ID A0A0F8WDD7_9EURO Unreviewed; 688 AA.
AC A0A0F8WDD7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=ARAM_006691 {ECO:0000313|EMBL:KKK15890.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK15890.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK15890.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK15890.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) 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:KKK15890.1}.
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DR EMBL; JZBS01003148; KKK15890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8WDD7; -.
DR STRING; 308745.A0A0F8WDD7; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000034291; 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:UP000034291}.
FT DOMAIN 38..326
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 435..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 75846 MW; 36E7FDAF52D68835 CRC64;
MASGPPLDPI VNGAGDRGKR VAYFYDSDVG NYAYVSGHPM KPHRIRMTHS LVMNYGLYKK
MEIYRAKPAS KYEMTQFHTD EYIDFLSKVT PDNMDSFAKE QSKYNVGDDC PVFDGLFEFC
GISAGGSMEG AARLNRNKCD IAVNWAGGLH HAKKSEASGF CYVNDIVLGI LELLRFKQRV
LYIDIDVHHG DGVEEAFYTT DRVMTVSFHK YGEYFPGTGE LRDIGVGQGK HYAVNFPLRD
GIDDISYKSI FEPVIRSVME WYRPEAVVLQ CGGDSLSGDR LGCFNLSMRG HANCVNFVKS
FNLPTLILGG GGYTMRNVAR TWAFETGILV GETLGSDLPY NDYYEYFAPD YELNVRPSNM
DNANTKDYLD KIRAQVVENL KRTAFAPSVQ MTDVPRESLV EGMDDEAEAI LDDLDEDENK
DKRFTQRRFD QYIEKTGELS DSEDEDENAA NGIHRKPAHL KRRNQANYRL DVGDSGVESG
MATPQDASSI PDEEMDTGGD AKMTEAPEPE SEAQQTPSAV EASSKAEDPS VREATDMAVD
EKEPAPTSAP ASRLESPKPI DEDTTMEDAG DIAPEPEQEK APAVNEAKEE GKTPAEGTPA
PDNSMREATP QDKAPSEPKE SDDQKGSEGA ASKAEPIEAE KPVATETVLA EEPRAEEAAT
VKTEQEAPET SNEPSTEPQP ETAAKSEE
//
