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Database: UniProt
Entry: A0A1I0DL00_9BACL
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ID   A0A1I0DL00_9BACL        Unreviewed;       271 AA.
AC   A0A1I0DL00;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 8.
DE   SubName: Full=DNA-(Apurinic or apyrimidinic site) lyase {ECO:0000313|EMBL:SET32838.1};
GN   ORFNames=SAMN03159358_1350 {ECO:0000313|EMBL:SET32838.1};
OS   Paenibacillus sp. NFR01.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1566279 {ECO:0000313|EMBL:SET32838.1, ECO:0000313|Proteomes:UP000198735};
RN   [1] {ECO:0000313|EMBL:SET32838.1, ECO:0000313|Proteomes:UP000198735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFR01 {ECO:0000313|EMBL:SET32838.1,
RC   ECO:0000313|Proteomes:UP000198735};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|SAAS:SAAS01121890};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|SAAS:SAAS00610166};
CC   -!- SIMILARITY: Belongs to the FPG family.
CC       {ECO:0000256|SAAS:SAAS00557294}.
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DR   EMBL; FOIK01000001; SET32838.1; -; Genomic_DNA.
DR   Proteomes; UP000198735; 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:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   Gene3D; 3.20.190.10; -; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR035937; MutM-like_N-ter.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
DR   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   SMART; SM00898; Fapy_DNA_glyco; 1.
DR   SMART; SM01232; H2TH; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   SUPFAM; SSF81624; SSF81624; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000198735};
KW   DNA damage {ECO:0000256|SAAS:SAAS01087016};
KW   DNA repair {ECO:0000256|SAAS:SAAS01087019};
KW   DNA-binding {ECO:0000256|SAAS:SAAS01087047};
KW   Glycosidase {ECO:0000256|SAAS:SAAS01087011};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01087030};
KW   Lyase {ECO:0000256|SAAS:SAAS01087025, ECO:0000313|EMBL:SET32838.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00551678};
KW   Multifunctional enzyme {ECO:0000256|SAAS:SAAS01087023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198735};
KW   Zinc {ECO:0000256|SAAS:SAAS00551670};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00391,
KW   ECO:0000256|SAAS:SAAS00551733}.
FT   DOMAIN        2    112       FPG_CAT. {ECO:0000259|PROSITE:PS51068}.
FT   DOMAIN      235    269       FPG-type. {ECO:0000259|PROSITE:PS51066}.
SQ   SEQUENCE   271 AA;  30404 MW;  B36B7F2B78D80858 CRC64;
     MPEFPEMENY RMLLGQHIIN IPITAVTVNR EKSINMDADA FAKALVGARV VYVERRAKHL
     LFHLHDGRRL LLHLMLGGLL YYGPESERPD RTTQVEIAFG DNLLYFMGLR LGYLHLLSVK
     ESEAAMGKLG PELLDRRMTA ERFAELLRGR RGALKSLLVN QQVMAGIGNC YADEIAFEAR
     LLPSALVQNL SPEAVGRLYD SVRKVLTEAT EIGGYMEMPF MAGDTVTGRY NDCCKVYDRG
     GEPCLRDGGT IVKTELSGRK VFYCPECQHE G
//
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