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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
AGB15402.1Hypothetical protein. (310 aa)    
Predicted Functional Partners:
gyrB
DNA gyrase, B subunit; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
   
 
 0.775
AGB15727.1
PFAM: ScpA/B protein.
  
 
 0.772
AGB17361.1
Deacetylase, histone deacetylase/acetoin utilization protein; PFAM: Histone deacetylase domain.
   
 0.615
topA
Topoisomerase IA; 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 superco [...]
  
 
 0.594
AGB15401.1
Mevalonate pyrophosphate decarboxylase; PFAM: GHMP kinases N terminal domain; TIGRFAM: diphosphomevalonate decarboxylase.
       0.531
AGB17678.1
PFAM: Helicase conserved C-terminal domain; DEAD/DEAH box helicase; Helix-hairpin-helix motif.
   
 
 0.518
AGB17633.1
Secreted protein with C-terminal beta-propeller domain; PFAM: Beta propeller domain.
    
 
 0.510
AGB15400.1
Putative transcriptional regulator; PFAM: ParB-like nuclease domain.
  
 
 0.469
dbh
nucleotidyltransferase/DNA polymerase involved in DNA repair; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.
  
 
 0.448
AGB14805.1
TPR repeat-containing protein; PFAM: Tetratricopeptide repeat.
  
 
 0.437
Your Current Organism:
Halovivax ruber
NCBI taxonomy Id: 797302
Other names: H. ruber XH-70, Halovivax ruber JCM 13892, Halovivax ruber XH-70, Halovivax ruber str. XH-70, Halovivax ruber strain XH-70
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