ID A0A1J9RLJ0_9PEZI Unreviewed; 394 AA.
AC A0A1J9RLJ0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OJD29383.1};
GN ORFNames=BKCO1_8200011 {ECO:0000313|EMBL:OJD29383.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD29383.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD29383.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD29383.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-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}.
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:OJD29383.1}.
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DR EMBL; MNUE01000082; OJD29383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9RLJ0; -.
DR STRING; 236234.A0A1J9RLJ0; -.
DR OrthoDB; 2619844at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08278; benzyl_alcohol_DH; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF2; PKS_ER DOMAIN-CONTAINING PROTEIN-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:UP000183809};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 31..113
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 220..355
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT REGION 131..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 41951 MW; 0A7079C370ABD71C CRC64;
MTTARAIVSR APLNDGGWKI EDVKVRDVGD DELLVRIVAS GICHTDILFG GLKEGPGVMY
PSVKGHEGAG YIEKIGKNVS VAAAGDPVLL SFTFCDSCQI CQAGHPAHCV RFGELNFGGC
PCFHSSSSSH SSDSSTSSAS PSSSPSTPDL QGSFFGQSSF ASRTIVKATS VVNVRGLVRD
DEELRLFSPL GCGIQTGSGT IVNVAQAGPQ DTVAVLGLGG VGLSAIMAAK LRGCKTIIGI
DKMSDRESIA RQLGATHFID TSKLADLFDI VSAVQDVTDG YGTSVTVDTT GFLPLIERAM
DFTRLKGKLI QVGSTPFDAK LDIQIFPFMV SGKQYIGAVE GDVVPAKYVP QMIEWYRAGK
FPVEKLVKFY KADEWERAVE EMHSGHTVKA VITW
//
