ID A0A1H6EGB3_9ACTN Unreviewed; 227 AA.
AC A0A1H6EGB3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000256|ARBA:ARBA00012030, ECO:0000256|HAMAP-Rule:MF_00148};
DE Short=UDG {ECO:0000256|HAMAP-Rule:MF_00148};
DE EC=3.2.2.27 {ECO:0000256|ARBA:ARBA00012030, ECO:0000256|HAMAP-Rule:MF_00148};
GN Name=ung {ECO:0000256|HAMAP-Rule:MF_00148};
GN ORFNames=SAMN05216223_13512 {ECO:0000313|EMBL:SEG95864.1};
OS Actinacidiphila yanglinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310779 {ECO:0000313|EMBL:SEG95864.1, ECO:0000313|Proteomes:UP000236754};
RN [1] {ECO:0000313|EMBL:SEG95864.1, ECO:0000313|Proteomes:UP000236754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2023 {ECO:0000313|EMBL:SEG95864.1,
RC ECO:0000313|Proteomes:UP000236754};
RA de Groot N.N.;
RL Submitted (OCT-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|ARBA:ARBA00002631,
CC ECO:0000256|HAMAP-Rule:MF_00148, 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|ARBA:ARBA00001400, ECO:0000256|HAMAP-
CC Rule:MF_00148, ECO:0000256|RuleBase:RU003780};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00148}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000256|ARBA:ARBA00008184, ECO:0000256|HAMAP-
CC Rule:MF_00148, ECO:0000256|RuleBase:RU003780}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNVU01000035; SEG95864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6EGB3; -.
DR Proteomes; UP000236754; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00148};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00148};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00148};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00148};
KW Reference proteome {ECO:0000313|Proteomes:UP000236754}.
FT DOMAIN 50..209
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00148,
FT ECO:0000256|PROSITE-ProRule:PRU10072"
SQ SEQUENCE 227 AA; 25254 MW; 529044FD1138396B CRC64;
MPSMLPDSWQ AVLGEELDKP YFQQLSEFVE AERQVHHVFP PRDEVFAALE ATPFDKVKVL
VLGQDPYHGA GQGHGLCFSV RPGVRTPPSL RNIFKELKDE FGYPVPDNGY LMPWAEQGVL
LLNAVLTVRE GEANSHKGKG WEKFTDAVIR AVSARPDPAV FVLWGNYAKK KKPLIDTDRH
TVIEGAHPSP LSAKLFLGSH PFTRIDEAVT SQGHVPIDWR IPDLASA
//
