STRINGSTRING
SEH51445.1 SEH51445.1 dnaN dnaN polA polA uvrD uvrD SEH58872.1 SEH58872.1 rep rep uvrA uvrA radA radA SEH66123.1 SEH66123.1 sbcD sbcD recN recN nth nth ung ung SEH72360.1 SEH72360.1 SEH72728.1 SEH72728.1 mutS mutS recA recA recX recX dinG dinG rnhB rnhB uvrB uvrB dinB dinB recQ recQ SEH82261.1 SEH82261.1 ligA ligA xthA xthA SEH84448.1 SEH84448.1 ligD ligD uvrC uvrC SEH88755.1 SEH88755.1 polB polB lexA lexA SEH96211.1 SEH96211.1 topA topA SEI02542.1 SEI02542.1 SEI02850.1 SEI02850.1 SEI05337.1 SEI05337.1 mutL mutL SEI08453.1 SEI08453.1
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.
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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:
SEH51445.1ATP-dependent DNA helicase, RecQ-like. (641 aa)
dnaNDNA polymerase-3 subunit beta; 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 re [...] (367 aa)
polADNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. (914 aa)
uvrDATP-dependent DNA helicase UvrD. (729 aa)
SEH58872.1Exodeoxyribonuclease-3. (259 aa)
repATP-dependent DNA helicase Rep; Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction. (669 aa)
uvrAExcinuclease ABC subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. (949 aa)
radADNA replication and repair protein RadA; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. (453 aa)
SEH66123.1Exonuclease SbcC. (1220 aa)
sbcDExodeoxyribonuclease I subunit D; 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. (411 aa)
recNDNA repair protein RecN (Recombination protein N); May be involved in recombinational repair of damaged DNA. (558 aa)
nthDNA-(apurinic or apyrimidinic site) lyase; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. (212 aa)
ungUracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. (231 aa)
SEH72360.1Exodeoxyribonuclease-3. (281 aa)
SEH72728.1DNA topoisomerase-3. (654 aa)
mutSDNA mismatch repair protein MutS; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. (856 aa)
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. (347 aa)
recXRegulatory protein; Modulates RecA activity; Belongs to the RecX family. (153 aa)
dinGATP-dependent DNA helicase DinG; DNA-dependent ATPase and 5'-3' DNA helicase. (714 aa)
rnhBRNase HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (215 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 [...] (671 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. (360 aa)
recQATP-dependent DNA helicase RecQ. (707 aa)
SEH82261.1DNA-3-methyladenine glycosylase II. (304 aa)
ligADNA ligase (NAD+); DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA; Belongs to the NAD-dependent DNA ligase family. LigA subfamily. (788 aa)
xthAExodeoxyribonuclease-3. (270 aa)
SEH84448.1DNA topoisomerase-1. (375 aa)
ligDBifunctional non-homologous end joining protein LigD. (854 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. (606 aa)
SEH88755.1UvrD/REP helicase N-terminal domain-containing protein. (659 aa)
polBDNA polymerase-2. (787 aa)
lexASOS-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. (202 aa)
SEH96211.1Cell division inhibitor SulA. (159 aa)
topADNA topoisomerase-1; 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 [...] (870 aa)
SEI02542.1Hypothetical protein. (87 aa)
SEI02850.1DNA-3-methyladenine glycosylase. (232 aa)
SEI05337.1AraC family transcriptional regulator, regulatory protein of adaptative response / methylated-DNA-[protein]-cysteine methyltransferase. (345 aa)
mutLDNA mismatch repair protein MutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex. (625 aa)
SEI08453.1DNA ligase (NAD+). (557 aa)
Your Current Organism:
Pseudomonas xanthomarina
NCBI taxonomy Id: 271420
Other names: CCUG 46543, DSM 18231, JCM 12468, NRIC 0617, P. xanthomarina, Pseudomonas xanthomarina Romanenko et al. 2005
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