STRINGSTRING
AB434_0222 AB434_0222 ligA ligA ung ung AB434_2137 AB434_2137 AB434_3099 AB434_3099 nth nth nfo nfo AB434_3617 AB434_3617 mutM mutM polA polA
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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
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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co-expression
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Your Input:
AB434_0222A/G-specific adenine glycosylase; Adenine glycosylase active on G-A mispairs. (372 aa)
ligADNA ligase; 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. (668 aa)
ungUracil-DNA glycosylase, family 1; 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)
AB434_2137DNA-3-methyladenine glycosylase II; Belongs to the DNA glycosylase MPG family. (200 aa)
AB434_3099Exodeoxyribonuclease III. (251 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. (219 aa)
nfoEndonuclease IV; 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. (299 aa)
AB434_3617Single-stranded-DNA-specific exonuclease RecJ. (787 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. (277 aa)
polADNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. (888 aa)
Your Current Organism:
Bacillus coagulans
NCBI taxonomy Id: 1398
Other names: ATCC 7050, B. coagulans, BCRC 10606, Bacillus sp. NCIM 2323, CCM 2013, CCRC 10606, CCRC:10606, CCUG 7417, CFBP 4225, CIP 66.25, DSM 1, IFO 12583, IMET 10993, JCM 2257, LMG 6326, LMG:6326, Lactobacillus sp. T4, NBRC 12583, NCAIM B.01086, NCCB 48014, NCCB 77025, NCIB 9365, NCIMB 9365, NCTC 10334, NRRL NRS-609, VKM B-731
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