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Database: UniProt
Entry: E4ZQN2_LEPMJ
LinkDB: E4ZQN2_LEPMJ
Original site: E4ZQN2_LEPMJ 
ID   E4ZQN2_LEPMJ            Unreviewed;       391 AA.
AC   E4ZQN2;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   08-NOV-2023, entry version 55.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=LEMA_P037110.1 {ECO:0000313|EMBL:CBX94037.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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DR   EMBL; FP929116; CBX94037.1; -; Genomic_DNA.
DR   RefSeq; XP_003837477.1; XM_003837429.1.
DR   AlphaFoldDB; E4ZQN2; -.
DR   STRING; 985895.E4ZQN2; -.
DR   EnsemblFungi; CBX94037; CBX94037; LEMA_P037110.1.
DR   GeneID; 13285082; -.
DR   eggNOG; KOG1197; Eukaryota.
DR   HOGENOM; CLU_026673_3_1_1; -.
DR   InParanoid; E4ZQN2; -.
DR   OMA; THIATRE; -.
DR   OrthoDB; 148501at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05286; QOR2; 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; IPR047618; QOR-like.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-RELATED; 1.
DR   PANTHER; PTHR48106:SF13; QUINONE OXIDOREDUCTASE-RELATED; 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.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT   DOMAIN          75..389
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   391 AA;  42138 MW;  C528C56345CDCC5A CRC64;
     MTCAGKRGSP AIARGRVFII NEASKNSNTG AIAAVARLPS LKAHQHFTDT PQNIWKRTMA
     SLPKTMKAVL IEQTGGTDVL QYKTDVPVPT PKDGEVLVKN DFIGINYIDT YFRSGVYQPP
     HFPYILGREG AGTVAAVGPN VPSDLPVGAR VAYMGQYAYA EYTAAPSNYT VPIPDSIDSK
     TAAASLLQAL TAVTLIRDAY AVQKGDWILV TAAAGGVGLW LCQLLKAVGA RVIATASTSE
     KRALAKENGA EVLLEYHEDD RDVFVKKVLE VTGGEGVHAV FDSVGKATFD SSLAVVRRKG
     TMVSFGNASG PVEGFSLARL SAKNVKLLRP TLFNYIATRE ELQQASKELW NFIDKDGLKV
     KIHDVYPLSD IVRATEDIQS RKTTGKLVLK P
//
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