ID   C3YZ80_BRAFL            Unreviewed;       894 AA.
AC   C3YZ80;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=BRAFLDRAFT_82922 {ECO:0000313|EMBL:EEN54151.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN54151.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54151.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN54151.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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DR   EMBL; GG666566; EEN54151.1; -; Genomic_DNA.
DR   RefSeq; XP_002598139.1; XM_002598093.1.
DR   AlphaFoldDB; C3YZ80; -.
DR   STRING; 7739.C3YZ80; -.
DR   eggNOG; KOG1304; Eukaryota.
DR   InParanoid; C3YZ80; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019104; F:DNA N-glycosylase activity; IBA:GO_Central.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR   CDD; cd08969; MeNeil3_N; 1.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 3.20.190.10; MutM-like, N-terminal; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 2.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   InterPro; IPR035937; MutM-like_N-ter.
DR   InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010666; Znf_GRF.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR22993:SF10; ENDONUCLEASE 8-LIKE 3; 1.
DR   PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
DR   Pfam; PF01490; Aa_trans; 2.
DR   Pfam; PF06839; zf-GRF; 1.
DR   Pfam; PF00641; zf-RanBP; 2.
DR   SMART; SM00547; ZnF_RBZ; 2.
DR   SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
DR   SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
DR   PROSITE; PS51999; ZF_GRF; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 2.
DR   PROSITE; PS50199; ZF_RANBP2_2; 2.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00322}.
FT   TRANSMEM        576..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        602..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        712..731
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        743..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        784..808
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        820..841
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        847..867
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          224..258
FT                   /note="FPG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51066"
FT   DOMAIN          288..319
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          324..355
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          494..536
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   REGION          25..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         894
FT                   /evidence="ECO:0000313|EMBL:EEN54151.1"
SQ   SEQUENCE   894 AA;  99118 MW;  B17D959C0E9CA6F2 CRC64;
     MVEGPGCKLK GERLVRLKGQ RVVQTQWGRN RTRPEGAAKG SGAEQKDTTS EKSDHLVGLP
     LSNVETLGKE LFVYFGDFCL RVHFGMNGSV QIKGHRNKAF QKTSEPVLTL TLTVDSVSFH
     DCTVQIRSSS DCHDKYLQFQ SLDICSTHFS LSQATRTVSC HGDRMLCDVL LDQSVLPGVG
     NIIKNEVLQL KEEHVKHLVK MTRDFSMLFY KCRKEGRALS RHCKVYKRQW CGQCQGRITV
     CRMGENGRMT YFCEGCQTRD PETIINNRRI LPTKNSLIGW VTTGGHSRAD DQEWTCSVCT
     LINKGKAGMC SACGSPKPLS STGRLSDTEW TCSLCTLVND GDTKVCLVCE GPRSEPENSR
     EQLQRVIATS DGDSVHSSLP SVPDGTPSPC NGQVSRKREL PCSSGVIVTK PTIPASGKLA
     RLESAPLTSP SGTRVPSAAI GFNSDAAGNR LERPQHEITF HSNGSKVARG TEGSNTVMCC
     KQHNKWADDN FPLCNHGKRC VKRTVLKQGV NNGKNFYTCR LERGKQCPFF QHCALRKQFN
     IVVDGKKLRT EEPDIEKMSV GGGGGDGEGT RHPLKIFANI FISFIGAGVL GVPYAFKEAG
     IIEGMVIMSA VGVLSVKAML MIIDSKYKIN RDKRPKRTDD KEFAADIEME VLLDGDSAHG
     ENNGDLKTGG KQHRRQSSFD HHLEELDYGD VGFCCSYIIF ISQNLMHYVD NSHILFADFA
     NVFAYGVVFW FDFEHVSKVR IFIFTMFVVT TLYLVFGVCG YLSFGPETNS IITLNLPPGV
     FPLLVKGCLC FSLFFTYPVM MFPVVQILEK KWFRDPLKQT FLGNTLRACL VLTTGMVVLL
     IPSFSTIMSL LGSTCCALLA FILPGLFHMR IHRESISKCH YALDVFFIVL GVVG
//