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
//