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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)

 G0V2A4_TRYCI            Unreviewed;       259 AA.
G0V2A4;
19-OCT-2011, integrated into UniProtKB/TrEMBL.
19-OCT-2011, sequence version 1.
05-DEC-2018, entry version 29.
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=TCIL3000_11_12720 {ECO:0000313|EMBL:CCC95776.1};
Trypanosoma congolense (strain IL3000).
Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma;
Nannomonas.
NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC95776.1};
[1] {ECO:0000313|EMBL:CCC95776.1}
NUCLEOTIDE SEQUENCE.
STRAIN=IL3000 {ECO:0000313|EMBL:CCC95776.1};
PubMed=22331916; DOI=10.1073/pnas.1117313109;
Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H.,
Gamble J., Gilderthorp R., Marcello L., McQuillan J., Otto T.D.,
Quail M.A., Sanders M.J., van Tonder A., Ginger M.L., Field M.C.,
Barry J.D., Hertz-Fowler C., Berriman M.;
"Antigenic diversity is generated by distinct evolutionary mechanisms
in African trypanosome species.";
Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
-!- 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:
Reaction=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.; EC=4.2.99.18; Evidence={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; HE575324; CCC95776.1; -; Genomic_DNA.
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-UniRule.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProtKB-UniRule.
CDD; cd00056; ENDO3c; 1.
Gene3D; 1.10.1670.10; -; 1.
HAMAP; MF_03183; Endonuclease_III_Nth; 1.
InterPro; IPR011257; DNA_glycosylase.
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.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_03183};
DNA damage {ECO:0000256|HAMAP-Rule:MF_03183};
DNA repair {ECO:0000256|HAMAP-Rule:MF_03183};
Glycosidase {ECO:0000256|HAMAP-Rule:MF_03183};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03183};
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};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03183}.
DOMAIN 57 207 ENDO3c. {ECO:0000259|SMART:SM00478}.
ACT_SITE 139 139 Nucleophile; for N-glycosylase activity.
{ECO:0000256|HAMAP-Rule:MF_03183}.
METAL 209 209 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_03183}.
METAL 216 216 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_03183}.
METAL 219 219 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_03183}.
METAL 225 225 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_03183}.
SITE 158 158 Important for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_03183}.
SEQUENCE 259 AA; 29105 MW; BBAD58FB84FC4B70 CRC64;
MSKTFKPPPN WNKLYTKVKE IREEIVAPVD TVGCSKLFGK NVSNEIRRYH ILLALMLSAQ
TKDHVTAAAM FSLIEHGCTP EMIFNMPEVK LNEHISKVGF HNTKAKHIKA ATRFIVERHN
GMVPRSYEDL VGLPGVGPKM AHLFLQEADG VILGIGVDTH VHRIAQRFRW VPSTVKGPED
TRKALESWLP RVYWGEINGL LVGLGQTICT PRLPQCSECG ANKLCPSAFR EARRGTKRQK
SPELEDLAPA ELPKQRKRA


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