ID A0A0P0QGT0_SERMA Unreviewed; 279 AA. AC A0A0P0QGT0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 17-FEB-2016, entry version 2. 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; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=615 {ECO:0000313|EMBL:ALL39061.1}; RN [1] {ECO:0000313|EMBL:ALL39061.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B3R3 {ECO:0000313|EMBL:ALL39061.1}; RA Millard Andrew; 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 sites (AP sites) CC to produce new 5'-ends that are base-free deoxyribose 5-phosphate CC residues. It preferentially attacks modified AP sites created by CC bleomycin and neocarzinostatin. {ECO:0000256|HAMAP-Rule:MF_00152}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphooligonucleotide end-products. {ECO:0000256|HAMAP- CC Rule:MF_00152}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC 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|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 Gene3D; 3.20.20.150; -; 1. DR HAMAP; MF_00152; Nfo; 1. DR InterPro; IPR001719; AP_endonuc_2. DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS. 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; PS00731; AP_NUCLEASE_F2_3; 1. DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS00474492}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS00474504}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS00474513, ECO:0000313|EMBL:ALL39061.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS00474508, ECO:0000313|EMBL:ALL39061.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS00474496}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS00474499}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS00474512}. FT COILED 81 101 {ECO:0000256|SAM:Coils}. FT METAL 69 69 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_00152}. FT METAL 109 109 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_00152}. FT METAL 145 145 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_00152}. FT METAL 145 145 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00152}. FT METAL 179 179 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00152}. FT METAL 182 182 Zinc 3. {ECO:0000256|HAMAP-Rule: FT MF_00152}. FT METAL 216 216 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00152}. FT METAL 229 229 Zinc 3. {ECO:0000256|HAMAP-Rule: FT MF_00152}. FT METAL 231 231 Zinc 3. {ECO:0000256|HAMAP-Rule: FT MF_00152}. FT METAL 261 261 Zinc 2. {ECO:0000256|HAMAP-Rule: FT 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 //