END4_THET2
ID END4_THET2 Reviewed; 270 AA.
AC Q72KH8;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Endonuclease 4 {ECO:0000303|PubMed:16782061};
DE EC=3.1.21.2 {ECO:0000255|HAMAP-Rule:MF_00152, ECO:0000269|PubMed:16782061, ECO:0000269|PubMed:20410075};
DE AltName: Full=Endodeoxyribonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152};
DE AltName: Full=Endonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152, ECO:0000303|PubMed:16782061};
DE AltName: Full=TthNfo {ECO:0000303|PubMed:16782061};
GN Name=nfo {ECO:0000255|HAMAP-Rule:MF_00152}; OrderedLocusNames=TT_C0482;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16782061; DOI=10.1016/j.bbrc.2006.05.187;
RA Back J.H., Chung J.H., Park J.H., Han Y.S.;
RT "A versatile endonuclease IV from Thermus thermophilus has uracil-excising
RT and 3'-5' exonuclease activity.";
RL Biochem. Biophys. Res. Commun. 346:889-895(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SHOWS THAT IT HAS NO URACIL-DNA
RP GLYCOSYLASE ACTIVITY.
RX PubMed=20410075; DOI=10.1093/nar/gkq270;
RA Schomacher L., Smolorz S., Ciirdaeva E., Ber S., Kramer W., Fritz H.J.;
RT "Helix-hairpin-helix protein MJ1434 from Methanocaldococcus jannaschii and
RT EndoIV homologue TTC0482 from Thermus thermophilus HB27 do not process DNA
RT uracil residues.";
RL Nucleic Acids Res. 38:5119-5129(2010).
CC -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
CC phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating
CC a 3'-hydroxyl group and a 5'-terminal sugar phosphate (PubMed:16782061,
CC PubMed:20410075). In addition, possesses a 3'-5' exonuclease activity
CC (PubMed:16782061). {ECO:0000269|PubMed:16782061,
CC ECO:0000269|PubMed:20410075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-
CC products.; EC=3.1.21.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00152,
CC ECO:0000269|PubMed:16782061, ECO:0000269|PubMed:20410075};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00152};
CC Note=Binds 3 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_00152};
CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00152}.
CC -!- CAUTION: Back et al. found that TthNfo also catalyzes the excision of
CC uracil from DNA, but further protein analysis by Schomacher et al. show
CC that it does not exhibit DNA uracil glycosylase activity or DNA uridine
CC endonuclease activity. {ECO:0000269|PubMed:16782061,
CC ECO:0000269|PubMed:20410075}.
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DR EMBL; AE017221; AAS80830.1; -; Genomic_DNA.
DR RefSeq; WP_011172928.1; NC_005835.1.
DR AlphaFoldDB; Q72KH8; -.
DR SMR; Q72KH8; -.
DR STRING; 262724.TT_C0482; -.
DR EnsemblBacteria; AAS80830; AAS80830; TT_C0482.
DR KEGG; tth:TT_C0482; -.
DR eggNOG; COG0648; Bacteria.
DR HOGENOM; CLU_025885_0_4_0; -.
DR OMA; NPRGWAT; -.
DR OrthoDB; 1088517at2; -.
DR BRENDA; 3.1.21.2; 2305.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd00019; AP2Ec; 1.
DR HAMAP; MF_00152; Nfo; 1.
DR InterPro; IPR001719; AP_endonuc_2.
DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR PANTHER; PTHR21445; PTHR21445; 1.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SMART; SM00518; AP2Ec; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR00587; nfo; 1.
DR PROSITE; PS00731; AP_NUCLEASE_F2_3; 1.
DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Zinc.
FT CHAIN 1..270
FT /note="Endonuclease 4"
FT /id="PRO_0000190882"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
SQ SEQUENCE 270 AA; 29051 MW; 2463AD224FA24CD2 CRC64;
MPRYGFHLSI AGKKGVAGAV EEATALGLTA FQIFAKSPRS WRPRALSPAE VEAFRALREA
SGGLPAVIHA SYLVNLGAEG ELWEKSVASL ADDLEKAALL GVEYVVVHPG SGRPERVKEG
ALKALRLAGV RSRPVLLVEN TAGGGEKVGA RFEELAWLVA DTPLQVCLDT CHAYAAGYDV
AEDPLGVLDA LDRAVGLERV PVVHLNDSVG GLGSRVDHHA HLLQGKIGEG LKRVFLDPRL
KDRVFILETP RGPEEDAWNL RVLRAWLEEA
