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 27-JUL-2011, entry version 24. DE RecName: Full=Probable endonuclease 4; DE EC=3.1.21.2; DE AltName: Full=Endodeoxyribonuclease IV; DE AltName: Full=Endonuclease IV; GN Name=nfo; OrderedLocusNames=Amuc_0845; OS Akkermansia muciniphila (strain ATCC BAA-835). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., RA de Vos W.M., Richardson P.; RT "Complete sequence of Akkermansia muciniphila ATCC BAA-835."; RL Submitted (MAY-2008) 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 (By similarity). CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphooligonucleotide end-products. CC -!- COFACTOR: Binds 3 zinc ions (By similarity). CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family. 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; YP_001877459.1; NC_010655.1. DR ProteinModelPortal; B2UQE3; -. DR SMR; B2UQE3; 3-276. DR STRING; B2UQE3; -. DR GeneID; 6274324; -. DR GenomeReviews; CP001071_GR; Amuc_0845. DR KEGG; amu:Amuc_0845; -. DR HOGENOM; HBG565018; -. DR OMA; QIALETM; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:EC. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR HAMAP; MF_00152; Nfo; 1; -. DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS. DR InterPro; IPR001719; Endodeoxyribonuclease_IV. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR InterPro; IPR012307; Xyl_isomerase_TIM-brl. DR Gene3D; G3DSA:3.20.20.150; Xyl_isomerase-like_TIM-brl; 1. DR PANTHER; PTHR21445; AP_endnuclease2; 1. DR Pfam; PF01261; AP_endonuc_2; 1. DR SMART; SM00518; AP2Ec; 1. DR SUPFAM; SSF51658; Xyl_isomerase-like_TIM-brl; 1. DR TIGRFAMs; TIGR00587; Nfo; 1. DR PROSITE; PS00729; AP_NUCLEASE_F2_1; FALSE_NEG. DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1. DR PROSITE; PS00731; AP_NUCLEASE_F2_3; FALSE_NEG. 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; Zinc. FT CHAIN 1 277 Probable endonuclease 4. FT /FTId=PRO_1000096867. FT METAL 67 67 Zinc 1 (By similarity). FT METAL 107 107 Zinc 1 (By similarity). FT METAL 142 142 Zinc 1 (By similarity). FT METAL 142 142 Zinc 2 (By similarity). FT METAL 176 176 Zinc 2 (By similarity). FT METAL 179 179 Zinc 3 (By similarity). FT METAL 211 211 Zinc 2 (By similarity). FT METAL 224 224 Zinc 3 (By similarity). FT METAL 226 226 Zinc 3 (By similarity). FT METAL 256 256 Zinc 2 (By similarity). 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 //