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Database: UniProt
Entry: C6X9C0_METGS
LinkDB: C6X9C0_METGS
Original site: C6X9C0_METGS 
ID   C6X9C0_METGS            Unreviewed;       219 AA.
AC   C6X9C0;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
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   OrderedLocusNames=Msip34_0492 {ECO:0000313|EMBL:ACT49740.1};
OS   Methylovorus glucosotrophus (strain SIP3-4).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylovorus.
OX   NCBI_TaxID=582744 {ECO:0000313|EMBL:ACT49740.1, ECO:0000313|Proteomes:UP000002743};
RN   [1] {ECO:0000313|Proteomes:UP000002743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP3-4 {ECO:0000313|Proteomes:UP000002743};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Clum A., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT   "Complete sequence of chromosome of Methylovorus sp. SIP3-4.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACT49740.1, ECO:0000313|Proteomes:UP000002743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP3-4 {ECO:0000313|EMBL:ACT49740.1,
RC   ECO:0000313|Proteomes:UP000002743};
RX   PubMed=21622745; DOI=10.1128/JB.00404-11;
RA   Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA   Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA   Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT   "Genomes of three methylotrophs from a single niche uncover genetic and
RT   metabolic divergence of Methylophilaceae.";
RL   J. Bacteriol. 193:3757-3764(2011).
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; CP001674; ACT49740.1; -; Genomic_DNA.
DR   RefSeq; WP_015829389.1; NC_012969.1.
DR   AlphaFoldDB; C6X9C0; -.
DR   STRING; 582744.Msip34_0492; -.
DR   KEGG; mei:Msip34_0492; -.
DR   eggNOG; COG0692; Bacteria.
DR   HOGENOM; CLU_032162_3_1_4; -.
DR   OrthoDB; 9804372at2; -.
DR   Proteomes; UP000002743; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00148};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002743}.
FT   DOMAIN          47..209
FT                   /note="Uracil-DNA glycosylase-like"
FT                   /evidence="ECO:0000259|SMART:SM00986"
FT   ACT_SITE        62
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00148,
FT                   ECO:0000256|PROSITE-ProRule:PRU10072"
SQ   SEQUENCE   219 AA;  24406 MW;  8B11FF11584C06EF CRC64;
     MHSPETIPSA WAERLPELAQ QYASIREQLR DETDIRPRPG LWFEALRAVN PQEARVVILG
     QDPYHGEDHG IQQAHGLAFS VPAGVRPPPS LRNILKELAS DMGEAHIEGG NLSNWSKQGV
     LLLNASLTTR GGEAGAHAAY WHAFTEKLMT WLGQREQPLV FILWGSHAQR HKSLIAPQHQ
     IIESVHPSPL SAHRGFFGSR PFSQTNAVLA EWGQTPIHW
//
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