ID A0A0P0QGT0_SERMA Unreviewed; 279 AA. AC A0A0P0QGT0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 08-NOV-2023, entry version 36. DE RecName: Full=Probable endonuclease 4 {ECO:0000256|HAMAP-Rule:MF_00152}; DE EC=3.1.21.2 {ECO:0000256|HAMAP-Rule:MF_00152}; DE AltName: Full=Endodeoxyribonuclease IV {ECO:0000256|HAMAP-Rule:MF_00152}; DE AltName: Full=Endonuclease IV {ECO:0000256|HAMAP-Rule:MF_00152}; GN Name=nfo {ECO:0000256|HAMAP-Rule:MF_00152}; GN ORFNames=AR325_19550 {ECO:0000313|EMBL:ALL39061.1}; OS Serratia marcescens. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=615 {ECO:0000313|EMBL:ALL39061.1, ECO:0000313|Proteomes:UP000058492}; RN [1] {ECO:0000313|Proteomes:UP000058492} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B3R3 {ECO:0000313|Proteomes:UP000058492}; RA Gilbert D.G.; RL Submitted (OCT-2015) 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:0000256|HAMAP-Rule:MF_00152}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end- CC products.; EC=3.1.21.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00152}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00152}; CC Note=Binds 3 Zn(2+) ions. {ECO:0000256|HAMAP-Rule:MF_00152}; CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family. CC {ECO:0000256|ARBA:ARBA00005340, ECO:0000256|HAMAP-Rule:MF_00152}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP013046; ALL39061.1; -; Genomic_DNA. DR RefSeq; WP_033632566.1; NZ_VBRJ01000010.1. DR AlphaFoldDB; A0A0P0QGT0; -. DR STRING; 273526.SMDB11_2556; -. DR EnsemblBacteria; ALL39061; ALL39061; AR325_19550. DR PATRIC; fig|615.364.peg.3460; -. DR OrthoDB; 9805666at2; -. DR Proteomes; UP000058492; Chromosome. DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt. 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 Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 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 NCBIfam; TIGR00587; nfo; 1. DR PANTHER; PTHR21445:SF0; AP_ENDONUC_2 DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR21445; ENDONUCLEASE IV ENDODEOXYRIBONUCLEASE IV; 1. DR Pfam; PF01261; AP_endonuc_2; 1. DR SMART; SM00518; AP2Ec; 1. DR SUPFAM; SSF51658; Xylose isomerase-like; 1. DR PROSITE; PS00729; AP_NUCLEASE_F2_1; 1. DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 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 {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_00152}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_00152}; Endonuclease {ECO:0000256|HAMAP-Rule:MF_00152}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00152}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00152}; Nuclease {ECO:0000256|HAMAP-Rule:MF_00152}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00152}. FT DOMAIN 20..277 FT /note="Xylose isomerase-like TIM barrel" FT /evidence="ECO:0000259|Pfam:PF01261" FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152" FT BINDING 109 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152" FT BINDING 179 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152" FT BINDING 182 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152" FT BINDING 216 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152" FT BINDING 229 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152" FT BINDING 261 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152" SQ SEQUENCE 279 AA; 30761 MW; 69EF82266FD157FF CRC64; MKFVGAHVSA SGGVDQAVIR AHELEATAFA LFTKNQRQWK AAPLAADVID KFKSACAQYG FGPGQILPHD SYLINLGHPV AEALEKSREA FIDELQRCEQ LGLTLLNFHP GSHLLQIDED KCLARIAESI NIALDKTAGV TAVIENTAGQ GSNLGFKFEH LAAIIDGVED KSRVGVCIDT CHAFAAGYDL RTEETCEHTF KQLGDIVGFN YLRGMHLNDA KSEFNSRVDR HHSLGEGNIG KTVFSYIMRD PRFDNIPLIL ETVNPDIWAE EIAWLKAQQ //