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.
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:
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[Homology]
Score
Gobs_4232PFAM: UvrD/REP helicase; HRDC domain protein; SMART: HRDC domain protein; KEGG: art:Arth_2753 UvrD/REP helicase. (674 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.
  
 0.987
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 [...]
 
 0.981
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.
 
 0.977
Gobs_0002
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 [...]
 
 0.969
Gobs_4360
KEGG: sen:SACE_0953 putative ATP-dependent dsDNA exonuclease.
  
 0.962
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.
  
 0.960
Gobs_4243
PFAM: UvrD/REP helicase; KEGG: saq:Sare_4130 UvrD/REP helicase.
 
  
0.957
Gobs_4430
TIGRFAM: ATP-dependent DNA helicase PcrA; PFAM: UvrD/REP helicase; KEGG: sco:SCO4797 ATP-dependent DNA helicase II.
 
0.956
Gobs_0747
PFAM: TrwC relaxase; DNA primase catalytic core domain; TOPRIM domain protein; SMART: Toprim sub domain protein; KEGG: nca:Noca_4800 DNA primase catalytic core.
  
 
 0.955
Gobs_2694
PFAM: 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2; KEGG: kra:Krad_1887 5'-3' exonuclease.
 
 0.948
Your Current Organism:
Geodermatophilus obscurus
NCBI taxonomy Id: 526225
Other names: G. obscurus DSM 43160, Geodermatophilus obscurus ATCC 25078, Geodermatophilus obscurus DSM 43160, Geodermatophilus obscurus IFO 13315, Geodermatophilus obscurus JCM 3152, Geodermatophilus obscurus NBRC 13315, Geodermatophilus obscurus NRRL B-3577, Geodermatophilus obscurus VKM Ac-658, Geodermatophilus obscurus str. DSM 43160, Geodermatophilus obscurus strain DSM 43160
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