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Database: UniProt
Entry: A0A3Q0T237_AMPCI
LinkDB: A0A3Q0T237_AMPCI
Original site: A0A3Q0T237_AMPCI 
ID   A0A3Q0T237_AMPCI        Unreviewed;       401 AA.
AC   A0A3Q0T237;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE            EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000028918.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000028918.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC         deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC         dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC         2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC         ChEBI:CHEBI:167181; EC=4.2.99.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00024490};
CC   -!- SIMILARITY: Belongs to the type-1 OGG1 family.
CC       {ECO:0000256|ARBA:ARBA00010679}.
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DR   AlphaFoldDB; A0A3Q0T237; -.
DR   Ensembl; ENSACIT00000029685.1; ENSACIP00000028918.1; ENSACIG00000022385.1.
DR   GeneTree; ENSGT00640000091554; -.
DR   OMA; GYAQEYL; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 3.30.310.40; -; 1.
DR   Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR012904; OGG_N.
DR   PANTHER; PTHR10242; 8-OXOGUANINE DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR10242:SF2; N-GLYCOSYLASE_DNA LYASE; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   Pfam; PF07934; OGG_N; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   SUPFAM; SSF55945; TATA-box binding protein-like; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204}.
FT   DOMAIN          176..344
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
FT   REGION          92..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  45854 MW;  B87F1BF3130DECB1 CRC64;
     MASHAVLSSG SKMWKSMACA KSELRLDLTL SCGQSFRWRE TAEGHWTGAM GGRVWTLTQT
     DDTLWYHVYK NQDKQKEGSD RKRRSGISLA EENTAEKRFK GAPEKDEEEP LAVSSVQNRE
     LDEEMLRDYF QLDVRMDDLY KEWGAADCHF KRIASIFTGV RMLRQDPTEC LFSFICTSNN
     HISRIQGMVE RLCQALGSPL CQLDQTSYHD FPSVSALADS SVEAHLRDLG FGYRARFVHQ
     SAKQILDNHG PQWLVGLRSV PYLEARDALR TLPGVGTKVA DCVCLMSLDK PEAVPIDTHM
     WQIAKRDYKY TANNGQKSIT EKLYRDIGDF FRKLWGPYAG WAQSVLFCSD LKKFQSFKET
     AHPKQPKKEE EDKEDKIVPT FCNKKVITCQ KHQGAPFLEL K
//
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