STRINGSTRING
OLR19291.1 OLR19291.1 OLR17637.1 OLR17637.1 mutM mutM mug mug OLR18274.1 OLR18274.1 ung ung nth nth OLR20517.1 OLR20517.1 nei nei
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
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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:
OLR19291.1DNA-3-methyladenine glycosylase I; Derived by automated computational analysis using gene prediction method: Protein Homology. (192 aa)
OLR17637.1DNA-3-methyladenine glycosylase 2; Derived by automated computational analysis using gene prediction method: Protein Homology. (288 aa)
mutMDNA-formamidopyrimidine 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)
mugDouble-stranded uracil-DNA glycosylase; Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells; Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family. (168 aa)
OLR18274.1A/G-specific adenine glycosylase; Adenine glycosylase active on G-A mispairs. (352 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. (229 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)
OLR20517.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (409 aa)
neiEndonuclease VIII; 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 pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. 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. (263 aa)
Your Current Organism:
Enterobacter kobei
NCBI taxonomy Id: 208224
Other names: ATCC BAA-260, CCUG 49023, CIP 105566, DSM 13645, E. kobei, Enterobacter sp. 35730, Enterobacter sp. 42202, Enterobacter sp. 44593, Enterobacter sp. GN02186, Enterobacter sp. GN02204, Enterobacter sp. GN02225, Enterobacter sp. GN02266, Enterobacter sp. GN02275, Enterobacter sp. GN02366, Enterobacter sp. GN02454, Enterobacter sp. GN02825, Enterobacter sp. GN03191, JCM 8580, NIH group 21
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