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Database: UniProt
Entry: A0A074X9J0_AURPU
LinkDB: A0A074X9J0_AURPU
Original site: A0A074X9J0_AURPU 
ID   A0A074X9J0_AURPU        Unreviewed;       669 AA.
AC   A0A074X9J0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN   ORFNames=M438DRAFT_399901 {ECO:0000313|EMBL:KEQ80404.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ80404.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ80404.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ80404.1,
RC   ECO:0000313|Proteomes:UP000030706};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR   EMBL; KL584998; KEQ80404.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074X9J0; -.
DR   STRING; 1043002.A0A074X9J0; -.
DR   HOGENOM; CLU_007727_0_1_1; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000030706; 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:UP000030706}.
FT   DOMAIN          42..332
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          392..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..429
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..661
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   669 AA;  73577 MW;  52843364357CFE33 CRC64;
     MANSAQYGPP LDPPRATNGG RPKKVAYFYD SDVGNYAYNA GHPMKPHRIR MAHSLIMNYG
     LYKKMEIYRA KPASKYEMTQ FHTDEYVDFL SKVTPDNMDS YAKEQGKYNV GDDCPVFDGL
     FEYCGISAGG SMEGAARLNR QKCDVAVNWA GGLHHAKKSE ASGFCYINDI VLGIIELLRF
     KSRVLYIDID VHHGDGVEEA FYSTDRVMTC SFHKYGEYFP GTGELRDIGV GNGKNYAVNF
     PLRDGMDDVA YKSVFEPIIA KIMEFFRPDA VVLQCGGDSL SGDRLGCFNL SMRGHANCVK
     YVKSFNLPTL VLGGGGYTMR NVARTWAYET GQLVGQEMGP ELPYTDYYEY YSPDFELDVR
     PSNMDNANSP EYLEKIKLQV FENLSRTRFA PSVQMTDVPR SPLVVQPNEN DPDNEGDTED
     LDEREQRLDD KDDDENPDSR YTERKWDARI ERDDEFEDSD DEEMDALLGV KKQPGAEPRR
     PRITDHKNPY ADMAEGSLAE SGTTTPLDTT LPPAAAQADQ MVVDRAQAAN AAVGDAIMAA
     KASEDPHAVQ PAMGEEVASN GTQRARSPQN APSTTAQAPA AEPEDVEMGE DDVAEPPANA
     PNSNNTQAGA GPTATPPPDP TVAETTTTAP EDVEMGDGAA EAKEEGRQER DAEDVQGEMK
     REGEAGGIN
//
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