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
ACX96462.1KEGG: lme:LEUM_1109 hypothetical protein. (196 aa)    
Predicted Functional Partners:
ACX96463.1
Hypothetical protein.
       0.727
recC
Exodeoxyribonuclease V, gamma subunit; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and r [...]
  
 
 0.592
ACX94868.1
DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]
  
 
 0.558
ACX96461.1
Hypothetical protein.
       0.554
recB
Exodeoxyribonuclease V, beta subunit; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and re [...]
  
 
 0.553
ACX96464.1
PFAM: RES domain protein; KEGG: ter:Tery_1503 hypothetical protein.
       0.472
ACX96465.1
PFAM: conserved hypothetical protein; KEGG: tbd:Tbd_1342 hypothetical protein.
       0.472
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.
  
 
 0.453
ACX95162.1
KEGG: afr:AFE_2194 ATP-dependent DNA helicase RecQ; TIGRFAM: ATP-dependent DNA helicase RecQ; ATP-dependent DNA helicase, RecQ family; PFAM: RQC domain; DEAD/DEAH box helicase domain protein; helicase domain protein; HRDC domain protein; SMART: DEAD-like helicase; helicase domain protein; HRDC domain protein.
   
 
 0.416
Your Current Organism:
Halothiobacillus neapolitanus
NCBI taxonomy Id: 555778
Other names: H. neapolitanus c2, Halothiobacillus neapolitanus ATCC 23641, Halothiobacillus neapolitanus c2, Halothiobacillus neapolitanus str. c2, Halothiobacillus neapolitanus strain c2
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.