ID A0A166B992_EXIGL Unreviewed; 245 AA.
AC A0A166B992;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_03166, ECO:0000256|RuleBase:RU003780};
DE Short=UDG {ECO:0000256|HAMAP-Rule:MF_03166};
DE EC=3.2.2.27 {ECO:0000256|HAMAP-Rule:MF_03166, ECO:0000256|RuleBase:RU003780};
GN Name=UNG1 {ECO:0000256|HAMAP-Rule:MF_03166};
GN ORFNames=EXIGLDRAFT_606139 {ECO:0000313|EMBL:KZV99099.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV99099.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV99099.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV99099.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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|HAMAP-Rule:MF_03166,
CC 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|HAMAP-Rule:MF_03166,
CC ECO:0000256|RuleBase:RU003780};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03166}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000256|ARBA:ARBA00008184, ECO:0000256|HAMAP-
CC Rule:MF_03166, ECO:0000256|RuleBase:RU003780}.
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DR EMBL; KV425912; KZV99099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166B992; -.
DR STRING; 1314781.A0A166B992; -.
DR InParanoid; A0A166B992; -.
DR OrthoDB; 11658at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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|HAMAP-
KW Rule:MF_03166};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_03166};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03166};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03166};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 67..229
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT ACT_SITE 82
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03166,
FT ECO:0000256|PROSITE-ProRule:PRU10072"
SQ SEQUENCE 245 AA; 27014 MW; 3044EED1404E0250 CRC64;
MTTETVEDVS ALTWDTLEEQ TMGADWREAL APEFSKAYFK TLKSFLKVEA KSNKIFPPMK
DIYSWSRLTP LNEVKVVILG QDPYHDDGQA HGLAFSVLPP TKTPPSLRNI YKQLAADIPG
FKIPKSGDLS PLARQGVLWL NTALTVKAHA ANSHQKKGWL NLTTAALRAV TSRPSKGVVV
MAWGKNAQAL CSGVDDKKNL ILQSAHPSPL SASRGFLGNE HFKKANEWLR ETYGEDGGVD
WTVLN
//