ID A0A401KEE2_ASPAW Unreviewed; 688 AA.
AC A0A401KEE2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=AAWM_00563 {ECO:0000313|EMBL:GCB17678.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB17678.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB17678.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB17678.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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:GCB17678.1}.
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DR EMBL; BDHI01000001; GCB17678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KEE2; -.
DR STRING; 105351.A0A401KEE2; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:1902494; C:catalytic complex; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR CDD; cd10004; RPD3-like; 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; PTHR10625:SF13; 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 Reference proteome {ECO:0000313|Proteomes:UP000286921}.
FT DOMAIN 39..327
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 436..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 75652 MW; F199349186E1057B CRC64;
MSNSLAPLDP ITNGPADRNK KVAYFYDSDV GNYAYVSGHP MKPHRIRMAH SLVMNYGLYK
KMEIYRAKPA SKYEMTQFHT DEYIDFLSKV TPDNMDSFAK EQSKYNVGDD CPVFDGLFEF
CGISAGGSME GAARLNRNKC DIAVNWAGGL HHAKKSEASG FCYVNDIVLG ILELLRFKQR
VLYVDIDVHH GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG ELRDIGVGQG KHYAVNFPLR
DGIDDVSYKS IFEPVIKSVM EWYRPEAVVL QCGGDSLSGD RLGCFNLSMR GHANCVNFVK
SFNLPTMILG GGGYTMRNVA RTWAFETGIL VGDTLGAELP YNDYYEYFAP DYELDVRPSN
MDNANTKEYL DKIRTQVVEN LKRTAFAPSV QMTEVPREPL VEGMDDEADA ILDDLDEDEN
KDKRFTKRRF DQYIEKPGEL SDSDDEELAG ANGVRRQPNA LKRRNQVNYR NLDVNDSGLE
SGMATPQDAS SLPDDDMDTT ADAKMTEAPE PETEAQATPS AADAPSRADE ASATEQTEMA
VDGPETTAAS APISRQPSPK PQDEDTTMVD AGEVAPETEK SEAAPEGAAE EEEEKKKPSE
ETPAADKPAT EETPATKDES PAKETTEAAD TAEAETKPAE ASEPSETKDK TPEAAKDESG
EAKSKEPSAE AAGATEAEKT EEASKTEE
//
