STRINGSTRING
OLR19291.1 OLR19291.1 polA polA OLR18768.1 OLR18768.1 mutM mutM OLR18711.1 OLR18711.1 OLR18708.1 OLR18708.1 mug mug OLR18274.1 OLR18274.1 OLR18226.1 OLR18226.1 xni xni ung ung OLR17740.1 OLR17740.1 nfo nfo OLR17637.1 OLR17637.1 OLR20889.1 OLR20889.1 nth nth OLR20774.1 OLR20774.1 nei nei OLR19322.1 OLR19322.1 ligA ligA
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.
Node Color
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
Edges:
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)
polADNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. (928 aa)
OLR18768.1DUF4862 domain-containing protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (310 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)
OLR18711.1XRE family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. (352 aa)
OLR18708.1DNA ligase B; Derived by automated computational analysis using gene prediction method: Protein Homology. (559 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)
OLR18226.1single-stranded-DNA-specific exonuclease RecJ; Derived by automated computational analysis using gene prediction method: Protein Homology. (577 aa)
xniFlap endonuclease Xni; Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. (251 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)
OLR17740.1Bifunctional transcriptional regulator/O6-methylguanine-DNA methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (354 aa)
nfoDeoxyribonuclease 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. (285 aa)
OLR17637.1DNA-3-methyladenine glycosylase 2; Derived by automated computational analysis using gene prediction method: Protein Homology. (288 aa)
OLR20889.1methylated-DNA--protein-cysteine methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. (171 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)
OLR20774.1Exodeoxyribonuclease III; Derived by automated computational analysis using gene prediction method: Protein Homology. (268 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)
OLR19322.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (353 aa)
ligADNA ligase (NAD(+)) LigA; 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. (672 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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