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
addARecombination helicase AddA; The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities; Belongs to the helicase family. AddA subfamily. (1377 aa)    
Predicted Functional Partners:
addB
ATP-dependent nuclease subunit B; The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity.
 
 
 0.999
recD2
Helicase, RecD/TraA family; DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity; Belongs to the RecD family. RecD-like subfamily.
  
 
 0.881
sbcD
Nuclease SbcCD, D subunit; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family.
 
  
 0.766
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
     
 0.701
Cphy_1246
PFAM: SMC domain protein; KEGG: ctc:CTC00579 exonuclease sbcC.
 
  
 0.664
Cphy_3520
PFAM: protein of unknown function DUF633; KEGG: cac:CAC1302 predicted SAM-dependent methyltransferase.
 
     0.633
Cphy_3350
KEGG: cac:CAC1655 bifunctional enzyme phosphoribosylformylglycinamidine (FGAM) synthase (synthetase domain/glutamine amidotransferase domain); TIGRFAM: phosphoribosylformylglycinamidine synthase; PFAM: AIR synthase related protein domain protein.
     
 0.595
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.
  
 
 0.577
Cphy_1745
KEGG: lpf:lpl1156 methylated-DNA-[protein]-cysteine S-methyltransferase; TIGRFAM: methylated-DNA--protein-cysteine methyltransferase; PFAM: Ada metal-binding domain protein; Methylated-DNA-[protein]-cysteine S-methyltransferase DNA binding; SMART: helix-turn-helix- domain containing protein AraC type.
     
 0.574
Cphy_3425
Hypothetical protein.
       0.565
Your Current Organism:
Lachnoclostridium phytofermentans
NCBI taxonomy Id: 357809
Other names: Clostridium phytofermentans ISDg, L. phytofermentans ISDg, Lachnoclostridium phytofermentans ISDg
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.