ID A0A199VI33_ANACO Unreviewed; 296 AA.
AC A0A199VI33;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=ACMD2_08194 {ECO:0000313|EMBL:OAY76802.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY76802.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY76802.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY76802.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(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|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}.
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:OAY76802.1}.
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DR EMBL; LSRQ01001710; OAY76802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A199VI33; -.
DR STRING; 4615.A0A199VI33; -.
DR Proteomes; UP000092600; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
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:UP000092600}.
FT DOMAIN 146..294
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 19..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10072"
FT NON_TER 296
FT /evidence="ECO:0000313|EMBL:OAY76802.1"
SQ SEQUENCE 296 AA; 32363 MW; B67EA8188795C56C CRC64;
MASSSKTLVE ILHPAKRLRS LSSSPETLTP KSSISALSKS FSSDSCAGDG EIPPESASAL
TPEQRKRIEL NKALARSRRN LRLCAERIES AKGTLEELLV EETWLEALPG ELQKPYAKNL
CRFVEREVRG SVPVYPPPQL IFNALHSTPF DQVKAVIIGQ DPYHGPGQAM GLAFSVPEGI
KIPSSLINIF RELEKDVGCS VPAHGNLEKW AVQGVLLLNT VLTVRKHQAN SHAKKGWEPF
TDAVIRTISQ KKSGVVFLLW GNSAQGKIRL IDESKHFILK AAHPSGLSAN RGFFGC
//
