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
KRM86572.1Ribonuclease hi; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (157 aa)    
Predicted Functional Partners:
polA
DNA-directed DNA polymerase; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
   
 0.961
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 [...]
   
 
 0.928
rnhB
Ribonuclease HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
   
 
 0.890
KRM87132.1
Single-strand DNA-binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.
   
 
 0.885
KRM88095.1
Hypothetical protein.
  
  
  0.609
prfB
Protein chain release factor B; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
   
   0.591
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
  
 
 0.531
KRM87140.1
DNA polymerase sliding clamp subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiatio [...]
    
 0.525
KRM86573.1
Branched-chain amino acid transport protein; Component of the transport system for branched-chain amino acids.
       0.524
KRM88035.1
DNA polymerase III.
    
 0.514
Your Current Organism:
Lactobacillus thailandensis
NCBI taxonomy Id: 1423810
Other names: L. thailandensis DSM 22698 = JCM 13996, Lactobacillus thailandensis DSM 22698, Lactobacillus thailandensis DSM 22698 = JCM 13996, Lactobacillus thailandensis JCM 13996, Lactobacillus thailandensis JCM 13996 = DSM 22698
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.