ID A0A194Q6J6_PAPXU Unreviewed; 651 AA. AC A0A194Q6J6; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 27-NOV-2024, entry version 24. DE RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease {ECO:0000256|RuleBase:RU362131}; DE EC=3.1.-.- {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; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea; OC 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., Jiang X., RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R., RA Wang W.; RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies."; RL Nat. Commun. 6:8212-8212(2015). CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield CC nucleoside 5'-phosphates.; EC=3.1.11.2; CC Evidence={ECO:0000256|ARBA:ARBA00000493}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2, CC ECO:0000256|RuleBase:RU362131}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2, CC ECO:0000256|RuleBase:RU362131}; CC Note=Probably binds two magnesium or manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR604808-2, ECO:0000256|RuleBase:RU362131}; CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family. CC {ECO:0000256|ARBA:ARBA00007092, 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 AlphaFoldDB; A0A194Q6J6; -. DR STRING; 66420.A0A194Q6J6; -. DR Proteomes; UP000053268; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:TreeGrafter. DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:TreeGrafter. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:TreeGrafter. DR GO; GO:0006284; P:base-excision repair; IEA:TreeGrafter. DR CDD; cd09087; Ape1-like_AP-endo; 1. DR FunFam; 3.60.10.10:FF:000009; DNA-(apurinic or apyrimidinic site) lyase; 1. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 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 NCBIfam; TIGR00195; exoDNase_III; 1. DR NCBIfam; TIGR00633; xth; 1. DR PANTHER; PTHR22748; AP ENDONUCLEASE; 1. DR PANTHER; PTHR22748:SF6; DNA-(APURINIC OR APYRIMIDINIC SITE) ENDONUCLEASE; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR SUPFAM; SSF56219; DNase I-like; 1. DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1. DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1. PE 3: Inferred from homology; KW DNA damage {ECO:0000256|RuleBase:RU362131}; KW DNA repair {ECO:0000256|RuleBase:RU362131}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604808-2}; KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2, KW ECO:0000256|RuleBase:RU362131}; KW Reference proteome {ECO:0000313|Proteomes:UP000053268}. FT DOMAIN 394..634 FT /note="Endonuclease/exonuclease/phosphatase" FT /evidence="ECO:0000259|Pfam:PF03372" FT REGION 1..369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 8..92 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 112..195 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 203..233 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..316 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 331..369 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 497 FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 536 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 634 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT BINDING 396 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 424 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 536 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 538 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 633 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 634 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT SITE 538 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 608 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 634 FT /note="Interaction with DNA substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" 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 //