ID   A0A2B7ZNQ3_9EURO        Unreviewed;      1173 AA.
AC   A0A2B7ZNQ3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Histone deacetylase HOS3 {ECO:0000313|EMBL:PGH34642.1};
GN   ORFNames=GX50_02532 {ECO:0000313|EMBL:PGH34642.1};
OS   Emmonsia crescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH34642.1, ECO:0000313|Proteomes:UP000226031};
RN   [1] {ECO:0000313|EMBL:PGH34642.1, ECO:0000313|Proteomes:UP000226031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH34642.1,
RC   ECO:0000313|Proteomes:UP000226031};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PGH34642.1}.
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DR   EMBL; PDND01000036; PGH34642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7ZNQ3; -.
DR   STRING; 73230.A0A2B7ZNQ3; -.
DR   VEuPathDB; FungiDB:EMCG_05203; -.
DR   OrthoDB; 10780at2759; -.
DR   Proteomes; UP000226031; Unassembled WGS sequence.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   CDD; cd09998; HDAC_Hos3; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR47558; HISTONE DEACETYLASE HOS3; 1.
DR   PANTHER; PTHR47558:SF1; HISTONE DEACETYLASE HOS3; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000226031}.
FT   DOMAIN          272..605
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          1..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          958..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1151..1173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..790
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..848
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..884
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..973
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..1023
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1078
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1173 AA;  127296 MW;  181D1E5B2140534A CRC64;
     MDRSQREQPS SAGKFQRRMS NKPPDELTNT FNRLSLATGS VTAGPSSSPS PSPYQSPSRS
     FDRNPSHSRH DSPSRAFANH PSVARRTPSS SSLRDERRVS VPSLQKRSSV SSLRSVQNYS
     GSGVAPPRPS LSRRASSNFL STTSSSMRPK SPLPESPVQP VAPTASSIAR EHFKKELALH
     QSADLQSKTL VIVQDACYGH RFSRPRTSKA GLEQIVERPE RLLASVLGVS TAYIRMGRRH
     DDGQFAPHPD IDLRSLPIPP FQIRKTARTM SLSAPAVTHV HGTKWMDELR VMCEAAESRL
     ALNGKELVRP SSSGKESNLA NPPKFHEGDL YLCPESLNAF EGALGGVCEA VDAVFGPAST
     TRAFVSIRPP GHHCSADYPS GFCWLNNVHV GITHAAMSHG LTHAAIIDFD LHHGDGSQEI
     AWEQNRKAKA ASKNAPPHKK TSIGYFSLHD INSYPCEAGD VNKVRNASVC IDNAHGQSIW
     NVHLEPWKTS ARFWELYNTK YSILLEKTRN FLRSHTQRLL NSQNPSPPKA AIFISAGFDA
     SEWEGAGMQR HKVNVPTDFY AKFTADIVRM AEEEGLGVDG RVISVLEGGY SDRALISGVL
     SHLSGLAEGQ RNTSENGDSR LATEMLSRLG LNDRPEIVLE DHPTFDTEWW QLPLLEELEL
     LANPPPPAPA RKTREKGPPT YCSPTQASVA KIVLPCRDRR SISSQLSAGD GGYLRPPLPV
     IDWATAAYEM SKVLIPTDRQ TVSCQHAELK AENTRTRRDR HSTSNVSELH AVDDRRPMQL
     RERKPKSPSP ELQTPKRPLR ASRRTTIASV SDLPDTSTIE SSGNSNRNSK AVDSQSSRRL
     SVASTAASPV GGINRRGSVE GTSPPSSNGS SGRMLNSRPG TSNGKHTDPL AVKKSRVAIV
     RTSPRKAAVA PQARSIGGGP IPPARSSSIN TDTSERDLTN LSAGIKKLSI KLKVPSLEEH
     AAREEERRKV TTSRSTSRKP QTSKTSRSSS TKSSGKIPRP DTASGQTPPA TATTTTLSAS
     SDPIKQEMPP PLPHVNSDID TVPTPDLSSP PLSAISSSPC VSGWPSDPLT QHTYKEPSKS
     LSPAIKLEND VPSTSHTHMS PPLTPLFLQS SAAQPQITVK PPSSSTTLGY HRTTATQLSN
     QQLPVFTSTS AIPFAPSTAS NAPYFPRQEE HGE
//