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Database: UniProt
Entry: D4CZY6_TRIVH
LinkDB: D4CZY6_TRIVH
Original site: D4CZY6_TRIVH 
ID   D4CZY6_TRIVH            Unreviewed;       345 AA.
AC   D4CZY6;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   03-MAY-2023, entry version 44.
DE   SubName: Full=Zinc alcohol dehydrogenase, putative {ECO:0000313|EMBL:EFE44829.1};
GN   ORFNames=TRV_00380 {ECO:0000313|EMBL:EFE44829.1};
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE44829.1, ECO:0000313|Proteomes:UP000008383};
RN   [1] {ECO:0000313|Proteomes:UP000008383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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:EFE44829.1}.
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DR   EMBL; ACYE01000020; EFE44829.1; -; Genomic_DNA.
DR   RefSeq; XP_003025440.1; XM_003025394.1.
DR   AlphaFoldDB; D4CZY6; -.
DR   GeneID; 9581666; -.
DR   KEGG; tve:TRV_00380; -.
DR   HOGENOM; CLU_026673_3_3_1; -.
DR   OrthoDB; 5473274at2759; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd05289; MDR_like_2; 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   PANTHER; PTHR11695; ALCOHOL DEHYDROGENASE RELATED; 1.
DR   PANTHER; PTHR11695:SF294; RETICULON-4-INTERACTING PROTEIN 1, MITOCHONDRIAL; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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;
FT   DOMAIN          10..341
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   345 AA;  37080 MW;  6934DA13A7C097C0 CRC64;
     MLSLNTPSYS APSGYQLSEL PKPVLEDSND VIIRVHAASI NPIDVKKANG MLKMAMADKF
     PYKIGYDCAG TVEEAGSSVS HLKAGDEIYT RLPEASRAKD VALKPPSLSF ADAASIPLAA
     MTALQALRRY DGDLAGKTVL VPAGLGGTGM FACQLAKHAF KAGKVITTVS TSKIPKVKEL
     LGDDTVDEII DYTKVNPKDA IPPGTVDFLF DTVANAMEYL SLMRPKTGHI ISVSTAPSGD
     QLQASSLMQL PHRPALPMPI KLALNAMDSI RKFRARRYGV TYSYMFLESS CKDLEELRDL
     VESGKLRTVV GTTASLRDLQ AVREACQIVY SGRGGLGKVV IKVVD
//
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