ID A0A166J6A4_9AGAM Unreviewed; 564 AA.
AC A0A166J6A4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=FIBSPDRAFT_826864 {ECO:0000313|EMBL:KZP20539.1},
GN FIBSPDRAFT_826870 {ECO:0000313|EMBL:KZP20541.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP20539.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP20539.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP20539.1,
RC ECO:0000313|Proteomes:UP000076532};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV417554; KZP20539.1; -; Genomic_DNA.
DR EMBL; KV417554; KZP20541.1; -; Genomic_DNA.
DR STRING; 436010.A0A166J6A4; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000076532; 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 CDD; cd09991; HDAC_classI; 1.
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:UP000076532}.
FT DOMAIN 23..312
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 373..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 63050 MW; BB14C8A1204E7316 CRC64;
MSKRRVAYSY DNDVGAFTYA TTHPMKPHRM RITHDLISAY GMLEQMHVIR PKRASPEAMT
AFHTDEYVNF LSRVTPETHM ELTYHQTRFL TLDDNPAFEG LFEFCSMSAG GSIDAAKRLA
SGSADIAINW AGGLHHAKKR EASGFCYIND IVLGILELLR TYARVLYVDI DCHHGDGVEE
AFYTTDRVMT CSIHKHGDFF PGTGTQNDIG KGKGKGYSVN IPLQDGITDE SFRSIFDPVI
GKILDVYQPS VVVLQCGADS LAGDKLGCFN LTMQGHAYCV QYFRKVNLPL IMLGGGGYTV
KNVARAWTYE TACALGIEDT LDSNLPWTEF FDWFGPRYQL EVCGNNMVDA NLKDNALDRI
RTAAMKQLND LQPAPSVGMH DVPRESVGQH LGFGKDEEEG RDALDESVAQ HARLVYNLQE
AELASDDSDA DSHRWDSDDS MGGSTSRRRR RHPRPGKKRM SIINNQVYDI PSYENGFEYA
VSGRPETRRR FFQSVARWDT RYQKVMIPGH AAQALPRAVP HSRSRSEESE DDGEEDDAGQ
NGVLGKRATQ SDYEDDEAGS GMDE
//