ID   C7MY31_SACVD            Unreviewed;       225 AA.
AC   C7MY31;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   01-MAY-2013, entry version 24.
DE   SubName: Full=Uracil-DNA glycosylase;
GN   OrderedLocusNames=Svir_09210;
OS   Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 /
OS   NBRC 12207 / P101).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=471857;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101;
RX   DOI=10.4056/sigs.20263;
RA   Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA   Glavina del Rio T., Lucas S., Chen F., Tice H., Pitluck S.,
RA   Cheng J.-F., Chertkov O., Brettin T., Han C., Detter J.C., Kuske C.,
RA   Bruce D., Goodwin L., Chain P., D'haeseleer P., Chen A.,
RA   Palaniappan K., Ivanova N., Mavromatis K., Mikhailova N., Rohde M.,
RA   Tindall B.J., Goeker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT   "Complete genome sequence of Saccharomonospora viridis type strain
RT   (P101).";
RL   Stand. Genomic Sci. 1:141-149(2009).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as
CC       a result of misincorporation of dUMP residues by DNA polymerase or
CC       due to deamination of cytosine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched
CC       double-stranded DNA and polynucleotides, releasing free uracil.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
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DR   EMBL; CP001683; ACU95979.1; -; Genomic_DNA.
DR   RefSeq; YP_003132806.1; NC_013159.1.
DR   STRING; 471857.Svir_09210; -.
DR   EnsemblBacteria; ACU95979; ACU95979; Svir_09210.
DR   GeneID; 8386258; -.
DR   KEGG; svi:Svir_09210; -.
DR   PATRIC; 23392232; VBISacVir111818_0912.
DR   eggNOG; COG0692; -.
DR   HOGENOM; HOG000229528; -.
DR   KO; K03648; -.
DR   OMA; KGWEEVT; -.
DR   ProtClustDB; CLSK2819136; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:HAMAP.
DR   GO; GO:0006284; P:base-excision repair; IEA:HAMAP.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_00148; UDG; 1; -.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR002043; Ura_DNA_glycsylse.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; UDNA_glycsylseSF; 1.
DR   TIGRFAMs; TIGR00628; ung; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase.
SQ   SEQUENCE   225 AA;  24661 MW;  365EC5EA4737AED8 CRC64;
     MTARPLHEIL DPGWAKALEP VADEIAAMGQ FLRAEIAAGR TYLPAGDKIL RAFQQPFDDV
     RVLIVGQDPY PTPGHPIGLS FAVAPDVRPL PKSLVNIFRE YCDDLGYPEP SNGDLTPWAE
     QGVLLLNRAL TVQPGKPNSH QGKGWEEITE RAIVALVERN KPLVAILWGS NARKLKPLLG
     SVPCVESVHP SPLSARNGFF GSRPFSRTNA LLRQQGAEPI DWKLP
//