ID A0A0G4BXC2_NEIME Unreviewed; 256 AA. AC A0A0G4BXC2; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 03-AUG-2022, entry version 19. DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:AKM92108.1}; DE EC=3.1.11.2 {ECO:0000313|EMBL:AKM92108.1}; GN Name=xthA {ECO:0000313|EMBL:AKM92108.1}; GN ORFNames=M0579_00594 {ECO:0000313|EMBL:AKM92108.1}; OS Neisseria meningitidis M0579. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=935590 {ECO:0000313|EMBL:AKM92108.1, ECO:0000313|Proteomes:UP000035660}; RN [1] {ECO:0000313|EMBL:AKM92108.1, ECO:0000313|Proteomes:UP000035660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M0579 {ECO:0000313|EMBL:AKM92108.1, RC ECO:0000313|Proteomes:UP000035660}; RX PubMed=25845594; DOI=10.1093/nar/gkv219; RA Seib K.L., Jen F.E., Tan A., Scott A.L., Kumar R., Power P.M., Chen L.T., RA Wu H.J., Wang A.H., Hill D.M., Luyten Y.A., Morgan R.D., Roberts R.J., RA Maiden M.C., Boitano M., Clark T.A., Korlach J., Rao D.N., Jennings M.P.; RT "Specificity of the ModA11, ModA12 and ModD1 epigenetic regulator N6- RT adenine DNA methyltransferases of Neisseria meningitidis."; RL Nucleic Acids Res. 43:4150-4162(2015). CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family. CC {ECO:0000256|ARBA:ARBA00007092}. 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; CP007668; AKM92108.1; -; Genomic_DNA. DR RefSeq; WP_002218768.1; NZ_CP007668.1. DR EnsemblBacteria; AKM92108; AKM92108; M0579_00594. DR PATRIC; fig|935590.3.peg.479; -. DR Proteomes; UP000035660; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR CDD; cd09086; ExoIII-like_AP-endo; 1. DR Gene3D; 3.60.10.10; -; 1. DR InterPro; IPR004808; AP_endonuc_1. DR InterPro; IPR020847; AP_endonuclease_F1_BS. DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR InterPro; IPR037493; ExoIII-like. DR PANTHER; PTHR43250; PTHR43250; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR SUPFAM; SSF56219; SSF56219; 1. DR TIGRFAMs; TIGR00633; xth; 1. DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1. DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000313|EMBL:AKM92108.1}. FT DOMAIN 5..247 FT /note="Endo/exonuclease/phosphatase" FT /evidence="ECO:0000259|Pfam:PF03372" SQ SEQUENCE 256 AA; 29117 MW; 3BBA2AD467FBADAB CRC64; MKITTWNVNS LNVRLPQVQN LLADNPPDIL VLQELKLDQD KFPAAALQMM GWHCVWSGQK TYNGVAIVSR NAPEDVHIGL PALPDDPQRR VIAATVGGVR VINVYCVNGE ALDSPKFKYK EQWFAALTEF VRDEMTRYGK LVLLGDFNIA PADADCYDPE KWHEKIHCSS VERQWFKNLL DLGLTDSLRQ VHPEGAFYTW FDYRGAMFQR KLGLRIDHIL VSPAMAAALK DVRVDLETRA LERPSDHAPV TAEFDW //