STRINGSTRING
recA recA polA polA lexA lexA Dde_1932 Dde_1932 Dde_2974 Dde_2974 Dde_2446 Dde_2446 Dde_0002 Dde_0002 Dde_3499 Dde_3499 Dde_3571 Dde_3571 Dde_2596 Dde_2596 dinB dinB
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
recArecA 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. (351 aa)    
Predicted Functional Partners:
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
 
 0.988
lexA
SOS-response transcriptional repressor, LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
  
 
 0.956
Dde_1932
SOS-response transcriptional repressor, LexA; Represses a number of genes involved in the response to DNA damage (SOS response).
  
 
 0.939
Dde_2974
PFAM: Peptidase S24/S26A/S26B, conserved region; KEGG: dvl:Dvul_0458 prophage repressor; Belongs to the peptidase S24 family.
  
 
 0.939
Dde_2446
TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type, N-terminal; PFAM: RQC domain; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; DNA/RNA helicase, C-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: das:Daes_0230 ATP-dependent DNA helicase RecQ; SMART: DEAD-like helicase, N-terminal; DNA/RNA helicase, C-terminal; Helicase/RNase D C-terminal, HRDC domain.
  
 0.921
Dde_0002
SMART: DNA polymerase III, beta chain; TIGRFAM: DNA polymerase III, beta chain; KEGG: dvl:Dvul_0006 subunit beta; PFAM: DNA polymerase III, beta chain.
  
 0.904
Dde_3499
PFAM: DNA helicase, UvrD/REP type; PHP, C-terminal; KEGG: dvl:Dvul_2483 UvrD/REP helicase.
 
 
 0.896
Dde_3571
PFAM: DNA helicase, UvrD/REP type; KEGG: dvm:DvMF_1967 UvrD/REP helicase.
  
 
 0.878
Dde_2596
SMC domain protein; May be involved in recombinational repair of damaged DNA.
  
  
 0.849
dinB
DNA-directed DNA polymerase; 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, in conjunction with the beta clamp from PolIII.
  
 0.845
Your Current Organism:
Desulfovibrio alaskensis
NCBI taxonomy Id: 207559
Other names: D. alaskensis G20, Desulfovibrio alaskensis G20, Desulfovibrio alaskensis str. G20, Desulfovibrio alaskensis strain G20, Desulfovibrio desulfuricans subsp. desulfuricans str. G20
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.