ID S9VE50_9TRYP Unreviewed; 304 AA.
AC S9VE50;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=ADEAN_000979900 {ECO:0000313|EMBL:CAD2222259.1};
OS Angomonas deanei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Strigomonadinae; Angomonas.
OX NCBI_TaxID=59799 {ECO:0000313|EMBL:CAD2222259.1, ECO:0000313|Proteomes:UP000515908};
RN [1] {ECO:0000313|EMBL:CAD2222259.1, ECO:0000313|Proteomes:UP000515908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Crithidia deanei Carvalho (ATCC PRA-265)
RC {ECO:0000313|Proteomes:UP000515908};
RA Newling K., Davey J., Forrester S.;
RL Submitted (AUG-2020) 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|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; LR877169; CAD2222259.1; -; Genomic_DNA.
DR AlphaFoldDB; S9VE50; -.
DR EnsemblProtists; EPY25341; EPY25341; AGDE_11866.
DR EnsemblProtists; EPY38930; EPY38930; AGDE_04999.
DR VEuPathDB; TriTrypDB:ADEAN_000979900; -.
DR OrthoDB; 11658at2759; -.
DR Proteomes; UP000515908; Chromosome 25.
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:UP000515908}.
FT DOMAIN 123..284
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03166,
FT ECO:0000256|PROSITE-ProRule:PRU10072"
SQ SEQUENCE 304 AA; 33516 MW; 1FE077B14F4E31CB CRC64;
MQSAAPKKQA TLESMFAKRS PTKTTEVISV DEDSQLAGGK RPRSRSGSKE KRKSPSPPKR
SGGNGWLGDL ITEPSWRKEL QPVLQDAAQG KGLLSQIEKF IDTAEGKGAT VLPPRPCIFT
AFNRTPFDKV KVVLLGQDPY HDIGQAHGLC FSVQPGVRPP PSLKNMYKEL ESDVPGFTTP
SHGYLQSWAD QGILMLNATL TVTAHEANSH AKCGWQQFTD EVIVRVSAQR ERRVVFLLWG
NFARGKKKLI DTSRHIVIEN GHPSPLSVKH WVGCKCFSKC NEALVKAGHT PIDWKLPATV
TMES
//
