ID   A0A194Q6J6_PAPXU        Unreviewed;       651 AA.
AC   A0A194Q6J6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   05-JUN-2019, entry version 10.
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}.
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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|MobiDB-lite:
FT                                A0A194Q6J6}.
FT   COMPBIAS      8     92       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A194Q6J6}.
FT   COMPBIAS    112    195       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A194Q6J6}.
FT   COMPBIAS    203    233       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A194Q6J6}.
FT   COMPBIAS    243    316       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A194Q6J6}.
FT   COMPBIAS    331    369       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A194Q6J6}.
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
//