ID A0A3E2HL27_SCYLI Unreviewed; 324 AA.
AC A0A3E2HL27;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000256|RuleBase:RU003780};
DE EC=3.2.2.27 {ECO:0000256|RuleBase:RU003780};
DE Flags: Fragment;
GN ORFNames=B7463_g2566 {ECO:0000313|EMBL:RFU33761.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU33761.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU33761.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU33761.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) 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|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|RuleBase:RU003780};
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000256|ARBA:ARBA00008184,
CC ECO:0000256|RuleBase:RU003780}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFU33761.1}.
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DR EMBL; NCSJ02000030; RFU33761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HL27; -.
DR STRING; 5539.A0A3E2HL27; -.
DR OMA; AGKKWFP; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
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 DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU003780};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU003780};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003780};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309}.
FT DOMAIN 137..301
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10072"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU33761.1"
FT NON_TER 324
FT /evidence="ECO:0000313|EMBL:RFU33761.1"
SQ SEQUENCE 324 AA; 35957 MW; 595C213206DEB246 CRC64;
MSLKRKADDG NALATKKTKA DGNIAAFFSA PKAAQVTTTK TTVTKDGVET TVSTVTEAVV
APAPPKFDKE KWVAKLTPEQ KELLQLEIDT LDESWLAVLK EDLVGKEFLE LKKFIKREID
SGKKIFPPLP EVYSWSRHTP LNNVRAVIIG QDPYHNHNQA HGLCFSVRAP TPAPPSLKNI
YIALKNDYPD FKPPASNGGL LTPWADQGVL MLNTCLTVRA HEANSHSNRG WEKFTQRVID
IVAARRTRGV VFLAWGAPAG RRVVKVDKKR HLVLQSVHPS PLSASRGWFN CGHFKKTNEW
LAQRYGEEGV IDWNLNVTPA KAGV
//
