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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ADQ05401.1KEGG: ate:Athe_2182 DNA protecting protein DprA; TIGRFAM: DNA protecting protein DprA; PFAM: SMF family protein. (365 aa)    
Predicted Functional Partners:
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 [...]
   
 0.935
ADQ04967.1
PFAM: phosphoribosyltransferase; KEGG: ate:Athe_1679 phosphoribosyltransferase.
 
 
 0.897
ADQ05183.1
KEGG: ate:Athe_1921 DNA internalization-related competence protein ComEC/Rec2; TIGRFAM: DNA internalization-related competence protein ComEC/Rec2; ComEC/Rec2-related protein; PFAM: ComEC/Rec2-related protein.
 
  
 0.893
ADQ05409.1
TIGRFAM: Mg chelatase, subunit ChlI; PFAM: magnesium chelatase ChlI subunit; KEGG: ate:Athe_2193 Mg chelatase, subunit ChlI; SMART: AAA ATPase.
 
 0.845
ADQ05144.1
KEGG: csc:Csac_1065 peptidase A24A domain-containing protein; PFAM: peptidase A24A domain protein; peptidase A24A prepilin type IV.
  
  
 0.784
trmFO
Gid protein; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily.
       0.775
hslV
20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
   0.757
ADQ05379.1
KEGG: ate:Athe_2160 CheC, inhibitor of MCP methylation / FliN fusion protein; TIGRFAM: flagellar motor switch protein FliN; PFAM: surface presentation of antigens (SPOA) protein; CheC domain protein.
  
    0.721
recA
recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
   
 
 0.716
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.
       0.713
Your Current Organism:
Caldicellulosiruptor owensensis
NCBI taxonomy Id: 632518
Other names: C. owensensis OL, Caldicellulosiruptor owensensis DSM 13100, Caldicellulosiruptor owensensis OL, Caldicellulosiruptor owensensis str. OL, Caldicellulosiruptor owensensis strain OL
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.