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}.
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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
//