ID A2QSA7_ASPNC Unreviewed; 345 AA.
AC A2QSA7;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Contig An08c0250, genomic contig {ECO:0000313|EMBL:CAK45707.1};
GN ORFNames=An08g10020 {ECO:0000313|EMBL:CAK45707.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK45707.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK45707.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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DR EMBL; AM270180; CAK45707.1; -; Genomic_DNA.
DR RefSeq; XP_001393110.1; XM_001393073.1.
DR AlphaFoldDB; A2QSA7; -.
DR EnsemblFungi; CAK45707; CAK45707; An08g10020.
DR GeneID; 4983319; -.
DR KEGG; ang:An08g10020; -.
DR VEuPathDB; FungiDB:An08g10020; -.
DR HOGENOM; CLU_042829_1_1_1; -.
DR OrthoDB; 2096057at2759; -.
DR Proteomes; UP000006706; Chromosome 8R.
DR GO; GO:0000700; F:mismatch base pair DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IEA:InterPro.
DR CDD; cd10028; UDG-F2_TDG_MUG; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR InterPro; IPR015637; MUG/TDG.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR PANTHER; PTHR12159; G/T AND G/U MISMATCH-SPECIFIC DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR12159:SF9; G_T MISMATCH-SPECIFIC THYMINE 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.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 140..318
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 38393 MW; 26EB81BDD30471C8 CRC64;
MPLVEDSPRE DIDAIQIPST TPSHDNEAHN EEHYDDNDVP VNRKTSFGGR LNQYFHTAKP
TSSAPPALPS TKQITTSTSS PLKRKRTTPP TALITRITRS RSRSSTSTPT STTTTTSSPR
PRKTPTPTPP TSSAADSLLV DTIPPNLTLL LVGVNPGVLT GVTGYAYAHP SNLFWKLLHW
SGITPIRHPP SDTYKLPELY NIGNTNIVER PTRDASMLSK KEMDAGVPVL EEKVREKRPE
VVCLVGKSIW EAVWRVKVGR GIRKEEFRYG WQDLEMNMGR VGGEGGWEGA RVFVATTTSG
LAAGMSLQEK REVWDELGRW VCERRKVWER EREKVEVGGD DTKVE
//
