ac-152, VKM Ac-764
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