ID A0A2S6BXP3_9PEZI Unreviewed; 207 AA.
AC A0A2S6BXP3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PPJ52242.1};
GN ORFNames=CBER1_10511 {ECO:0000313|EMBL:PPJ52242.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ52242.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ52242.1}.
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DR EMBL; PNEN01001711; PPJ52242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6BXP3; -.
DR OrthoDB; 666181at2759; -.
DR Proteomes; UP000237631; 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; PTHR43544:SF7; LD36273P; 1.
DR PANTHER; PTHR43544; SHORT-CHAIN DEHYDROGENASE/REDUCTASE; 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:UP000237631}.
SQ SEQUENCE 207 AA; 22289 MW; E003B96F4FBA249E CRC64;
MIDASGDRIV NIVIKDVTNE DSVQGGVSEI QKYTSSLDVL VNNAGQGSFT PDGVRSVKAA
DLREILNTNL VSAQVVTAAF LPLLESGKDK KVINISSTLG SISRIPLHAK TPTHAYNITK
AGMNMLTALY AQDHEDFTFL AVSPGWLKTD LGSQSADLPV EVGVSSLKDI ILKADRSQNG
KFLNIHVPGW KKEEKGPEVY EGGEVPW
//
