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Database: UniProt
Entry: A0A165ZYJ2_EXIGL
LinkDB: A0A165ZYJ2_EXIGL
Original site: A0A165ZYJ2_EXIGL 
ID   A0A165ZYJ2_EXIGL        Unreviewed;       562 AA.
AC   A0A165ZYJ2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN   ORFNames=EXIGLDRAFT_621353 {ECO:0000313|EMBL:KZV86859.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV86859.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV86859.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV86859.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR   EMBL; KV426142; KZV86859.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165ZYJ2; -.
DR   STRING; 1314781.A0A165ZYJ2; -.
DR   InParanoid; A0A165ZYJ2; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR48252; HISTONE DEACETYLASE 2-RELATED; 1.
DR   PANTHER; PTHR48252:SF69; HISTONE DEACETYLASE 3; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN          54..351
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          431..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   562 AA;  61168 MW;  D642E5E339F7465A CRC64;
     MVRSLNSTFS ARQYFDDDGL ETEPTQEYIA SHSRPVVSYY FPRGVGEYHY GERHPMKPHR
     LSLTNALVLG YGLDKQIDQF YCPRAATRAE LEAYHDSDYI DFLARQVSHI TPETQNEMKA
     AIDKYNCVED CPVFTDMYTF CKQYAGASLA GARKLTQGAT DIAINWSGGL HHARRGEASG
     FCYVNDIVMA ILELLRYHPR VLYIDIDIHH GDGVELAFWN SNRVMTVSFH KYTGDFFPGT
     GKLDDNGGGL LGKHFALNVP LQDGIDDESY LTIFRSVIDD TVTAFQPASI VLQCGADSLG
     CDRLGAFNLS IAAHGSCVDF VRRYDLPLLV LGGGGYTIHN VARCWTHETS VLVGRTLPAS
     LPRTTYYEYF APDYALHPPI VTKVENMNSP AALQRIAVHI KNKLRYLQGA PSVQMQEIPP
     DLEGWLADEQ RTADERDEER FGTGGAGESR ADRHRAQNEF YDGDNDVDDD GPRKRGGRPS
     RGTAASTPVP AAAPATGRGR GRGRGRGRGR GRGRGAAAAA AAAAAAAAVA PAGETDTTPA
     TPAESAAPTV PESGAATPMV VD
//
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