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
rnj-2Ribonuclease J; An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay; Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily. (561 aa)    
Predicted Functional Partners:
rnj
Zn-dependent hydrolase; An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay; Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily.
  
  
0.914
AKS73987.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0356 family.
  
    0.901
rny
Ribonuclease; Endoribonuclease that initiates mRNA decay.
  
 
 0.709
rnpA
Ribonuclease P; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
    
 
 0.595
pnpA
Polynucleotide phosphorylase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
 
  
 0.573
AKS73140.1
RNA helicase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the DEAD box helicase family.
   
  
 0.563
AKS73986.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.498
tig
Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily.
 
    0.477
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
 
  
 0.466
ispA
Geranyl transferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FPP/GGPP synthase family.
  
    0.459
Your Current Organism:
Staphylococcus schleiferi
NCBI taxonomy Id: 1295
Other names: ATCC 43808, CCUG 25351, CIP 103643, DSM 4807, LMG 13347, LMG:13347, NCTC 12218, NRRL B-14775, S. schleiferi, strain N850274
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.