ID A0A317XWE0_9BASI Unreviewed; 269 AA.
AC A0A317XWE0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=BCV70DRAFT_150853 {ECO:0000313|EMBL:PWZ02422.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWZ02422.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWZ02422.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWZ02422.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819189; PWZ02422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XWE0; -.
DR STRING; 1882483.A0A317XWE0; -.
DR InParanoid; A0A317XWE0; -.
DR Proteomes; UP000246740; 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:UP000246740}.
FT DOMAIN 66..254
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 169..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 81
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10072"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PWZ02422.1"
FT NON_TER 269
FT /evidence="ECO:0000313|EMBL:PWZ02422.1"
SQ SEQUENCE 269 AA; 29016 MW; 9CDEA2729A3C7012 CRC64;
KVQPPADPAS DPLWLERQTM SPDWFQRLES EMKQPYFIEL KRFLASEDRA GKRTYPPPPL
VHSWSRLTPI DRVKVVVVGQ DPYHGPNQAC GLSFSVNRGV ATPPSLRNIY KEIATEYPGF
KPPNHGCLDG WATQGVLLLN ACLTVSAGQA GSHHGKGWEK LTKHILKLNG GGGGGDDNDN
DGDGDGDGKG KGKDKGKGVV FLVWGAPAAK TLAEAGVTDT SGNVLILKSP HPSPLSAHRG
FLGNGHFVKA NTWLQQRYGP DGGIDWTKL
//
