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END4_ALKCK
ID   END4_ALKCK              Reviewed;         292 AA.
AC   Q5WHC2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Probable endonuclease 4 {ECO:0000255|HAMAP-Rule:MF_00152};
DE            EC=3.1.21.2 {ECO:0000255|HAMAP-Rule:MF_00152};
DE   AltName: Full=Endodeoxyribonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152};
DE   AltName: Full=Endonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152};
GN   Name=nfo {ECO:0000255|HAMAP-Rule:MF_00152}; OrderedLocusNames=ABC1698;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) 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       {ECO:0000255|HAMAP-Rule:MF_00152}.
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   -!- 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}.
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DR   EMBL; AP006627; BAD64233.1; -; Genomic_DNA.
DR   RefSeq; WP_011246542.1; NC_006582.1.
DR   AlphaFoldDB; Q5WHC2; -.
DR   SMR; Q5WHC2; -.
DR   STRING; 66692.ABC1698; -.
DR   PRIDE; Q5WHC2; -.
DR   EnsemblBacteria; BAD64233; BAD64233; ABC1698.
DR   KEGG; bcl:ABC1698; -.
DR   eggNOG; COG0648; Bacteria.
DR   HOGENOM; CLU_025885_4_1_9; -.
DR   OMA; HPGSHLK; -.
DR   OrthoDB; 1088517at2; -.
DR   Proteomes; UP000001168; 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; PS00729; AP_NUCLEASE_F2_1; 1.
DR   PROSITE; PS00730; AP_NUCLEASE_F2_2; 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   Reference proteome; Zinc.
FT   CHAIN           1..292
FT                   /note="Probable endonuclease 4"
FT                   /id="PRO_0000190824"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
SQ   SEQUENCE   292 AA;  32500 MW;  A3B6D828B20495EB CRC64;
     MSLLIGSHVS MSGKKMLLQS SEEAASYGAT TFMIYTGAPQ NTRRKAIEDL NIEAGKAHMA
     EHGLSNIVVH APYIINIGNT QKPETFRLGV DFLRSEIERT EAIGAKQIVL HPGAHVGAGA
     EEGIKKIIEG LNEVLTEKRD VQIALETMAG KGSECGCTFE ELAKIIDGVT HNERLSVCFD
     TCHTHDAGYD IVNDFDGVLD EFDRIIGAER IKVVHINDSK NERSARKDRH ENIGHGHIGL
     KALDYIVHHD QFKDIPKILE TPFIGKDKKD KRPPYKHEIA LLRRELLEPI EK
 
 
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