UNG_DICDI
ID UNG_DICDI Reviewed; 346 AA.
AC P53766; Q54YQ3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166};
DE Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166};
DE EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
GN Name=uglA; ORFNames=DDB_G0277877;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 90-346.
RA Guyer R.B., Deering R.A.;
RT "Uracil-DNA glycosylase from Dictyostelium discoideum.";
RL Submitted (SEP-1995) 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.
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:0000255|HAMAP-Rule:MF_03166};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03166}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03166}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000255|HAMAP-Rule:MF_03166}.
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DR EMBL; AAFI02000023; EAL68111.1; -; Genomic_DNA.
DR EMBL; U32866; AAA75334.1; -; mRNA.
DR RefSeq; XP_642149.1; XM_637057.1.
DR AlphaFoldDB; P53766; -.
DR SMR; P53766; -.
DR STRING; 44689.DDB0214910; -.
DR PaxDb; P53766; -.
DR EnsemblProtists; EAL68111; EAL68111; DDB_G0277877.
DR GeneID; 8621357; -.
DR KEGG; ddi:DDB_G0277877; -.
DR dictyBase; DDB_G0277877; uglA.
DR eggNOG; KOG2994; Eukaryota.
DR HOGENOM; CLU_032162_0_0_1; -.
DR InParanoid; P53766; -.
DR PhylomeDB; P53766; -.
DR Reactome; R-DDI-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-DDI-110357; Displacement of DNA glycosylase by APEX1.
DR PRO; PR:P53766; -.
DR Proteomes; UP000002195; Chromosome 3.
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; -; 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 PANTHER; PTHR11264; PTHR11264; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
DR TIGRFAMs; TIGR00628; ung; 1.
DR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Hydrolase; Mitochondrion; Nucleus;
KW Reference proteome.
FT CHAIN 1..346
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176172"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03166"
SQ SEQUENCE 346 AA; 39374 MW; 60784FFC4CB339BF CRC64;
MSGKITDFFE KKTTTTIDEA ENKDNDKELT STTTTTTTTS TTSKKKVAAA PKKKAAVASK
KRKHESSDEE TDKEEQQNDD DDDGEEKVEN NNNNKKLKNE EKSEEINSTI TDNNYYDDIE
NYFTDKQWKE ALSGEFGKAY FKKMITQLNK RYSSKEKPIY PPKNEIFSAF NYAHLEDVKV
VIIGQDPYHG KGQAHGLSFS VKKGVSPPPS LINIYKELET DIEGFKRPLK NGFLEPWARQ
GVFLLNAVLT VEEATPNSHK DFGWADFTDA VLKILSKQDQ PIVFILWGGF AQKKEKLFTN
KNHLVLKSGH PSPLSIKHFI GCKHFSKSNE FLKSKGIEEI DWKITE
