ID A0A1Y1ZEJ3_9PLEO Unreviewed; 707 AA.
AC A0A1Y1ZEJ3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 08-OCT-2025, entry version 33.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=BCR34DRAFT_626130 {ECO:0000313|EMBL:ORY08636.1};
OS Clohesyomyces aquaticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORY08636.1, ECO:0000313|Proteomes:UP000193144};
RN [1] {ECO:0000313|EMBL:ORY08636.1, ECO:0000313|Proteomes:UP000193144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115471 {ECO:0000313|EMBL:ORY08636.1,
RC ECO:0000313|Proteomes:UP000193144};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORY08636.1}.
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DR EMBL; MCFA01000097; ORY08636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1ZEJ3; -.
DR STRING; 1231657.A0A1Y1ZEJ3; -.
DR OrthoDB; 1918432at2759; -.
DR Proteomes; UP000193144; 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 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:UP000193144};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 41..331
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 389..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..451
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..489
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..543
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..561
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..605
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..653
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..674
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 76579 MW; 54E5972E8DC3051B CRC64;
MAGTGTELAA ETSALNGSAT PKKVAYFYDS DVGNYAYVAG HPMKPHRIRM AHSLIMNYGL
YTKMEIYRAK PASKYEMTQF HTDEYIDFLN KVTPDNMDNF AKEQSKYNVG DDCPVFDGLF
EFCGISAGGT MEGAARLNRG KCDVAVNWAG GLHHAKKSEA SGFCYVNDIV LGIIELLRYK
QRVLYIDIDV HHGDGVEEAF YTTDRVMTVS FHKYGEYFPG TGELRDTGVG NGKNYAVNFP
LRDGITDETY KSIFQPTIQA VMDYYGPEAI VLQCGGDSLS GDRLGCFNLS MEGHANCVKF
VKGFGVPVIV LGGGGYTMRN VARTWAYETG TLVNTHMAKQ LPFNDYYEYF APDYELDVRP
SNMENANSFD YLTKIKNTVI DNIRRTGKPS VEALSETPRV SLQRGMESDD EDEENDLDAD
ENPDVRVTQS QRDQQIENEA EFYEASDDED YKDSLGVRRQ PGAMRRRNIM DYQNSNAAPD
DTGADTPDGL RTMNGETGRT SHLSPAPGRR STSRASSSRP ANTTNGTGPA GTRSNGTSSR
TRTPAVQADE DGDIEMDDPA DEDSHLSPGN AAAGAASTCE TAPAAAGNAN ANPSSSTPAN
PSDAAGPSEA TSNTARADAS RSRSPAGVVT PPESPLTNAG ANASASAGAV PAAAEEDVEM
EESDGERVDD EEKEADTQKE KDEGLREREA EDERAEARTE AAGVKES
//
