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
Ping_0074PFAM: DNA topoisomerase, type IA, zn finger domain protein; KEGG: pha:PSHAa0027 DNA topoisomerase. (187 aa)    
Predicted Functional Partners:
tsaC
Translation factor SUA5; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
 
    0.863
topB
DNA topoisomerase III; 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 su [...]
  
 
 0.859
smg
PFAM: protein of unknown function DUF494; KEGG: ilo:IL0020 hypothetical protein; Belongs to the Smg family.
 
     0.840
Ping_0076
TIGRFAM: DNA protecting protein DprA; PFAM: SMF family protein; KEGG: pat:Patl_0025 DNA protecting protein DprA.
     0.763
purE
Phosphoribosylaminoimidazole carboxylase, catalytic subunit; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
       0.634
Ping_3391
Single-strand 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.
  
 
 0.544
aroE
Shikimate dehydrogenase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
       0.500
Ping_0077
PFAM: Peptidoglycan-binding LysM; KEGG: sfr:Sfri_0025 peptidoglycan-binding LysM.
       0.489
polA
Fused DNA polymerase 5'->3' exonuclease and 3'->5' polymerase and 3'->5' exonuclease; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
     
 0.434
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.
 
     0.427
Your Current Organism:
Psychromonas ingrahamii
NCBI taxonomy Id: 357804
Other names: P. ingrahamii 37, Psychromonas ingrahamii 37, Psychromonas ingrahamii str. 37, Psychromonas ingrahamii strain 37, gas vacuolate str. 37
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.