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
ADU96311.1PFAM: peptidase M24; creatinase; KEGG: gtn:GTNG_2342 proline dipeptidase. (343 aa)    
Predicted Functional Partners:
guaB
Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
   
   0.892
hslV
20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
       0.783
hslU
Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
       0.781
ADU96308.1
KEGG: geo:Geob_1483 hypothetical protein.
       0.762
ADU96988.1
PFAM: ATP-citrate lyase/succinyl-CoA ligase; KEGG: pmx:PERMA_1714 ATP-citrate synthase (ATP-citrate (pro-S-)-lyase)(citrate cleavage enzyme).
  
 
 0.611
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 [...]
  
  
 0.594
pheT
TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: tte:TTE1688 phenylalanyl-tRNA synthetase subunit beta.
     
 0.581
ADU97341.1
PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; KEGG: hya:HY04AAS1_0082 pyruvate flavodoxin/ferredoxin oxidoreductase domain protein.
     
 0.566
ADU96307.1
PFAM: Protein of unknown function DUF2081; protein of unknown function DUF262; KEGG: kol:Kole_0055 protein of unknown function DUF262.
       0.502
atpE
ATP synthase F0, C subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
 
  
 0.464
Your Current Organism:
Thermovibrio ammonificans
NCBI taxonomy Id: 648996
Other names: T. ammonificans HB-1, Thermovibrio ammonificans DSM 15698, Thermovibrio ammonificans HB-1, Thermovibrio ammonificans str. HB-1, Thermovibrio ammonificans strain HB-1
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