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Database: UniProt
Entry: A0A094BWY7_9PEZI
LinkDB: A0A094BWY7_9PEZI
Original site: A0A094BWY7_9PEZI 
ID   A0A094BWY7_9PEZI        Unreviewed;       436 AA.
AC   A0A094BWY7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=V494_00541 {ECO:0000313|EMBL:KFY46219.1};
OS   Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY46219.1, ECO:0000313|Proteomes:UP000029288};
RN   [1] {ECO:0000313|EMBL:KFY46219.1, ECO:0000313|Proteomes:UP000029288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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:KFY46219.1}.
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DR   EMBL; JPJW01000155; KFY46219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094BWY7; -.
DR   STRING; 1420907.A0A094BWY7; -.
DR   HOGENOM; CLU_026673_16_2_1; -.
DR   OrthoDB; 1746729at2759; -.
DR   Proteomes; UP000029288; Unassembled WGS sequence.
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; 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; PTHR43482; PROTEIN AST1-RELATED; 1.
DR   PANTHER; PTHR43482:SF2; ZINC-BINDING DEHYDROGENASE FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15030)-RELATED; 1.
DR   Pfam; PF08240; ADH_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:UP000029288}.
FT   DOMAIN          59..433
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  47078 MW;  201091ECF8ADCEA7 CRC64;
     MTTTSTSTTT TSTSPSTKRQ HHGNDDVVDK PRKRRQTIRE EPAVERFQVT HQEVLLLHGV
     KQRYTHTTKY EIPQIKNDGE MLVKVSVIGL NPIDWKASDF GWGLPTLPCI SGRDLAGTIV
     KTPKRESRFK VGDKVIAVST DYRDSRKSAY QEYAIASDHN VCRLPASISA VDAAPVGVAY
     VAAALMLGVC IGLDFSHVNG PDLYTISRKL DPESVPKDIK AEVFNDSITP ALRPKKGDWL
     AIWGGSSATG CIALQLAKLA GLRVVCILDV ARNGARMLKL GADLLIDRLD TERAVEIVRS
     VTGGQLTWGI DTRGKESAGL LARAMAASEA AAPSDEKEEK KDDGKEKALG HLVALTGRPS
     APTPGIQYHT LPIKLFHEAA PVGEALMVWL ERLFEEGTLH PPPIEVASGG LQGVNDALDR
     LREGAAGGER IVVPLA
//
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