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Endonuclease III homolog (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)

 A0A1A8Z5T4_9APIC        Unreviewed;       462 AA.
A0A1A8Z5T4;
05-OCT-2016, integrated into UniProtKB/TrEMBL.
05-OCT-2016, sequence version 1.
05-JUL-2017, entry version 7.
RecName: Full=Endonuclease III homolog {ECO:0000256|HAMAP-Rule:MF_03183};
EC=3.2.2.- {ECO:0000256|HAMAP-Rule:MF_03183};
EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_03183};
AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_03183};
Short=DNA glycosylase/AP lyase {ECO:0000256|HAMAP-Rule:MF_03183};
Name=NTH1 {ECO:0000256|HAMAP-Rule:MF_03183};
ORFNames=POVWA1_038330 {ECO:0000313|EMBL:SBT38579.1},
POVWA2_037300 {ECO:0000313|EMBL:SBT39222.1};
Plasmodium ovale wallikeri.
Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
NCBI_TaxID=864142 {ECO:0000313|EMBL:SBT39222.1, ECO:0000313|Proteomes:UP000078550};
[1] {ECO:0000313|EMBL:SBT39222.1, ECO:0000313|Proteomes:UP000078550, ECO:0000313|Proteomes:UP000078555}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Lavstsen T., Jespersen J.S.;
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Bifunctional DNA N-glycosylase with associated
apurinic/apyrimidinic (AP) lyase function that catalyzes the first
step in base excision repair (BER), the primary repair pathway for
the repair of oxidative DNA damage. The DNA N-glycosylase activity
releases the damaged DNA base from DNA by cleaving the N-
glycosidic bond, leaving an AP site. The AP lyase activity cleaves
the phosphodiester bond 3' to the AP site by a beta-elimination.
Primarily recognizes and repairs oxidative base damage of
pyrimidines. {ECO:0000256|HAMAP-Rule:MF_03183}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000256|HAMAP-Rule:MF_03183}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|HAMAP-Rule:MF_03183};
Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play
a role in catalysis, but is probably involved in the proper
positioning of the enzyme along the DNA strand.
{ECO:0000256|HAMAP-Rule:MF_03183};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03183}.
Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03183}.
-!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000256|HAMAP-
Rule:MF_03183}.
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EMBL; FLRD01000108; SBT38579.1; -; Genomic_DNA.
EMBL; FLRE01000144; SBT39222.1; -; Genomic_DNA.
EnsemblProtists; SBT38579; SBT38579; POVWA1_038330.
EnsemblProtists; SBT39222; SBT39222; POVWA2_037300.
Proteomes; UP000078550; Unassembled WGS sequence.
Proteomes; UP000078555; Unassembled WGS sequence.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-HAMAP.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-HAMAP.
GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProtKB-HAMAP.
CDD; cd00056; ENDO3c; 1.
Gene3D; 1.10.1670.10; -; 1.
HAMAP; MF_03183; Endonuclease_III_Nth; 1.
InterPro; IPR011257; DNA_glycosylase.
InterPro; IPR004036; Endonuclease-III-like_CS2.
InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
InterPro; IPR003265; HhH-GPD_domain.
InterPro; IPR000445; HhH_motif.
InterPro; IPR023170; HTH_base_excis_C.
InterPro; IPR030841; NTH1.
Pfam; PF00633; HHH; 1.
Pfam; PF00730; HhH-GPD; 1.
SMART; SM00478; ENDO3c; 1.
SMART; SM00525; FES; 1.
SUPFAM; SSF48150; SSF48150; 1.
PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_03183};
Complete proteome {ECO:0000313|Proteomes:UP000078550};
DNA damage {ECO:0000256|HAMAP-Rule:MF_03183};
DNA repair {ECO:0000256|HAMAP-Rule:MF_03183};
Endonuclease {ECO:0000313|EMBL:SBT39222.1};
Glycosidase {ECO:0000256|HAMAP-Rule:MF_03183};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03183,
ECO:0000313|EMBL:SBT39222.1}; Iron {ECO:0000256|HAMAP-Rule:MF_03183};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03183};
Lyase {ECO:0000256|HAMAP-Rule:MF_03183};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03183};
Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03183};
Nuclease {ECO:0000313|EMBL:SBT39222.1};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03183};
Reference proteome {ECO:0000313|Proteomes:UP000078550}.
DOMAIN 276 424 ENDO3c. {ECO:0000259|SMART:SM00478}.
ACT_SITE 358 358 Nucleophile; for N-glycosylase activity.
{ECO:0000256|HAMAP-Rule:MF_03183}.
METAL 426 426 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_03183}.
METAL 433 433 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_03183}.
METAL 436 436 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_03183}.
METAL 442 442 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_03183}.
SITE 377 377 Important for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_03183}.
SEQUENCE 462 AA; 53277 MW; 3D3FCC942B4A6466 CRC64;
MLVAHPPPAS QCSNTKEPDH VEHSDSPRML TRLMKLLKNF KKAFILNLYF LKMEKQSKYF
NKSLVKKIQI KYEDGLNDSP SSVSRMQAQN AEVNSNHSQN RDTQKSYEQN GCAWKSDVND
GRVKKEKTKE GGKNEGFRLP SGRVKLEQSG EEEEGKKGQV EKQHNDKVHP VKQPNKRRKK
NDYGADRKTF ESERMYKLRD GYDGINGQMG IIKGAQEKSE NNEELKKEHF LLTYNKIKEM
RKEIVAPVDK YGCHMLGERT GDLKTYRFQT LISCLLSSRT KDEVTATVMD KLKKHGLTVE
NILNTPEEEL RKMIYGVGFY NVKAKQILHI CRILKEKYNS DIPNNYDELI KLPGIGEKIA
QLVLQIALNK HEGIAVDIHV HRIANRLNWV YTKDELSTQV KLKNYVQKEL WSELNTLLVG
FGQVICKGKK PICEKCTLTN HCQYYKDSLV RKVKQKKGNG DN


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