ID A0A0P0QGT0_SERMA Unreviewed; 279 AA. AC A0A0P0QGT0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 31-JUL-2019, entry version 20. 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}, B7L62_04685 GN {ECO:0000313|EMBL:RZF20054.1}; OS Serratia marcescens. OC Bacteria; Proteobacteria; 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. RN [2] {ECO:0000313|EMBL:ALL39061.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B3R3 {ECO:0000313|EMBL:ALL39061.1}; RA Peterson S.W.; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:RZF20054.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RPH1 {ECO:0000313|EMBL:RZF20054.1}; RA Penna P.A.; RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:RZF20054.1, ECO:0000313|Proteomes:UP000291786} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RPH1 {ECO:0000313|EMBL:RZF20054.1, RC ECO:0000313|Proteomes:UP000291786}; RX PubMed=30733713; RA da Mota F.F., Castro D.P., Vieira C.S., Gumiel M., RA de Albuquerque J.P., Carels N., Azambuja P.; RT "In vitro Trypanocidal Activity, Genomic Analysis of Isolates, and in RT vivo Transcription of Type VI Secretion System of Serratia marcescens RT Belonging to the Microbiota of Rhodnius prolixus Digestive Tract."; RL Front. Microbiol. 9:0-3205(2019). 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: CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide CC end-products.; EC=3.1.21.2; Evidence={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, ECO:0000256|SAAS:SAAS01083619}. 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 EMBL; NCQI01000001; RZF20054.1; -; Genomic_DNA. DR RefSeq; WP_033632566.1; NZ_NERL01000047.1. DR EnsemblBacteria; ALL39061; ALL39061; AR325_19550. DR PATRIC; fig|615.364.peg.3460; -. DR OrthoDB; 1088517at2; -. DR Proteomes; UP000058492; Chromosome. DR Proteomes; UP000291786; 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: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; 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 Complete proteome {ECO:0000313|Proteomes:UP000058492, KW ECO:0000313|Proteomes:UP000291786}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS01083620}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS01083629}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS01083624}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS01083627}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS01083611}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_00152, KW ECO:0000256|SAAS:SAAS01083625}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083609}. FT DOMAIN 20 239 AP_endonuc_2. {ECO:0000259|Pfam:PF01261}. 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 //