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Database: UniProt
Entry: A0A2H3BV84_9AGAR
LinkDB: A0A2H3BV84_9AGAR
Original site: A0A2H3BV84_9AGAR 
ID   A0A2H3BV84_9AGAR        Unreviewed;       166 AA.
AC   A0A2H3BV84;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=GroES-like protein {ECO:0000313|EMBL:PBK73510.1};
GN   ORFNames=ARMSODRAFT_971943 {ECO:0000313|EMBL:PBK73510.1};
OS   Armillaria solidipes.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK73510.1, ECO:0000313|Proteomes:UP000218334};
RN   [1] {ECO:0000313|Proteomes:UP000218334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX   PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA   Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA   Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA   Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA   Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA   Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA   Gueldener U., Muensterkoetter M., Nagy L.G.;
RT   "Genome expansion and lineage-specific genetic innovations in the forest
RT   pathogenic fungi Armillaria.";
RL   Nat. Ecol. Evol. 1:1931-1941(2017).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; KZ293420; PBK73510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3BV84; -.
DR   STRING; 1076256.A0A2H3BV84; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000218334; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218334};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          39..86
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
SQ   SEQUENCE   166 AA;  17619 MW;  E09E9E61F522E237 CRC64;
     MAQPISNKAC VPVGPEMIEF KDVPVPSVGR HDVLVRVEAS DRETLTKPVV MGHEAAGIVV
     QVGEVVVDVA VGDRVAIEPI FFCKRSGLIR ILTRDGRAIG KPTWILQTLT EKLCLTFGGK
     AFPINPDTFN LGQAEQGSSD CVGGIVAGDF GAFNVKDETV GFANLA
//
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