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Database: UniProt
Entry: E3S2Y7_PYRTT
LinkDB: E3S2Y7_PYRTT
Original site: E3S2Y7_PYRTT 
ID   E3S2Y7_PYRTT            Unreviewed;       379 AA.
AC   E3S2Y7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=PTT_16764 {ECO:0000313|EMBL:EFQ87661.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ87661.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ87661.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; GL536874; EFQ87661.1; -; Genomic_DNA.
DR   RefSeq; XP_003304242.1; XM_003304194.1.
DR   AlphaFoldDB; E3S2Y7; -.
DR   EnsemblFungi; EFQ87661; EFQ87661; PTT_16764.
DR   KEGG; pte:PTT_16764; -.
DR   eggNOG; KOG1198; Eukaryota.
DR   HOGENOM; CLU_026673_16_1_1; -.
DR   OrthoDB; 2267374at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   CDD; cd08249; enoyl_reductase_like; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR047122; Trans-enoyl_RdTase-like.
DR   PANTHER; PTHR45348; HYPOTHETICAL OXIDOREDUCTASE (EUROFUNG); 1.
DR   PANTHER; PTHR45348:SF2; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C2E1P3.01; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..379
FT                   /note="Enoyl reductase (ER) domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003179663"
FT   DOMAIN          41..375
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   379 AA;  40833 MW;  834D343217DA0C9F CRC64;
     MTIIFLLSIM LDELGSYPDS EIYPMATTFT LPATQTAIVL GEADRPLIKR DSPCPKLSSN
     QIVVRTKAVA LNPSDTKMKG GFAVPYGVLG ADFAGTVVDV GSDVTEVAIG DTICGAQNIM
     FNSTPEQAAF AEYNWTRGGI WMKVPNSYTI EAAASLPVGV STAGLAMKLL GIPLPGEPAT
     ESATVLVYGG STATATIAMQ LLRLSGYTPI ATCSPKHFDL AKSNGAEEVF DYRDVDCAEE
     IRRYTKNNLK YALDCIVNVE STTACFKAIG RAGGKYVSLD PFPTHAASRK VVHTDFVVGP
     LIFGEGCTWP EPYGRPPSED LRQYGIKLWQ IASRLLNEGK LRHHPLRIMD GGFDTIMDGL
     QLVSKGQLSG EKIVVRLLN
//
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