ID U1GCN3_ENDPU Unreviewed; 398 AA.
AC U1GCN3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_03166};
DE Short=UDG {ECO:0000256|HAMAP-Rule:MF_03166};
DE EC=3.2.2.27 {ECO:0000256|HAMAP-Rule:MF_03166};
GN Name=UNG1 {ECO:0000256|HAMAP-Rule:MF_03166};
GN ORFNames=EPUS_07276 {ECO:0000313|EMBL:ERF69461.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF69461.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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|HAMAP-Rule:MF_03166}.
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|HAMAP-Rule:MF_03166};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03166}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000256|ARBA:ARBA00008184, ECO:0000256|HAMAP-
CC Rule:MF_03166}.
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DR EMBL; KE721405; ERF69461.1; -; Genomic_DNA.
DR RefSeq; XP_007804873.1; XM_007806682.1.
DR AlphaFoldDB; U1GCN3; -.
DR GeneID; 19242161; -.
DR eggNOG; KOG2994; Eukaryota.
DR HOGENOM; CLU_032162_2_0_1; -.
DR OMA; AGKKWFP; -.
DR OrthoDB; 11658at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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 DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_03166};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_03166};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03166};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03166};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373}.
FT DOMAIN 137..302
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03166,
FT ECO:0000256|PROSITE-ProRule:PRU10072"
SQ SEQUENCE 398 AA; 43605 MW; 29A3A0464CB69905 CRC64;
MSSPIDGPLK RKANDLPSSS PAEPKKPKTN ASITSFFGGP KSGTKSSKPA GSVANGSSLI
SLVTPRFDKA KWVAKLTPEQ RTLLKLEIDT LDESWLAHLK DEILTPSFLN LKRFLKSEIE
SGKKVFPPLE EIYSWSRYTP LPSVRAVILG QDPYHNHNQA HGLCFSVRPP TEAPPSLKNI
YLALANDYPS FTPPPRKLGL LTPWAEQGVL MLNTCLTVRA HEPASHKDKG WERFTQKVID
TVAKTRTRGV VFLAWGYPAQ LRCKGLGTTG KHLVLQSPHP SPLSAYKGFL TCGHFKKTNE
WLKERYGDEG VIDWNLDQPK PTAASNVEGP VRVTADPAKG AGEADPSTQL AEEKQESAAT
DPVVAGENNG QSPEEDDTDA IDALQEMAQA ELEAEKRE
//
