SMUG1_XENLA
ID SMUG1_XENLA Reviewed; 281 AA.
AC Q9YGN6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Single-strand selective monofunctional uracil DNA glycosylase;
DE EC=3.2.2.-;
GN Name=smug1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=10074426; DOI=10.1016/s0960-9822(99)80087-6;
RA Haushalter K.A., Stukenberg P.T., Kirschner M.W., Verdine G.L.;
RT "Identification of a new uracil-DNA glycosylase family by expression
RT cloning using synthetic inhibitors.";
RL Curr. Biol. 9:174-185(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 35-281 IN COMPLEX WITH A
RP DOUBLE-STRANDED DNA CONTAINING A G/U MISPAIR.
RX PubMed=12820976; DOI=10.1016/s1097-2765(03)00235-1;
RA Wibley J.E.A., Waters T.R., Haushalter K., Verdine G.L., Pearl L.H.;
RT "Structure and specificity of the vertebrate anti-mutator uracil-DNA
RT glycosylase SMUG1.";
RL Mol. Cell 11:1647-1659(2003).
CC -!- FUNCTION: Recognizes base lesions in the genome and initiates base
CC excision DNA repair. Acts as a monofunctional DNA glycosylase specific
CC for uracil (U) residues in DNA with a preference for single-stranded
CC DNA substrates. Does not exhibit any enzymatic activity towards G/T
CC mismatches. {ECO:0000269|PubMed:10074426}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC SMUG1 family.
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DR EMBL; AF125181; AAD17300.1; -; mRNA.
DR EMBL; BC090216; AAH90216.1; -; mRNA.
DR RefSeq; NP_001083825.1; NM_001090356.1.
DR RefSeq; XP_018100415.1; XM_018244926.1.
DR PDB; 1OE4; X-ray; 2.00 A; A/B=35-281.
DR PDB; 1OE5; X-ray; 2.30 A; A/B=35-281.
DR PDB; 1OE6; X-ray; 2.65 A; A/B=35-281.
DR PDBsum; 1OE4; -.
DR PDBsum; 1OE5; -.
DR PDBsum; 1OE6; -.
DR AlphaFoldDB; Q9YGN6; -.
DR SMR; Q9YGN6; -.
DR DNASU; 399139; -.
DR GeneID; 399139; -.
DR KEGG; xla:399139; -.
DR CTD; 399139; -.
DR Xenbase; XB-GENE-953126; smug1.L.
DR OrthoDB; 960725at2759; -.
DR EvolutionaryTrace; Q9YGN6; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 399139; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017065; F:single-strand selective uracil DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd19374; UDG-F3_SMUG1-like; 1.
DR Gene3D; 3.40.470.10; -; 1.
DR InterPro; IPR039134; SMUG1.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR PANTHER; PTHR13235; PTHR13235; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA-binding; Hydrolase; Nucleus;
KW Reference proteome.
FT CHAIN 1..281
FT /note="Single-strand selective monofunctional uracil DNA
FT glycosylase"
FT /id="PRO_0000071995"
FT REGION 182..198
FT /note="DNA-binding"
FT BINDING 95
FT /ligand="substrate"
FT BINDING 109
FT /ligand="substrate"
FT BINDING 174
FT /ligand="substrate"
FT BINDING 250
FT /ligand="substrate"
FT HELIX 39..54
FT /evidence="ECO:0007829|PDB:1OE4"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:1OE4"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1OE4"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:1OE4"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1OE4"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 195..216
FT /evidence="ECO:0007829|PDB:1OE4"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:1OE4"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1OE4"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 262..273
FT /evidence="ECO:0007829|PDB:1OE4"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:1OE4"
SQ SEQUENCE 281 AA; 31228 MW; B92292E5B77CD007 CRC64;
MAAEACVPAE FSKDEKNGSI LSAFCSDIPD ITSSTESPAD SFLKVELELN LKLSNLVFQD
PVQYVYNPLV YAWAPHENYV QTYCKSKKEV LFLGMNPGPF GMAQTGVPFG EVNHVRDWLQ
IEGPVSKPEV EHPKRRIRGF ECPQSEVSGA RFWSLFKSLC GQPETFFKHC FVHNHCPLIF
MNHSGKNLTP TDLPKAQRDT LLEICDEALC QAVRVLGVKL VIGVGRFSEQ RARKALMAEG
IDVTVKGIMH PSPRNPQANK GWEGIVRGQL LELGVLSLLT G
