ID A0A931CPX1_9BACT Unreviewed; 280 AA. AC A0A931CPX1; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 02-OCT-2024, entry version 9. 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 ECO:0000313|EMBL:MBG0779022.1}; GN ORFNames=H0S81_03755 {ECO:0000313|EMBL:MBG0779022.1}; OS Desulfotignum balticum. OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfotignum. OX NCBI_TaxID=115781 {ECO:0000313|EMBL:MBG0779022.1, ECO:0000313|Proteomes:UP000706172}; RN [1] {ECO:0000313|EMBL:MBG0779022.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIC098Bin6 {ECO:0000313|EMBL:MBG0779022.1}; RA Lahme S., Mand J., Longwell J., Smith R., Enning D.; RT "Severe corrosion of carbon steel in oil field produced water can be linked RT to methanogenic archaea containing a special type of NiFe hydrogenase."; RL Submitted (JUL-2020) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBG0779022.1}. 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; JACCQK010000177; MBG0779022.1; -; Genomic_DNA. DR Proteomes; UP000706172; Unassembled WGS sequence. 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 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; 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 {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..276 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 280 AA; 31280 MW; 2E351899FF9A4DFD CRC64; MKYIGAHVSI SGGVENAPVN AAKIGAKAFA MFTRNQRRWS SLPLTEKNIS GFRERCRQHE FDSTVILPHD SYLINLGHPD PAGLDKSRSA FFEEMGRCEQ LGLTYLNFHP GSHLNKLSPE HCLDRIAQSI NLALDRTTGV TAVIENTAGQ GTNLGYGFDH LARIIEQVTD KTRVGVCLDT CHLHGAGYDI RTAAAFEKTM DEFDRIVGMG FLKALHLNDS KKDFNSRVDR HASIGKGELG MTPFEFIMND ARFDNMPLVL ETPDDSLWEA EIRRLYDLIP //