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Database: UniProt
Entry: A0A319CU53_9EURO
LinkDB: A0A319CU53_9EURO
Original site: A0A319CU53_9EURO 
ID   A0A319CU53_9EURO        Unreviewed;       275 AA.
AC   A0A319CU53;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=NAD(P)-binding protein {ECO:0000313|EMBL:PYH88280.1};
GN   ORFNames=BO71DRAFT_404006 {ECO:0000313|EMBL:PYH88280.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH88280.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH88280.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH88280.1,
RC   ECO:0000313|Proteomes:UP000247810};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative oxidoreductase. {ECO:0000256|ARBA:ARBA00037096}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; KZ826109; PYH88280.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319CU53; -.
DR   STRING; 1448320.A0A319CU53; -.
DR   Proteomes; UP000247810; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR44196; DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 7B; 1.
DR   PANTHER; PTHR44196:SF1; DEHYDROGENASE_REDUCTASE SDR FAMILY MEMBER 7B; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247810}.
SQ   SEQUENCE   275 AA;  29168 MW;  C1494167EA7F5AC5 CRC64;
     MADRITTVLI IGATSGIGEA FARRFHAAGK QVIITGRRAE RLQQLSQELP GLDTRAWDIT
     DSATLSTHVA DILASHPTLD TVFVNAGIQR SFSMLDSSIS TPESITSEIQ ANLTAPILIS
     RAFLPHLLAR ASAGHPANLL ITSSSIGYFP LPFYPVYCAT KAAIHAFLVS LRAQVGFAAP
     DIQRNLSVVE VVPPYTDTGL DAAHRARIMA MQGGPDKAFA PMPLDEYIDA ALPRILTPGP
     DGKLPKEVGV GFGQVGVDAW RGAFGPGLEG MGLNC
//
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