ID R7Z570_CONA1 Unreviewed; 385 AA.
AC R7Z570;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EON69144.1};
GN ORFNames=W97_08330 {ECO:0000313|EMBL:EON69144.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON69144.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) 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; JH767607; EON69144.1; -; Genomic_DNA.
DR RefSeq; XP_007784461.1; XM_007786271.1.
DR AlphaFoldDB; R7Z570; -.
DR STRING; 1168221.R7Z570; -.
DR GeneID; 19905641; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_3_1; -.
DR OMA; TIGTGQC; -.
DR OrthoDB; 21669at2759; -.
DR Proteomes; UP000016924; 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; cd08282; PFDH_like; 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; PTHR42813:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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:UP000016924};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 25..136
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 185..253
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 385 AA; 41250 MW; 49B61E268738A0CD CRC64;
MKAVHYEGPF KVSVKEVEEP KIEHPDDAII KVTTAAICGS DLHMYQGRTA AESGLIFGHE
NMGIITEVGP GVTLLEKGDR IVLPFNVADG RCRNCEEGKT AFCTGVNPGF AGGAYGYVAM
GPYKGGQAQY LRVPYADFNA LKLPKGTEHE ADFSLLADIF PTGWHGLVLS GFQPGESVAI
FGAGPVGLMA AYSAVIRGAS RVFVVDQVAE RLQAAEKIGC TPINFTESDP VEQIIQKNGG
MVDRAVDAVG YQAVDKSGNK EQPNIVLDQL IMVTRPTGGL GIPGLYVPSD PGAPDEQSGK
GQILISFGKL FEKGLSLGTG QCNVKKYNRY LRDLIISGRA KPSFVVSHEV DIDDASDAYE
KFDKRIDGYT KVLIHPNGPI DKLQG
//
