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
rnhARibonuclease HI; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (154 aa)    
Predicted Functional Partners:
dnaQ
DNA polymerase III subunit epsilon; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease.
 
  
 0.953
ANP67537.1
Ribonuclease H; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.921
sbcD
Exonuclease sbcCD subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family.
      
 0.786
rnd
Ribonuclease D; Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides; Belongs to the RNase D family.
  
 
 0.720
rnhB
Ribonuclease HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
   
 
 0.712
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 [...]
   
 
 0.691
rnt
Ribonuclease T; Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
  
  
 0.679
clpA
ATP-dependent Clp protease ATP-binding subunit ClpA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family.
      
 0.620
ANP65408.1
TIGR03503 family protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.610
ANP64292.1
Single-stranded DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.580
Your Current Organism:
Vibrio alginolyticus
NCBI taxonomy Id: 663
Other names: ATCC 17749, Beneckea alginolytica, CAIM 516, CCUG 13445, CCUG 16315, CCUG 4989, CIP 103336, CIP 75.3, DSM 2171, IFO 15630, LMG 4409, LMG:4409, NBRC 15630, NCCB 71013, NCCB 77003, NCTC 12160, Oceanomonas alginolytica, Pseudomonas creosotensis, V. alginolyticus, Vibrio sp. PeIg0901
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.