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Database: UniProt
Entry: S4AMU1_9ACTN
LinkDB: S4AMU1_9ACTN
Original site: S4AMU1_9ACTN 
ID   S4AMU1_9ACTN            Unreviewed;       266 AA.
AC   S4AMU1;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE            EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
GN   ORFNames=STRAU_4196 {ECO:0000313|EMBL:EPH42732.1};
OS   Streptomyces aurantiacus JA 4570.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=1286094 {ECO:0000313|EMBL:EPH42732.1, ECO:0000313|Proteomes:UP000014629};
RN   [1] {ECO:0000313|EMBL:EPH42732.1, ECO:0000313|Proteomes:UP000014629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA 4570 {ECO:0000313|EMBL:EPH42732.1,
RC   ECO:0000313|Proteomes:UP000014629};
RA   Gruening B.A., Praeg A., Erxleben A., Guenther S., Mueller M.;
RT   "Draft Genome Sequence of Streptomyces aurantiacus, Which Produces
RT   Setomimycin.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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 FPG family. {ECO:0000256|ARBA:ARBA00009409}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPH42732.1}.
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DR   EMBL; AOPZ01000213; EPH42732.1; -; Genomic_DNA.
DR   RefSeq; WP_016642323.1; NZ_AOPZ01000213.1.
DR   AlphaFoldDB; S4AMU1; -.
DR   PATRIC; fig|1286094.4.peg.4149; -.
DR   OrthoDB; 9800855at2; -.
DR   Proteomes; UP000014629; Unassembled WGS sequence.
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:0019104; F:DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   CDD; cd08971; AcNei2_N; 1.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 3.20.190.10; MutM-like, N-terminal; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR035937; MutM-like_N-ter.
DR   InterPro; IPR044090; Nei2_N.
DR   InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   PANTHER; PTHR42697; ENDONUCLEASE 8; 1.
DR   PANTHER; PTHR42697:SF1; ENDONUCLEASE 8; 1.
DR   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   SMART; SM00898; Fapy_DNA_glyco; 1.
DR   SMART; SM01232; H2TH; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1.
DR   SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS01242; ZF_FPG_1; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014629};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00391}.
FT   DOMAIN          2..103
FT                   /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51068"
FT   DOMAIN          224..262
FT                   /note="FPG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51066"
SQ   SEQUENCE   266 AA;  29312 MW;  B116A4F7B2C8F0E7 CRC64;
     MPEGDTVHQA AHRLHTALAG HTLTRSDLRV PRHATADLTD RTVLDVTPRG KHLLTRVEGG
     LTLHSHLGMD GSWRVYAPQE RWRGGPAHQI RAVLATADHT AVGYRLPVLE LLRTTDEHRV
     VGHLGPDLLG PDWDPEQALR NLRAAPERPL GEALLDQRNL AGIGNIYKSE LCFLLGATPW
     LPVGDLPEET AARLPALAKK LLEANRDRPA RTTTGSTRPG QRLYVYGRAP RPCLRCGTAL
     RSAEQGDGTR RRPTYWCPTC QQGPTP
//
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