ID A0AAE8M135_9HYPO Unreviewed; 651 AA.
AC A0AAE8M135;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=FTOL_02084 {ECO:0000313|EMBL:SPJ72356.1};
OS Fusarium torulosum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=33205 {ECO:0000313|EMBL:SPJ72356.1, ECO:0000313|Proteomes:UP001187734};
RN [1] {ECO:0000313|EMBL:SPJ72356.1}
RP NUCLEOTIDE SEQUENCE.
RA Guldener U.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00061569}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:SPJ72356.1}.
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DR EMBL; ONZP01000057; SPJ72356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAE8M135; -.
DR Proteomes; UP001187734; Unassembled WGS sequence.
DR GO; GO:0033698; C:Rpd3L complex; IEA:UniProtKB-ARBA.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; IEA:TreeGrafter.
DR GO; GO:0032221; C:Rpd3S complex; IEA:UniProtKB-ARBA.
DR GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; IEA:UniProtKB-EC.
DR GO; GO:0031507; P:heterochromatin formation; IEA:TreeGrafter.
DR CDD; cd10004; RPD3-like; 1.
DR FunFam; 3.40.800.20:FF:000001; Histone deacetylase; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR003084; HDAC_I/II.
DR InterPro; IPR000286; HDACs.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF10; HISTONE DEACETYLASE HDAC1; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP001187734};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 39..327
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 384..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 72515 MW; 6977DC1B30F64D12 CRC64;
MGDDIRVELG SVALNASSPK KVAYFYDSDI GNYAYVTGHP MKPHRIRLAH SLIMQYNLYQ
KMEIYRAKPA TRGEMTQFHT DDYIDFLQKV TPDNMDSFMR EQGKYNVGDD CPVFDGLFEF
CGISAGGSME GAARLNRQKC DIAINWAGGL HHAKKCEASG FCYVNDIVLG ILELLRFKKR
VLYIDIDVHH GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG ELRDTGIGQG KNYAVNFPLR
DGITDVSYRS IFQPVIENVM KYYQPEAVVL QCGGDSLSGD RLGCFNLSMD GHANCVNFVK
SFNLPTLVLG GGGYTMRNVA RTWAFETGVL VGKEMERTLP YNEYYEYYAP DFELNVRSSN
MENSNSREYL EKITSAVIDN LRQTGPAPSV QLQDVPRKPF GGMTDEEEAE LDDLDEDENK
DVRMSEHRWD KHVEHDNEFE PSDDDDMARA NGATRQNGNK RSFTDYRKGE MDVDNPDAPP
AKVTNGTPAD ESVEEHVAED THDINDDTID DISAHGQADK DLPEKEVEKP KEAAKEPETT
KVDGDGDVGM EDSAAAEETT TIKTEEIEPE APAEPPVSTE KPTQDEPATQ ETADTATKES
ASEPKPTEEA AEKATVAPEK AQSDQPVDAM DVDVEKDKPE QPTEKSKSPA N
//
