ID A0A194Q6J6_PAPXU Unreviewed; 651 AA. AC A0A194Q6J6; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 31-JUL-2019, entry version 11. DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|RuleBase:RU362131}; DE EC=4.2.99.18 {ECO:0000256|RuleBase:RU362131}; GN ORFNames=RR46_05264 {ECO:0000313|EMBL:KPJ00999.1}; OS Papilio xuthus (Asian swallowtail butterfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; OC Papilionoidea; Papilionidae; Papilioninae; Papilio. OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPJ00999.1, ECO:0000313|Proteomes:UP000053268}; RN [1] {ECO:0000313|EMBL:KPJ00999.1, ECO:0000313|Proteomes:UP000053268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPJ00999.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ00999.1}; RX PubMed=26354079; DOI=10.1038/ncomms9212; RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L., RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., RA Jiang X., Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., RA Kronforst M.R., Wang W.; RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in RT butterflies."; RL Nat. Commun. 6:8212-8212(2015). CC -!- CATALYTIC ACTIVITY: CC Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in CC DNA is broken by a beta-elimination reaction, leaving a 3'- CC terminal unsaturated sugar and a product with a terminal 5'- CC phosphate.; EC=4.2.99.18; CC Evidence={ECO:0000256|RuleBase:RU362131}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU362131}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|RuleBase:RU362131}; CC Note=Probably binds two magnesium or manganese ions per subunit. CC {ECO:0000256|RuleBase:RU362131}; CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family. CC {ECO:0000256|RuleBase:RU362131}. 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; KQ459439; KPJ00999.1; -; Genomic_DNA. DR Proteomes; UP000053268; Unassembled WGS sequence. DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. 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 PANTHER; PTHR22748; PTHR22748; 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 Complete proteome {ECO:0000313|Proteomes:UP000053268}; KW DNA damage {ECO:0000256|RuleBase:RU362131}; KW DNA repair {ECO:0000256|RuleBase:RU362131}; KW Lyase {ECO:0000256|RuleBase:RU362131}; KW Magnesium {ECO:0000256|RuleBase:RU362131}; KW Metal-binding {ECO:0000256|RuleBase:RU362131}; KW Reference proteome {ECO:0000313|Proteomes:UP000053268}. FT DOMAIN 394 634 Endo/exonuclease/phosphatase. FT {ECO:0000259|Pfam:PF03372}. FT REGION 1 369 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 8 92 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 112 195 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 203 233 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 243 316 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 331 369 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. SQ SEQUENCE 651 AA; 73106 MW; 863FC8F0ECAD36A3 CRC64; MAPRSAKGKK AADVKVAESA PAKKGRKGKQ VAEPEPTEAE EVKTTVVEKK TKRGKKAKDE EIINGDNEEV CPPAKKSKKK ISEDKAEEQS NGDNSSPEEE PNLDEQNEGG DDESETNGHT EEAKPAGGRG RKKQTKKETV PENKPKETGR GRKNAKQEVQ EDVAKNSEVV EEKPKPSGRG RGKKAQAKPS NDLEEEDKAE SVEEEVKPEP PATKGKKKQN KGSKEKIETD AAMSDQEKEE EDIVEEEPKK KETKSRKNQG KKAQPKEQED KEEDIVEDTQ TTKKRRGAKK DDKSKDSKEE EEVEEKAPEV KPAKGKRGAK NAAAKAAEAE QDIQDTGESN NKRRRKAADD KAGAEDSKKK APAKNKTATK YEDIDFSSDS KTSQGKDWNF KISSWNVDGI RAWMDKGGLE YIQYEKPDIL CLQEIKCSKE KLPEPIKNVP GYHAYWLCSE QDGYAGVGIY TTKLAMNVQY GLQDEELDSE GRIITAEYEQ FYLICTYVPN AGRKLVTLPK RLKWNEEFRK HVKSLDKKKP VIICGDMNVS HNEIDLANPK TNRKNAGFTE EERTGMTELL GDGFVDTYRL LYPDKTSAYT FWTYMFNCRA KNVGWRLDYF IVSERLVTSV CDSIIRDSVY GSDHCPVTLL LHLSSADKPK E //