ID   A0A1B8ARH9_FUSPO        Unreviewed;       356 AA.
AC   A0A1B8ARH9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OBS22954.1};
GN   ORFNames=FPOA_09275 {ECO:0000313|EMBL:OBS22954.1};
OS   Fusarium poae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS22954.1, ECO:0000313|Proteomes:UP000091967};
RN   [1] {ECO:0000313|EMBL:OBS22954.1, ECO:0000313|Proteomes:UP000091967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2516 {ECO:0000313|EMBL:OBS22954.1,
RC   ECO:0000313|Proteomes:UP000091967};
RA   Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA   Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT   "Living apart together: crosstalk between the core and supernumerary
RT   genomes in a fungal plant pathogen.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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:OBS22954.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LYXU01000003; OBS22954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8ARH9; -.
DR   STRING; 36050.A0A1B8ARH9; -.
DR   OMA; CDITTVE; -.
DR   Proteomes; UP000091967; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance 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; PTHR24322; PKSB; 1.
DR   PANTHER; PTHR24322:SF736; RETINOL DEHYDROGENASE 10; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
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   Reference proteome {ECO:0000313|Proteomes:UP000091967}.
SQ   SEQUENCE   356 AA;  38973 MW;  94DC03E4DD56DE29 CRC64;
     MSSILYSPVL GYIQTLNDFV LSPLLSCPLL LTSIYAPDVA NNALSSIAAR LPPEISTTLN
     LTTVNKVLLI WTSLSILRTI NQVLNVMAHN SWRIRPASNW SWTNEIAVVT GGSSGIGLSM
     VHKLSGLGIR VAVFDVQDLP KELQADSRVH FYRCDITTVE SVAEASDAVR RELGHPTILI
     NNAGITSPMP ILNMSESFLR KIMGVNLMSL WYTTQQFLPR MIQLDKGHII TVASIASFVA
     LPTGADYSAT KAGALSFHES LASELKHFYK APNVLTTVVH PNFVRTPLVE GFLDKLQRGG
     VKFLTPDDIA NEVVAQIKRK RGGQLIIPKS ASGISGIRGW PTWMQEILRD MIGKTA
//