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Database: UniProt
Entry: A0A2D3VJK5_9PEZI
LinkDB: A0A2D3VJK5_9PEZI
Original site: A0A2D3VJK5_9PEZI 
ID   A0A2D3VJK5_9PEZI        Unreviewed;       363 AA.
AC   A0A2D3VJK5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Probable alcohol dehydrogenase, class V {ECO:0000313|EMBL:CZT22269.1};
GN   ORFNames=RCC_08138 {ECO:0000313|EMBL:CZT22269.1};
OS   Ramularia collo-cygni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX   NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT22269.1, ECO:0000313|Proteomes:UP000225277};
RN   [1] {ECO:0000313|EMBL:CZT22269.1, ECO:0000313|Proteomes:UP000225277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URUG2 {ECO:0000313|EMBL:CZT22269.1,
RC   ECO:0000313|Proteomes:UP000225277};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; FJUY01000013; CZT22269.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D3VJK5; -.
DR   STRING; 112498.A0A2D3VJK5; -.
DR   OrthoDB; 5353053at2759; -.
DR   Proteomes; UP000225277; 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   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   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:UP000225277};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          39..156
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          197..323
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   363 AA;  39566 MW;  01E46D3C42D697A5 CRC64;
     MAAKEDYKFA GWMGIDKESA KGNMVWQEFP DDRKPFEETD VDIQITHSGI CGSDLHTLRS
     GWGPTPYPVC VGHEIVGKAV RVGSKVEKGI KVGDRVGVGA QNLSCLKPDC EECSSGLENH
     CTQTTNTFAG KYPDGSTSYG GYADYHRAPS HFVFKIPEGI DSADAAPMLC GGITVYSPLK
     NNDCGPGKKV GIIGVGGLGH FGVLYAKALG ADKVVGISRR NDKREDVLKM GADEYIATEE
     DKDWAKKHSR SLDLIICTVS SPSMPLMQYL QLLRVKGTFI QVGAPEDKLP DMNAFAFIAK
     GVKFGGSMIG PPAQIEEMLK FTAEKNVKPW INKYSMKEAN KAIVDFEAGK ARYRISLVNE
     HFL
//
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