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Database: UniProt
Entry: R1EG82_BOTPV
LinkDB: R1EG82_BOTPV
Original site: R1EG82_BOTPV 
ID   R1EG82_BOTPV            Unreviewed;       359 AA.
AC   R1EG82;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Putative zinc-binding alcohol protein {ECO:0000313|EMBL:EOD46497.1};
GN   ORFNames=UCRNP2_6753 {ECO:0000313|EMBL:EOD46497.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD46497.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; KB916452; EOD46497.1; -; Genomic_DNA.
DR   RefSeq; XP_007586012.1; XM_007585950.1.
DR   AlphaFoldDB; R1EG82; -.
DR   STRING; 1287680.R1EG82; -.
DR   KEGG; npa:UCRNP2_6753; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   OMA; HYGCAPG; -.
DR   OrthoDB; 5353053at2759; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 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; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-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.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          20..354
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   359 AA;  38279 MW;  ADA7DF98355F5322 CRC64;
     MATDYKFEGW CGLDPKSAEG NMVWQEFQPK PFAPTDVDIR ISHCGICGSD IHTLRSGWMP
     TPYPCVVGHE IVGRAARVGS AVSRIAVGDR VGVGAQSGSC LKPDCEFCAD GNENHCPGNV
     NTYAGRFPDG GSSYGGYATY NRTPQHFVFK IPDAIASADA APMLCGGITV YSPLKRNGCG
     PGKTVGIVGL GGLGHFGVLF AKALGADKVV VISRTAAKKK DAEAMGADGF VATDEDPDWA
     TTGPHANSLD LIVSTVSSPK MPLIGYLSLL RYRGTFIQVG APEDSLPPIS AFPLILKEIK
     IGGSMIGAPH EIEEMLQLVA QRGLKPWIQE HPMKEANKAI VEFEEGKPRY RFVLVNEGQ
//
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