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UNG_STAAR
ID   UNG_STAAR               Reviewed;         218 AA.
AC   Q6GJ88;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00148};
DE            Short=UDG {ECO:0000255|HAMAP-Rule:MF_00148};
DE            EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_00148};
GN   Name=ung {ECO:0000255|HAMAP-Rule:MF_00148}; OrderedLocusNames=SAR0586;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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:0000255|HAMAP-Rule:MF_00148}.
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_00148};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000255|HAMAP-Rule:MF_00148}.
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DR   EMBL; BX571856; CAG39606.1; -; Genomic_DNA.
DR   RefSeq; WP_000455258.1; NC_002952.2.
DR   PDB; 3WDF; X-ray; 1.48 A; A/B=1-218.
DR   PDB; 3WDG; X-ray; 2.20 A; A=1-218.
DR   PDBsum; 3WDF; -.
DR   PDBsum; 3WDG; -.
DR   AlphaFoldDB; Q6GJ88; -.
DR   SMR; Q6GJ88; -.
DR   KEGG; sar:SAR0586; -.
DR   HOGENOM; CLU_032162_3_1_9; -.
DR   OMA; PDNGYLM; -.
DR   OrthoDB; 1260295at2; -.
DR   Proteomes; UP000000596; 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; -; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA damage; DNA repair; Hydrolase.
FT   CHAIN           1..218
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176139"
FT   ACT_SITE        59
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
FT   HELIX           3..13
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           17..29
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           41..45
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           82..94
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           105..110
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   STRAND          112..118
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   TURN            126..131
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           134..148
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   STRAND          153..158
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           159..162
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           163..167
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   TURN            170..172
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   STRAND          173..178
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   TURN            183..185
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           186..190
FT                   /evidence="ECO:0007829|PDB:3WDF"
FT   HELIX           195..205
FT                   /evidence="ECO:0007829|PDB:3WDF"
SQ   SEQUENCE   218 AA;  24967 MW;  5731B93297F0D154 CRC64;
     MEWSQIFHDI TTKHDFKAMH DFLEKEYSTA IVYPDRENIY QAFDLTPFEN IKVVILGQDP
     YHGPNQAHGL AFSVQPNAKF PPSLRNMYKE LADDIGCVRQ TPHLQDWARE GVLLLNTVLT
     VRQGEANSHR DIGWETFTDE IIKAVSDYKE HVVFILWGKP AQQKIKLIDT SKHCIIKSVH
     PSPLSAYRGF FGSKPYSKAN TYLESVGKSP INWCESEA
 
 
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