NTH_BOVIN
ID NTH_BOVIN Reviewed; 305 AA.
AC Q2KID2; M5FK15;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Endonuclease III-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03183};
DE EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03183};
DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_03183};
DE AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_03183};
DE Short=DNA glycosylase/AP lyase {ECO:0000255|HAMAP-Rule:MF_03183};
DE Flags: Precursor;
GN Name=NTHL1 {ECO:0000255|HAMAP-Rule:MF_03183};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136};
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional DNA N-glycosylase with associated
CC apurinic/apyrimidinic (AP) lyase function that catalyzes the first step
CC in base excision repair (BER), the primary repair pathway for the
CC repair of oxidative DNA damage. The DNA N-glycosylase activity releases
CC the damaged DNA base from DNA by cleaving the N-glycosidic bond,
CC leaving an AP site. The AP lyase activity cleaves the phosphodiester
CC bond 3' to the AP site by a beta-elimination. Primarily recognizes and
CC repairs oxidative base damage of pyrimidines. {ECO:0000255|HAMAP-
CC Rule:MF_03183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03183};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03183};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a
CC role in catalysis, but is probably involved in the proper positioning
CC of the enzyme along the DNA strand. {ECO:0000255|HAMAP-Rule:MF_03183};
CC -!- SUBUNIT: Interacts with YBX1 (By similarity). Interacts with ERCC5/XPG;
CC the interaction stimulates NTHL1 activity and NTHL1 binding to its DNA
CC substrate (By similarity). {ECO:0000250|UniProtKB:P78549,
CC ECO:0000255|HAMAP-Rule:MF_03183}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183}.
CC Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183}.
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP-
CC Rule:MF_03183}.
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DR EMBL; GJ062847; DAA15605.1; -; Genomic_DNA.
DR EMBL; BC112681; AAI12682.1; -; mRNA.
DR RefSeq; NP_001039862.1; NM_001046397.2.
DR AlphaFoldDB; Q2KID2; -.
DR SMR; Q2KID2; -.
DR STRING; 9913.ENSBTAP00000046623; -.
DR PaxDb; Q2KID2; -.
DR PRIDE; Q2KID2; -.
DR Ensembl; ENSBTAT00000049780; ENSBTAP00000046623; ENSBTAG00000006272.
DR GeneID; 535203; -.
DR KEGG; bta:535203; -.
DR CTD; 4913; -.
DR VEuPathDB; HostDB:ENSBTAG00000006272; -.
DR VGNC; VGNC:32301; NTHL1.
DR eggNOG; KOG1921; Eukaryota.
DR GeneTree; ENSGT00510000047513; -.
DR HOGENOM; CLU_012862_4_2_1; -.
DR InParanoid; Q2KID2; -.
DR OrthoDB; 1322642at2759; -.
DR TreeFam; TF314967; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Proteomes; UP000321980; Chromosome 25.
DR Bgee; ENSBTAG00000006272; Expressed in isthmus of fallopian tube and 105 other tissues.
DR ExpressionAtlas; Q2KID2; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; -; 1.
DR HAMAP; MF_03183; Endonuclease_III_Nth; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR030841; NTH1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00525; FES; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur;
KW Lyase; Metal-binding; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT CHAIN 29..305
FT /note="Endonuclease III-like protein 1"
FT /id="PRO_0000244406"
FT DOMAIN 192..216
FT /note="HhH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="Nucleophile; for N-glycosylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT BINDING 283
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT BINDING 290
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT BINDING 293
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT BINDING 299
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT SITE 232
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78549"
SQ SEQUENCE 305 AA; 33645 MW; 9318553C857F500C CRC64;
MNAAGVRMVV TRARSRGTGA SLRRRGEKAA PLRSGEAAAE ERKSYSPVKR RRKAQRLSVA
YEASEGEGGE GAEHLQAPSW QPQDWRQQLD NIRTMRSGKD APVDQLGAEH CFDPSASPKV
RRYQVLLSLM LSSQTKDQVT AGAMQRLRAR GLTVDSILQT DDSTLGALIY PVGFWRSKVK
YIKQTSAILQ QRYDGDIPAS VAELVALPGV GPKMAHLAMA VAWGTVSGIA VDTHVHRIAN
RLRWTKKATK SPEETRRALE EWLPRELWSE INGLLVGFGQ QTCLPIRPRC QACLNRALCP
AARGL
