ID V2WN73_MONRO Unreviewed; 364 AA.
AC V2WN73;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=GroES-like protein {ECO:0000313|EMBL:ESK81635.1};
GN ORFNames=Moror_3256 {ECO:0000313|EMBL:ESK81635.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK81635.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK81635.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK81635.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK81635.1}.
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; AWSO01002331; ESK81635.1; -; Genomic_DNA.
DR RefSeq; XP_007859058.1; XM_007860867.1.
DR AlphaFoldDB; V2WN73; -.
DR KEGG; mrr:Moror_3256; -.
DR HOGENOM; CLU_026673_16_5_1; -.
DR OrthoDB; 1446933at2759; -.
DR Proteomes; UP000017559; 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; 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 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:UP000017559}.
FT DOMAIN 14..360
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 364 AA; 39146 MW; BF4B6B2B6266C79A CRC64;
MIEQKALLLE KQCGALVLGT RPIPKPGSGE LLVKVQAVGL NPVDWKIQRN GFVVKKEDYP
TVLGTDIAGD VETLGEGVDA EKWSKGTRVF FQGKYTADTA GFQQYTLIPA DLAAKIPPKL
AYSEAASIPV AFVAAAYGLF APKPLGGALN PEFDNSVKFT GKSSLVIGGN TSVGQYSELF
ANSSNGVETS TFTAIQLLSK VLGFSQVIAY ASKSSEDYLK SLGATRIIDR HQTTLQDLPS
VIREITTDRP LKVVYDAFGS SEGHDIGFSL LVDDGLFCTV DPSRTDITEN GKRAFGVFGI
VHLPTHRDYG VKLIEQLERL AEEDVIVPNR VLDLPNGLAG IVEGLETVKN DKTGGYKLVA
HPQD
//
