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ruvC ruvC ruvA ruvA ruvB ruvB Cthe_0247 Cthe_0247 uvrB uvrB uvrA uvrA Cthe_0355 Cthe_0355 Cthe_0458 Cthe_0458 Cthe_0772 Cthe_0772 lexA lexA Cthe_0814 Cthe_0814 polA polA Cthe_0968 Cthe_0968 ligA ligA recA recA nth nth Cthe_1554 Cthe_1554 Cthe_1735 Cthe_1735 Cthe_2068 Cthe_2068 dinB dinB Cthe_2208 Cthe_2208 Cthe_2372 Cthe_2372 uvrC uvrC Cthe_2876 Cthe_2876
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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ruvCCrossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. (162 aa)
ruvAHolliday junction DNA helicase 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. (202 aa)
ruvBHolliday junction DNA helicase 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. (330 aa)
Cthe_0247KEGG: swo:Swol_2027 MutS-like mismatch repair protein, ATPase; PFAM: DNA mismatch repair protein MutS domain protein; SMART: DNA mismatch repair protein MutS domain protein. (601 aa)
uvrBExcinuclease ABC, B subunit; 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 [...] (660 aa)
uvrAExcinuclease ABC, A subunit; 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. (942 aa)
Cthe_0355KEGG: hypothetical protein. (392 aa)
Cthe_0458TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; KEGG: aoe:Clos_2318 exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. (251 aa)
Cthe_0772PFAM: Peptidoglycan-binding lysin domain; KEGG: cce:Ccel_1692 peptidoglycan-binding LysM. (95 aa)
lexATranscriptional repressor, LexA family; 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. (213 aa)
Cthe_0814DNA repair protein RecN; May be involved in recombinational repair of damaged DNA. (570 aa)
polADNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. (894 aa)
Cthe_0968PFAM: UvrD/REP helicase; KEGG: ctc:CTC00692 DNA helicase II. (706 aa)
ligADNA ligase, NAD-dependent; 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. (663 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. (349 aa)
nthEndonuclease III; 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. (213 aa)
Cthe_1554KEGG: afn:Acfer_0164 methylated-DNA/protein-cysteinemethyltransferase; TIGRFAM: methylated-DNA/protein-cysteine methyltransferase; PFAM: Methylated-DNA-[protein]-cysteine S-methyltransferase DNA binding. (175 aa)
Cthe_1735PFAM: DNA polymerase B region; KEGG: cbb:CLD_2434 phage DNA polymerase. (563 aa)
Cthe_2068DNA-(apurinic or apyrimidinic site) lyase; PFAM: 8-oxoguanine DNA glycosylase domain-containing protein; KEGG: cce:Ccel_3329 8-oxoguanine DNA glycosylase domain protein; SMART: HhH-GPD family protein. (295 aa)
dinBDNA-directed DNA polymerase; 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. (399 aa)
Cthe_2208Transcriptional repressor, LexA family; PFAM: LexA DNA-binding domain protein; KEGG: cac:CAC1832 LexA repressor. (195 aa)
Cthe_2372DNA 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 [...] (366 aa)
uvrCExcinuclease ABC, C subunit; 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. (625 aa)
Cthe_2876KEGG: cce:Ccel_0373 ATP-dependent DNA helicase PcrA; TIGRFAM: ATP-dependent DNA helicase PcrA; PFAM: UvrD/REP helicase. (741 aa)
Your Current Organism:
Hungateiclostridium thermocellum
NCBI taxonomy Id: 203119
Other names: Clostridium thermocellum ATCC 27405, H. thermocellum ATCC 27405, Hungateiclostridium thermocellum ATCC 27405, Ruminiclostridium thermocellum ATCC 27405
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