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Database: UniProt
Entry: A0A1E3QBG4_LIPST
LinkDB: A0A1E3QBG4_LIPST
Original site: A0A1E3QBG4_LIPST 
ID   A0A1E3QBG4_LIPST        Unreviewed;       379 AA.
AC   A0A1E3QBG4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Formamidopyrimidine-DNA glycosylase catalytic domain-containing protein {ECO:0000259|PROSITE:PS51068};
GN   ORFNames=LIPSTDRAFT_103096 {ECO:0000313|EMBL:ODQ75039.1};
OS   Lipomyces starkeyi NRRL Y-11557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ75039.1, ECO:0000313|Proteomes:UP000094385};
RN   [1] {ECO:0000313|EMBL:ODQ75039.1, ECO:0000313|Proteomes:UP000094385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ75039.1,
RC   ECO:0000313|Proteomes:UP000094385};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC         residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC         methyl)formamidopyrimidine.; EC=3.2.2.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001668};
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}.
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DR   EMBL; KV454291; ODQ75039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3QBG4; -.
DR   STRING; 675824.A0A1E3QBG4; -.
DR   OrthoDB; 276614at2759; -.
DR   Proteomes; UP000094385; 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   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; IPR012319; FPG_cat.
DR   InterPro; IPR035937; MutM-like_N-ter.
DR   InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR   PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR22993:SF9; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 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; 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.
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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094385}.
FT   DOMAIN          2..157
FT                   /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51068"
FT   REGION          330..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   379 AA;  43603 MW;  EE01E6AFC2A8A221 CRC64;
     MPELGEVAHA AKLLSTNLKG KTITKFITDA KDTLVFPSLS SQDRSQIESA YVSKRIADVG
     RHGKYFWIIL SGGRQSDMTK KTGEYDVMLM HFGMTGWLKI QNVHSHFFPM ERSRNGKKPD
     NYDEKAAAEP WPPKYHKFLL STDDGIEIAF TDPRRLSRVR FLEIVNTKSD METVEQVESE
     LMKVEPLVRM GPDFSKVESR WSQDQFLEVL AKRRVPIKSL LLDQAVCAGV GNWMADEILF
     QSRIHPEQYT NKMGLKKMQL LYNMLCEVCE VAVETEGDTE KFPKSWLMLH RWSKRQKRGE
     RPMTADGYIV DFVTVGGRTS CFVPELQKME NATGEEDDDA SERKPQAKAN SRTKKLKTEK
     EDKVVKPART RRRTRKGDR
//
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