ID A0A168KH21_CORDF Unreviewed; 950 AA.
AC A0A168KH21;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 30.
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=LEL_01225 {ECO:0000313|EMBL:OAA81680.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA81680.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA81680.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA81680.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001311};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03166}.
CC -!- SIMILARITY: Belongs to the amidase family.
CC {ECO:0000256|ARBA:ARBA00009199}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000256|ARBA:ARBA00008184, ECO:0000256|HAMAP-
CC Rule:MF_03166}.
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:OAA81680.1}.
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DR EMBL; AZHF01000001; OAA81680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168KH21; -.
DR STRING; 1081108.A0A168KH21; -.
DR OrthoDB; 11658at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
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; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR HAMAP; MF_00148; UDG; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
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; PTHR46072:SF11; AMIDASE-RELATED; 1.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR Pfam; PF01425; Amidase; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SMART; SM00987; UreE_C; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
DR PROSITE; PS00571; AMIDASES; 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:UP000076881}.
FT DOMAIN 706..870
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 409..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 721
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03166,
FT ECO:0000256|PROSITE-ProRule:PRU10072"
SQ SEQUENCE 950 AA; 104129 MW; EAA64855B94744CB CRC64;
MDSRDCRDTP RPAWEAIALD KRSQRDAAIP AEWRLQAGSV PESRLNVTGV PVESGILVSR
EIDITETDAP LLVQKLAARE YSSYEVTLAF CKRAAISQQL VNCLSEIFFD IALETARQLD
AEYEASGVLR GPLHGLPVSL KDCFKVAGTD ASIGCTAFAS QPTSEAAESE VTKIMRQSGA
ILFCKTNVPM ALMSGETFNA MYGYTSNPYN RDLSSGGSSG GESALLALRG SPLGVGTDVG
GSIRIPAAFC GLYSLKPSFG RFPTYGLRDA LEGQEAVRNV VGPMSTSVTG LELWSKAVMQ
SKPWVGVDPD CLNMPWRNVQ MPEKLCFGLL LDDGIVKPLP PVSRALLVTK AALEKAGHTV
IEFRIDDPLY TDRLKFALYR SATADALNKI LDQTQEPWPR GYEVLAEMAN KSSQPQNGDR
ERSPQSADGR ATVSQLWEAQ AKRTAFSKRM LTAWADTKLK TDTAREMDAL LMPTTPWPAS
RKQVNPCSNS RTQRADNTDR YEFSYDNYTS LWNVVDYCAT TIPVTQVLPT EDTKPEYKAR
AELEAKIWQD STALARLPLC RPSTLQARRL LVLASAYAMS SSLKRKASGS GASSPEVKKP
KANGNIASFF GAAPKPGQTA AGTSSPSAAT TTTTKFDKDK WVASLTPEQR SLLKLEIDTM
HESWLGLLKD DITTKEFLDL KKFLDRETAA GKKWFPPKED VYSWSRHTPF NNVKVVIVGQ
DPYHNVNQAH GMAFSVRPPT PAPPSLRNMY IALAKDYPSF EKPAKSAGLL TPWADRGVLM
LNTCLTVRAH EANSHSNRGW ERLTQRVIDL VAQKRARGVV FMAWGTPAGK RVMKVDKQKH
LVLQSVHPSP LSASRGFFDC GHFRKANDWL TARYGAAEGE IDWALVPGNS TLSAPKAEEA
KAEAKTETSK PEKKAATGKE NVEVDEEIGS DDEAALEEAI RAAEEETTKP
//
