ID END4_VIBPA Reviewed; 295 AA. AC Q87SC6; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 23-MAY-2003, sequence version 1. DT 10-JUN-2026, entry version 120. 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=VP0498; OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=223926; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIMD 2210633; RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1; RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.; RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism RT distinct from that of V. cholerae."; RL Lancet 361:743-749(2003). 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; Evidence={ECO:0000255|HAMAP- CC 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 --------------------------------------------------------------------------- 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; BA000031; BAC58761.1; -; Genomic_DNA. DR RefSeq; WP_005479588.1; NC_004603.1. DR AlphaFoldDB; Q87SC6; -. DR SMR; Q87SC6; -. DR GeneID; 1187966; -. DR KEGG; vpa:VP0498; -. DR PATRIC; fig|223926.6.peg.475; -. DR eggNOG; COG0648; Bacteria. DR HOGENOM; CLU_025885_0_4_6; -. DR Proteomes; UP000002493; Chromosome 1. 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:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:TreeGrafter. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006284; P:base-excision repair; IEA:TreeGrafter. DR CDD; cd00019; AP2Ec; 1. DR FunFam; 3.20.20.150:FF:000001; Probable endonuclease 4; 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 NCBIfam; NF002199; PRK01060.1-4; 1. DR PANTHER; PTHR21445:SF0; APURINIC-APYRIMIDINIC ENDONUCLEASE; 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; DNA repair; Endonuclease; Hydrolase; Metal-binding; Nuclease; KW Reference proteome; Zinc. FT CHAIN 1..295 FT /note="Probable endonuclease 4" FT /id="PRO_0000190885" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 118 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 154 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 154 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 188 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 225 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 238 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 240 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 270 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" SQ SEQUENCE 295 AA; 33017 MW; 784D0378858E3E0C CRC64; MTNMKNKFGN KLIGAHVSAA GGVDQAPLRA REIGANAFAL FTKNQRQWVA KPLEAKTISA FKANCKMLGF GAEHILPHDS YLINLGAPEA EKLDKSRAAF IDEMERCNQL GLTLLNFHPG SHLKKVSEQE CLATIAESIN LAHKTVPDVV AVIENTAGQG TNLGWKFEHL AEIIEQVEDK DRVGVCIDTC HTFTAGYDLR TKEDCERTFA EFDRIVGMHY LRAMHLNDSK VEFASKVDRH HSLGKGEIGW DCFEYIAKDS RFDGIPLILE TIDPDIWQQE INTLRQFHLA AINNQ //