ID END4_AKKM8 Reviewed; 277 AA. AC B2UQE3; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 16-JAN-2019, entry version 67. 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}; GN OrderedLocusNames=Amuc_0845; OS Akkermansia muciniphila (strain ATCC BAA-835 / Muc). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Akkermansiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835 / Muc; RX PubMed=21390229; DOI=10.1371/journal.pone.0016876; RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M., RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.; RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin RT degrader, and its use in exploring intestinal metagenomes."; RL PLoS ONE 6:E16876-E16876(2011). 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:0000255|HAMAP-Rule:MF_00152}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide CC end-products.; EC=3.1.21.2; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00152}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-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; CP001071; ACD04678.1; -; Genomic_DNA. DR RefSeq; WP_012419893.1; NC_010655.1. DR ProteinModelPortal; B2UQE3; -. DR SMR; B2UQE3; -. DR STRING; 349741.Amuc_0845; -. DR EnsemblBacteria; ACD04678; ACD04678; Amuc_0845. DR GeneID; 34173734; -. DR KEGG; amu:Amuc_0845; -. DR eggNOG; ENOG4105EFU; Bacteria. DR eggNOG; COG0648; LUCA. DR HOGENOM; HOG000224895; -. DR KO; K01151; -. DR OMA; HPGSHLK; -. DR OrthoDB; 1088517at2; -. DR BioCyc; AMUC349741:G1GBX-916-MONOMER; -. DR Proteomes; UP000001031; Chromosome. 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; PS00730; AP_NUCLEASE_F2_2; 1. DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; Endonuclease; Hydrolase; KW Metal-binding; Nuclease; Reference proteome; Zinc. FT CHAIN 1 277 Probable endonuclease 4. FT /FTId=PRO_1000096867. FT METAL 67 67 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 107 107 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 142 142 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 142 142 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 176 176 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 179 179 Zinc 3. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 211 211 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 224 224 Zinc 3. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 226 226 Zinc 3. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 256 256 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. SQ SEQUENCE 277 AA; 30780 MW; 0AB7EB291259D263 CRC64; MPYIGCHLSS AKGYEAMGRV ALSIGANTFQ FFTRNPRGSK AKAIDEQDIA RFLELARNNG FGTLLAHAPY TLNPCSADPS VARFAAQVLK EDLELMEHLP GNLYNFHPGC HVGQGVEKGI ELVADQLNDV LSPEQKTIVL LETMSGKGSE VGRTFEELAA IMERVDLKDK LGVCLDTCHV YSAGYDIVNR LDSVLEHFDA VLGLERLRAI HLNDSMTPFS SFKDRHETIG KGSLGEQAFI NIINHPVLRE LPFFLETPRD DAGHGEEITW LKEHYRN //