Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for O35980

Entry ID Method Resolution Chain Position Source
AF-O35980-F1 Predicted AlphaFoldDB

19 variants for O35980

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389444701 18 I>V No EVA
rs3389420211 21 E>* No EVA
rs864258469 35 E>A No EVA
rs233047438 43 V>M No EVA
rs250656719 48 R>K No EVA
rs3389439726 49 T>P No EVA
rs47475127 52 T>M No EVA
rs46089833 112 S>P No EVA
rs3389434074 128 S>I No EVA
rs3389420169 145 R>P No EVA
rs3389402009 150 E>D No EVA
rs241042012 182 A>T No EVA
rs258523289 197 A>T No EVA
rs3389389068 226 V>M No EVA
rs3389420136 228 T>I No EVA
rs3389450996 229 H>L No EVA
rs226439237 243 M>V No EVA
rs213256357 292 A>T No EVA
rs3389409267 293 L>Q No EVA

No associated diseases with O35980

4 regional properties for O35980

Type Name Position InterPro Accession
conserved_site Helix-hairpin-helix motif 187 - 211 IPR000445
domain HhH-GPD domain 118 - 276 IPR003265
conserved_site Endonuclease III-like, iron-sulphur cluster loop motif 277 - 297 IPR003651
conserved_site Endonuclease III-like, conserved site-2 190 - 219 IPR004036

Functions

Description
EC Number 4.2.99.18 Other carbon-oxygen lyases
Subcellular Localization
  • Nucleus
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

8 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
class I DNA-(apurinic or apyrimidinic site) endonuclease activity Catalysis of the cleavage of an AP site 3' of the baseless site by a beta-lyase mechanism, leaving an unsaturated aldehyde, termed a 3'-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5'-phosphate.
damaged DNA binding Binding to damaged DNA.
DNA N-glycosylase activity Catalysis of the removal of damaged bases by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apurinic/apyrimidinic (AP) site.
DNA-(apurinic or apyrimidinic site) endonuclease activity Catalysis of the cleavage of the C-O-P bond in the AP site created when DNA glycosylase removes a damaged base, involved in the DNA base excision repair pathway (BER).
double-stranded DNA binding Binding to double-stranded DNA.
metal ion binding Binding to a metal ion.
oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity Catalysis of the removal oxidized pyrimidine bases by cleaving the N-C1' glycosidic bond between the oxidized pyrimidine and the deoxyribose sugar. The reaction involves formation of a covalent enzyme-pyrimidine base intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apyrimidinic (AP) site.

4 GO annotations of biological process

Name Definition
base-excision repair, AP site formation The formation of an AP site, a deoxyribose sugar with a missing base, by DNA glycosylase which recognizes an altered base in DNA and catalyzes its hydrolytic removal. This sugar phosphate is the substrate recognized by the AP endonuclease, which cuts the DNA phosphodiester backbone at the 5' side of the altered site to leave a gap which is subsequently repaired.
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
nucleotide-excision repair A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
nucleotide-excision repair, DNA incision, 5'-to lesion The endonucleolytic cleavage of the damaged strand of DNA 5' to the site of damage. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The incision follows the incision formed 3' to the site of damage.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P31378 NTG1 Endonuclease III homolog 1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P78549 NTHL1 Endonuclease III-like protein 1 Homo sapiens (Human) PR
10 20 30 40 50 60
MNSGVRMVTR SRSRATRIAS EGCREELAPR EAAAEGRKSH RPVRHPRRTQ KTHVAYEAAN
70 80 90 100 110 120
GEEGEDAEPL KVPVWEPQNW QQQLANIRIM RSKKDAPVDQ LGAEHCYDAS ASPKVRRYQV
130 140 150 160 170 180
LLSLMLSSQT KDQVTAGAMQ RLRARGLTVE SILQTDDDTL GRLIYPVGFW RNKVKYIKQT
190 200 210 220 230 240
TAILQQRYEG DIPASVAELV ALPGVGPKMA HLAMAVAWGT ISGIAVDTHV HRIANRLRWT
250 260 270 280 290
KKMTKTPEET RKNLEEWLPR VLWSEVNGLL VGFGQQICLP VHPRCQACLN KALCPAAQDL