STRINGSTRING
recF recF ruvB ruvB dinB dinB recA recA uvrB uvrB SFQ25293.1 SFQ25293.1 ruvA ruvA uvrC uvrC SFQ37354.1 SFQ37354.1 SFQ48455.1 SFQ48455.1 SFQ48468.1 SFQ48468.1 SFQ52880.1 SFQ52880.1 SFQ53356.1 SFQ53356.1 SFQ53369.1 SFQ53369.1
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:
recFDNA replication and repair protein RecF; The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. (370 aa)
ruvBHolliday junction DNA helicase subunit RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. (352 aa)
dinBDNA polymerase-4; 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. (359 aa)
recARecombination protein RecA; 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. (371 aa)
uvrBExcinuclease ABC subunit B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] (680 aa)
SFQ25293.1Cell surface protein SprA. (2464 aa)
ruvAHolliday junction DNA helicase subunit RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. (201 aa)
uvrCExcinuclease ABC subunit C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. (611 aa)
SFQ37354.1ATP-dependent DNA helicase RecQ. (734 aa)
SFQ48455.1DNA polymerase V; Belongs to the peptidase S24 family. (157 aa)
SFQ48468.1DNA polymerase V. (431 aa)
SFQ52880.1ATP-dependent DNA helicase RecQ. (908 aa)
SFQ53356.1SOS response UmuD protein. Serine peptidase. MEROPS family S24; Belongs to the peptidase S24 family. (151 aa)
SFQ53369.1DNA polymerase V. (443 aa)
Your Current Organism:
Siccationidurans arizonensis
NCBI taxonomy Id: 1227077
Other names: DSM 17870, Hymenobacter arizonensis, Hymenobacter arizonensis Reddy and Garcia-Pichel 2013, Hymenobacter sp. OR362-8, JCM 13504, S. arizonensis, strain OR362-8
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