ID A0A1E3QTT7_9ASCO Unreviewed; 268 AA.
AC A0A1E3QTT7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000256|RuleBase:RU003780};
DE EC=3.2.2.27 {ECO:0000256|RuleBase:RU003780};
DE Flags: Fragment;
GN ORFNames=BABINDRAFT_29465 {ECO:0000313|EMBL:ODQ81093.1};
OS Babjeviella inositovora NRRL Y-12698.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ81093.1, ECO:0000313|Proteomes:UP000094336};
RN [1] {ECO:0000313|Proteomes:UP000094336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC result of misincorporation of dUMP residues by DNA polymerase or due to
CC deamination of cytosine. {ECO:0000256|RuleBase:RU003780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC Evidence={ECO:0000256|RuleBase:RU003780};
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000256|ARBA:ARBA00008184,
CC ECO:0000256|RuleBase:RU003780}.
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DR EMBL; KV454428; ODQ81093.1; -; Genomic_DNA.
DR RefSeq; XP_018986421.1; XM_019131450.1.
DR AlphaFoldDB; A0A1E3QTT7; -.
DR STRING; 984486.A0A1E3QTT7; -.
DR GeneID; 30149303; -.
DR OrthoDB; 11658at2759; -.
DR Proteomes; UP000094336; Unassembled WGS sequence.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR CDD; cd10027; UDG-F1-like; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR HAMAP; MF_00148; UDG; 1.
DR InterPro; IPR002043; UDG_fam1.
DR InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR NCBIfam; TIGR00628; ung; 1.
DR PANTHER; PTHR11264; URACIL-DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR11264:SF0; URACIL-DNA GLYCOSYLASE; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SMART; SM00987; UreE_C; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
DR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU003780};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU003780};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003780};
KW Reference proteome {ECO:0000313|Proteomes:UP000094336}.
FT DOMAIN 71..249
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10072"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ODQ81093.1"
FT NON_TER 268
FT /evidence="ECO:0000313|EMBL:ODQ81093.1"
SQ SEQUENCE 268 AA; 30787 MW; 250417F2241DA6C7 CRC64;
FDKDAWVASL SEEQRQLLQL EIQHLEISWL TLLHKELTKP YFINLKKFLL QQSKFKKEVF
PPENEIYSWS HLTPFPKLRV LVIGQDPYHN NGQAHGLAFL VKPGTRPPPS LQNIYKGMKL
NFENFEIPLF NEHNDAGYLV KWASQGVLLL NTCLTVEAHK PNSHSKQGWE QFTSKIIEII
AGEAANPGCV CLLWGGPAQR TFDGIITPKN RQLVQKKHLI LKSCHPSPLS ANRGGWFENR
HFRECNDWLI KKYGKGIDWA IIKSNSVL
//
