ID   D6ZJD8_MOBCV            Unreviewed;       232 AA.
AC   D6ZJD8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
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   ECO:0000313|EMBL:ADI66837.1};
GN   OrderedLocusNames=HMPREF0573_10518 {ECO:0000313|EMBL:ADI66837.1};
OS   Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio
OS   vaginalis).
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Mobiluncus.
OX   NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI66837.1, ECO:0000313|Proteomes:UP000006742};
RN   [1] {ECO:0000313|Proteomes:UP000006742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43063 / DSM 2711 / V125
RC   {ECO:0000313|Proteomes:UP000006742};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT   "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; CP001992; ADI66837.1; -; Genomic_DNA.
DR   RefSeq; WP_004011513.1; NC_014246.1.
DR   AlphaFoldDB; D6ZJD8; -.
DR   STRING; 548479.HMPREF0573_10518; -.
DR   GeneID; 55564680; -.
DR   KEGG; mcu:HMPREF0573_10518; -.
DR   eggNOG; COG0692; Bacteria.
DR   HOGENOM; CLU_032162_3_1_11; -.
DR   Proteomes; UP000006742; Chromosome.
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}; Glycosidase {ECO:0000313|EMBL:ADI66837.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00148};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006742}.
FT   DOMAIN          57..219
FT                   /note="Uracil-DNA glycosylase-like"
FT                   /evidence="ECO:0000259|SMART:SM00986"
FT   ACT_SITE        72
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00148,
FT                   ECO:0000256|PROSITE-ProRule:PRU10072"
SQ   SEQUENCE   232 AA;  25485 MW;  E3853EBA2A9A9AE1 CRC64;
     MQTGEERGGL ERIMSPDWAQ VMAPVEGQIH AMGDFLRAEL AAGRGYFPAG ENVFHAFQYP
     LERVKVLIVG QDPYPTPGHA MGLSFSVMSG TEIPRSLVNI FKELHQDLGL PLPTSGDLRP
     WAEQGVMLLN RALTVQPGKP ASHRGRGWEA ITEFAIRELA NHHAAQGLPL VAILWGADAR
     RTKEFMPHVP CLESVHPSPL SASRGFFGSR PFSRANELLV AQSGQPVDWR LP
//