ID A0A175YPM4_DAUCS Unreviewed; 719 AA.
AC A0A175YPM4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_03166};
DE Short=UDG {ECO:0000256|HAMAP-Rule:MF_03166};
DE EC=3.2.2.27 {ECO:0000256|HAMAP-Rule:MF_03166};
GN ORFNames=DCAR_026912 {ECO:0000313|EMBL:KZM85666.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM85666.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM85666.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM85666.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(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 -!- 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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM85666.1}.
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DR EMBL; LNRQ01000008; KZM85666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175YPM4; -.
DR STRING; 79200.A0A175YPM4; -.
DR EnsemblPlants; KZM85666; KZM85666; DCAR_026912.
DR Gramene; KZM85666; KZM85666; DCAR_026912.
DR Proteomes; UP000077755; Chromosome 8.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 2.
DR HAMAP; MF_00148; UDG; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
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; PF00067; p450; 1.
DR Pfam; PF03167; UDG; 2.
DR SMART; SM00986; UDG; 1.
DR SMART; SM00987; UreE_C; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 2.
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:UP000077755}.
FT DOMAIN 495..707
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 381..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 510
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03166,
FT ECO:0000256|PROSITE-ProRule:PRU10072"
SQ SEQUENCE 719 AA; 81591 MW; 28912B95A60B9193 CRC64;
MEVLFAASVA ISVILAILAH SALKLHQRLW IRPKKLEKQL KELGFKGNPY RFLHGDMKEY
FSIAQAANSK PIKFPHDIGA RLLPYEHRIV EKHGKNSFVW FGAKPRLNIM DPMLVKEILF
KHEEFHKVYP DPIADLVVGG LSTTHAETWT RRRKILNVAF NVEKLKGTLP VLYLSCKDTV
SKWKGLVSAG TTEIDVWPYI EILARDMISR AAFGSFYEEG RRIFQLHDMQ ADLAFQVMVS
SYIPWSRHFK FGANKKMKEL NKEMTGQLTR IIKKREKALK MGQKVNTDDL LSVLMDATKK
DIQEGSGMSM EEVIDECKLF YSAGADSTAR LLVWTIVCLS KHGDWQSRAR EEVFQVMGDK
DIDCEKLNQL KIRSSKRLKT TTTLSSPSDS ITLPDDSDLS PDQKSRIEFN KLLAKSKRNL
KLCSQRVSKA STGDGVMRLN LKLEELLVEE TWLEALPNEF EKPYAKKLCE FVENEICGSG
FPIYPPPHLI FNALNTTPFD RVKAVIIGQD PYHGPGQAMG LSFSVPEGIK VPSSLGNMYK
ELKQDLQCSI PSHGNLERWA LQGVLLLNSV LTVRQHQANS HAKKGWEQYT DAVIETISKK
KRGVVFLLWG NYAQGVLLLN SVLTVRQHQA NSHAKKGWEQ YTDAVIETIS KKKRGVVFLL
WGNYAQVKSR LIDGTKHHIL KAAHPSGLSA NRGFFGCRHF SRTNQLLEEM GMSPIDWQL
//
