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ACS83877.1 ACS83877.1 mutM mutM ligA ligA nth nth ACS85754.1 ACS85754.1 nfo nfo ung ung ACS86800.1 ACS86800.1 ACS86947.1 ACS86947.1 ACS87060.1 ACS87060.1 ligB ligB polA polA
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query proteins and first shell of interactors
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second shell of interactors
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filled nodes:
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ACS83877.1KEGG: eca:ECA0082 DNA-3-methyladenine glycosylase I; TIGRFAM: DNA-3-methyladenine glycosylase I; PFAM: methyladenine glycosylase. (212 aa)
mutMformamidopyrimidine-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). 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. (269 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; Belongs to the NAD-dependent DNA ligase family. LigA subfamily. (684 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. (211 aa)
ACS85754.1TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase; KEGG: ypi:YpsIP31758_1976 exonuclease III. (268 aa)
nfoApurinic endonuclease Apn1; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. (288 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. (228 aa)
ACS86800.1A/G-specific adenine glycosylase; Adenine glycosylase active on G-A mispairs. (363 aa)
ACS86947.1KEGG: eca:ECA0907 putative DNA-3-methyladenine glycosylase; PFAM: HhH-GPD family protein; SMART: HhH-GPD family protein. (225 aa)
ACS87060.1TIGRFAM: single-stranded-DNA-specific exonuclease RecJ; PFAM: phosphoesterase RecJ domain protein; phosphoesterase DHHA1; KEGG: eca:ECA0772 ssDNA exonuclease RecJ. (580 aa)
ligBDNA ligase (NAD(+)); 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. Belongs to the NAD-dependent DNA ligase family. LigB subfamily. (575 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. (931 aa)
Your Current Organism:
Dickeya paradisiaca
NCBI taxonomy Id: 579405
Other names: D. paradisiaca Ech703, Dickeya dadantii Ech703, Dickeya paradisiaca Ech703
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