node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
alkA | fpg | Rv1317c | Rv2924c | Probable bifunctional transcriptional activator/DNA repair enzyme AlkA; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the Sp diastereomer of DNA methylphosphotriester lesions by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. Also catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions (By similarity); In the C-terminal sect [...] | Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves [...] | 0.654 |
alkA | mutY | Rv1317c | Rv3589 | Probable bifunctional transcriptional activator/DNA repair enzyme AlkA; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the Sp diastereomer of DNA methylphosphotriester lesions by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. Also catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions (By similarity); In the C-terminal sect [...] | Probable adenine glycosylase MutY; Adenine glycosylase active on G:A and C:A mispairs, as well as processing 7,8-dihydro-8-oxoguanine:A (8-oxoG) mismatches. Minor activity against 8-oxoG:G and 8-oxo:T mismatches is also seen. Bind dsDNA oligonucleotides containing the above mismatches. | 0.783 |
alkA | nth | Rv1317c | Rv3674c | Probable bifunctional transcriptional activator/DNA repair enzyme AlkA; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the Sp diastereomer of DNA methylphosphotriester lesions by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. Also catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions (By similarity); In the C-terminal sect [...] | Endonuclease 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. Has a preference for oxidized pyrimidines, such as thymine glycol (prefers 5S isomers) 5,6-dihydrouracil:G, 5-hydroxyuracil:G, 5- hydroxycytosine:G and urea [...] | 0.652 |
alkA | uvrB | Rv1317c | Rv1633 | Probable bifunctional transcriptional activator/DNA repair enzyme AlkA; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the Sp diastereomer of DNA methylphosphotriester lesions by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. Also catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions (By similarity); In the C-terminal sect [...] | Probable excinuclease ABC (subunit B-helicase) UvrB; 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 [...] | 0.557 |
alkA | uvrD1 | Rv1317c | Rv0949 | Probable bifunctional transcriptional activator/DNA repair enzyme AlkA; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the Sp diastereomer of DNA methylphosphotriester lesions by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. Also catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions (By similarity); In the C-terminal sect [...] | Probable ATP-dependent DNA helicase II UvrD1; DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. A minimal tail of 18 nt is required for activity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair, as well as in nitrosative and oxidative stress response and possibly in persistence in the host. Inhibits RecA-mediated DNA strand exchange; this does not require ATPase activity. When combined with UvrA greatly inhibits RecA- mediated DNA strand exchange; Belongs to the helicase family. UvrD sub [...] | 0.495 |
alkA | xthA | Rv1317c | Rv0427c | Probable bifunctional transcriptional activator/DNA repair enzyme AlkA; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the Sp diastereomer of DNA methylphosphotriester lesions by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. Also catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions (By similarity); In the C-terminal sect [...] | Probable exodeoxyribonuclease III protein XthA (exonuclease III) (EXO III) (AP endonuclease VI); Rv0427c, (MTCY22G10.24c), len: 291 aa. Probable xthA (alternate gene name: xth), exodeoxyribonuclease III protein (see citation below), similar to others e.g. EX3_ECOLI|P09030 exodeoxyribonuclease III from Escherichia Coli strain K12 (268 aa), FASTA scores: opt: 360, E(): 1.2e-17, (29.3% identity in 270 aa overlap); etc. Belongs to the AP/EXOA family of DNA repair enzymes. | 0.894 |
canB | mutY | Rv3588c | Rv3589 | Beta-carbonic anhydrase CanB; Catalyzes the reversible hydration of carbon dioxide to form bicarbonate; Belongs to the beta-class carbonic anhydrase family. | Probable adenine glycosylase MutY; Adenine glycosylase active on G:A and C:A mispairs, as well as processing 7,8-dihydro-8-oxoguanine:A (8-oxoG) mismatches. Minor activity against 8-oxoG:G and 8-oxo:T mismatches is also seen. Bind dsDNA oligonucleotides containing the above mismatches. | 0.857 |
canB | xthA | Rv3588c | Rv0427c | Beta-carbonic anhydrase CanB; Catalyzes the reversible hydration of carbon dioxide to form bicarbonate; Belongs to the beta-class carbonic anhydrase family. | Probable exodeoxyribonuclease III protein XthA (exonuclease III) (EXO III) (AP endonuclease VI); Rv0427c, (MTCY22G10.24c), len: 291 aa. Probable xthA (alternate gene name: xth), exodeoxyribonuclease III protein (see citation below), similar to others e.g. EX3_ECOLI|P09030 exodeoxyribonuclease III from Escherichia Coli strain K12 (268 aa), FASTA scores: opt: 360, E(): 1.2e-17, (29.3% identity in 270 aa overlap); etc. Belongs to the AP/EXOA family of DNA repair enzymes. | 0.480 |
fpg | alkA | Rv2924c | Rv1317c | Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves [...] | Probable bifunctional transcriptional activator/DNA repair enzyme AlkA; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the Sp diastereomer of DNA methylphosphotriester lesions by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. Also catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions (By similarity); In the C-terminal sect [...] | 0.654 |
fpg | mutY | Rv2924c | Rv3589 | Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves [...] | Probable adenine glycosylase MutY; Adenine glycosylase active on G:A and C:A mispairs, as well as processing 7,8-dihydro-8-oxoguanine:A (8-oxoG) mismatches. Minor activity against 8-oxoG:G and 8-oxo:T mismatches is also seen. Bind dsDNA oligonucleotides containing the above mismatches. | 0.968 |
fpg | nei | Rv2924c | Rv3297 | Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves [...] | Probable endonuclease VIII Nei; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity). Complements an E.coli nei nth double mutant. | 0.528 |
fpg | nei1 | Rv2924c | Rv2464c | Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves [...] | Possible DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. DNA glycosylase that recognizes and removes damaged pyrimidines. Excises Tg:A (thymine glycol, prefers 5R isomers), Tg:G, 5,6-dihydrouracil:G base pairs and urea:A, also excises oxidized purine derivatives guanidinohydantoin:C and spiroiminodihydantoin:C. Poorly cleaves dsDNA with uracil substitutions, thus also acting as a weak uracil-DNA glycosylase. Acts on DNA bubble and 3'-fork structures, suggesting a role in replication-associated DNA repair. Activity on 7,8-dihydro-8-o [...] | 0.570 |
fpg | nth | Rv2924c | Rv3674c | Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves [...] | Endonuclease 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. Has a preference for oxidized pyrimidines, such as thymine glycol (prefers 5S isomers) 5,6-dihydrouracil:G, 5-hydroxyuracil:G, 5- hydroxycytosine:G and urea [...] | 0.915 |
fpg | udgB | Rv2924c | Rv1259 | Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves [...] | Probable uracil DNA glycosylase, UdgB; DNA glycosylase with broad substrate specificity. Can remove uracil from double-stranded DNA containing either a U/G, U/A, U/C or U/T base pair. Can also excise ethenocytosine and hypoxanthine from double-stranded DNA. | 0.757 |
fpg | uvrB | Rv2924c | Rv1633 | Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves [...] | Probable excinuclease ABC (subunit B-helicase) UvrB; 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 [...] | 0.732 |
fpg | uvrD1 | Rv2924c | Rv0949 | Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves [...] | Probable ATP-dependent DNA helicase II UvrD1; DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. A minimal tail of 18 nt is required for activity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair, as well as in nitrosative and oxidative stress response and possibly in persistence in the host. Inhibits RecA-mediated DNA strand exchange; this does not require ATPase activity. When combined with UvrA greatly inhibits RecA- mediated DNA strand exchange; Belongs to the helicase family. UvrD sub [...] | 0.559 |
mutY | alkA | Rv3589 | Rv1317c | Probable adenine glycosylase MutY; Adenine glycosylase active on G:A and C:A mispairs, as well as processing 7,8-dihydro-8-oxoguanine:A (8-oxoG) mismatches. Minor activity against 8-oxoG:G and 8-oxo:T mismatches is also seen. Bind dsDNA oligonucleotides containing the above mismatches. | Probable bifunctional transcriptional activator/DNA repair enzyme AlkA; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the Sp diastereomer of DNA methylphosphotriester lesions by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. Also catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions (By similarity); In the C-terminal sect [...] | 0.783 |
mutY | canB | Rv3589 | Rv3588c | Probable adenine glycosylase MutY; Adenine glycosylase active on G:A and C:A mispairs, as well as processing 7,8-dihydro-8-oxoguanine:A (8-oxoG) mismatches. Minor activity against 8-oxoG:G and 8-oxo:T mismatches is also seen. Bind dsDNA oligonucleotides containing the above mismatches. | Beta-carbonic anhydrase CanB; Catalyzes the reversible hydration of carbon dioxide to form bicarbonate; Belongs to the beta-class carbonic anhydrase family. | 0.857 |
mutY | fpg | Rv3589 | Rv2924c | Probable adenine glycosylase MutY; Adenine glycosylase active on G:A and C:A mispairs, as well as processing 7,8-dihydro-8-oxoguanine:A (8-oxoG) mismatches. Minor activity against 8-oxoG:G and 8-oxo:T mismatches is also seen. Bind dsDNA oligonucleotides containing the above mismatches. | Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves [...] | 0.968 |
mutY | nei | Rv3589 | Rv3297 | Probable adenine glycosylase MutY; Adenine glycosylase active on G:A and C:A mispairs, as well as processing 7,8-dihydro-8-oxoguanine:A (8-oxoG) mismatches. Minor activity against 8-oxoG:G and 8-oxo:T mismatches is also seen. Bind dsDNA oligonucleotides containing the above mismatches. | Probable endonuclease VIII Nei; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity). Complements an E.coli nei nth double mutant. | 0.890 |