ID   A0A0M8MR81_9HYPO        Unreviewed;       483 AA.
AC   A0A0M8MR81;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   03-MAY-2023, entry version 23.
DE   SubName: Full=Quinone oxidoreductase-like protein 2-like protein {ECO:0000313|EMBL:KOS17686.1};
GN   ORFNames=ESCO_002519 {ECO:0000313|EMBL:KOS17686.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS17686.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS17686.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS17686.1}.
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; LGSR01000022; KOS17686.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8MR81; -.
DR   STRING; 150374.A0A0M8MR81; -.
DR   OrthoDB; 102245at2759; -.
DR   Proteomes; UP000053831; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd08241; QOR1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 3.
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   PANTHER; PTHR43677:SF4; QUINONE OXIDOREDUCTASE-LIKE PROTEIN 2; 1.
DR   PANTHER; PTHR43677; SHORT-CHAIN DEHYDROGENASE/REDUCTASE; 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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831}.
FT   DOMAIN          11..472
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          97..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..145
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  52749 MW;  CB39311F45EEB501 CRC64;
     MRAVQVRRYV KSPQDLTVKR LPDPIPRPDE YTIEISAAAA NLSDLLQIQG HYQNQPPFPF
     IAGSEFAGTV VATPQRRRLK TIHLRRRRII KRDDNDAISN NGNIIINNNT NNISNVNSSS
     SSSNNDDDDD SRDGDDDDDE TESNDSSESG TTRESKTRYV DGRDSFDDEY HEEEVDSGSE
     YEPFPVGTRV FGAAQGAFAT KVCVPAIGLR HIPDGWSFRS AAGLFSAVPT AYAALVARAK
     VREGDYVLVH AAAGSVGLAS IQIAKAYGAR VIAMVSPARA APRPRTPMTP MTPPSGHRAG
     FSAAPAHPAA SSPRGAVTTT VNRKSRAALL FGADHVLSYD EPDWPAKVRA LTPRERGVDV
     VIDPVGLVER SIKCTAWNGR VLVVGFAGGA AERIAAAGVL LKNISLMGVY WGGYYMHERH
     VVDEVWEGIM RLVADGKIKP MEYCDEEFVG LVQVKEALLK LSKRETWGKV VIRIPKERMK
     SKL
//