ID K3Z887_SETIT Unreviewed; 307 AA.
AC K3Z887;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=101781691 {ECO:0000313|EnsemblPlants:KQL12826};
GN ORFNames=SETIT_3G018900v2 {ECO:0000313|EMBL:RCV14939.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL12826, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EMBL:RCV14939.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL12826,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV14939.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV14939.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV14939.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQL12826}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL12826};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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; AGNK02001403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003530; RCV14939.1; -; Genomic_DNA.
DR RefSeq; XP_004960107.1; XM_004960050.1.
DR AlphaFoldDB; K3Z887; -.
DR STRING; 4555.K3Z887; -.
DR EnsemblPlants; KQL12826; KQL12826; SETIT_022757mg.
DR GeneID; 101781691; -.
DR Gramene; KQL12826; KQL12826; SETIT_022757mg.
DR KEGG; sita:101781691; -.
DR eggNOG; KOG2994; Eukaryota.
DR HOGENOM; CLU_032162_2_1_1; -.
DR InParanoid; K3Z887; -.
DR OMA; PDNGYLM; -.
DR OrthoDB; 11658at2759; -.
DR Proteomes; UP000004995; Chromosome III.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
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:UP000004995}.
FT DOMAIN 135..295
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 25..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03166,
FT ECO:0000256|PROSITE-ProRule:PRU10072"
SQ SEQUENCE 307 AA; 33635 MW; 9999C038E98F69A0 CRC64;
MPPSPPTPTA PKTIADFFTR PAKRLRAGAT APASASLSSS SSPSSLTPEQ RRRADTNLAL
ARARRNLRLA ESKAKASGGA AKLEELLVEK TWVEALDGEL RKPYALELCR FVTHERLHGP
LPVYPPPHLV FHALNATPFD RVKAVIIGQD PYHGPGQAMG LSFSVPEGIK KPSSLGNIFK
ELEKDLGCTV PSHGNLERWA VQGVLMLNTV LTVREHQANS HAKKGWEEFT DAVIKTISQK
RSGLVFLLWG NSAQSKTRLI DETKHHILKS AHPSGLSANR GFFGCRHFSK TNQILEKLGL
SAIDWQL
//
