ID A0A3D8S6B7_9HELO Unreviewed; 315 AA.
AC A0A3D8S6B7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=GroES-like protein {ECO:0000313|EMBL:RDW81818.1};
GN ORFNames=BP6252_02930 {ECO:0000313|EMBL:RDW81818.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW81818.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW81818.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW81818.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW81818.1}.
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DR EMBL; PDLM01000003; RDW81818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8S6B7; -.
DR STRING; 1849047.A0A3D8S6B7; -.
DR Proteomes; UP000256645; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd05276; p53_inducible_oxidoreductase; 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; IPR014189; Quinone_OxRdtase_PIG3.
DR PANTHER; PTHR48106:SF8; QUINONE OXIDOREDUCTASE PIG3; 1.
DR PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000256645}.
FT DOMAIN 1..312
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 315 AA; 34271 MW; 48C0E4696CA9EB32 CRC64;
MNPDTPKPVP AEGQALIKIH SFGLNRMDLM QREGRYQVPP QAGKILGVEF SGSIEGFGDG
DHEGFEIGDE VFGLAYGGAY AEYLASSTKM LIRKPKEMSW TTAAGIPETW ITATQALHLV
GCFKPGDNVL WHAGASSVSI AGIQLAKAAG AKAIFVTAGS DAKVDFCISI GANAGFNYHT
EDWVTGILRA TNGYGVDVIV DFIGKNYSQG NFEAAAIDGR IVQLASLSGG KLDAGLDIGL
LENKRLRWEG SRLRSRPLEY QQKLRELLVE FALPKFADGT FKVMIEKEFS WKDIQRAHEL
MESNQSKGKI ICHVD
//