ID   END4_THENE              Reviewed;         108 AA.
AC   O86954;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Probable endonuclease 4;
DE            EC=3.1.21.2;
DE   AltName: Full=Endodeoxyribonuclease IV;
DE   AltName: Full=Endonuclease IV;
DE   Flags: Fragment;
GN   Name=nfo;
OS   Thermotoga neapolitana.
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=2337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Z2706-MC24;
RA   Zverlov V.V., Mashchenko O.V., Liebl W., Velikodvorskaya G.A.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-
CC         products.; EC=3.1.21.2; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00763};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00763};
CC       Note=Binds 3 Zn(2+) ions. {ECO:0000255|PROSITE-ProRule:PRU00763};
CC   -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00763}.
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DR   EMBL; AJ009831; CAA08862.1; -; Genomic_DNA.
DR   AlphaFoldDB; O86954; -.
DR   SMR; O86954; -.
DR   GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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   SUPFAM; SSF51658; SSF51658; 1.
DR   PROSITE; PS00731; AP_NUCLEASE_F2_3; 1.
DR   PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Zinc.
FT   CHAIN           <1..108
FT                   /note="Probable endonuclease 4"
FT                   /id="PRO_0000190881"
FT   BINDING         2
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT   NON_TER         1
SQ   SEQUENCE   108 AA;  12331 MW;  B0EB000F958264C2 CRC64;
     CHGFDSGYDI TKKEGVESLL SEIENLFGLE RLKMIHLNDS KYPLGAAKDR HERIGSGFIG
     EAGFAVFFSF KEVQRIPWIL ETPGGNEEHA EDIKKVFEII EKYRIEVD