ID   A0A072PJ51_9EURO        Unreviewed;      1066 AA.
AC   A0A072PJ51;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Histone deacetylase domain-containing protein {ECO:0000259|Pfam:PF00850};
GN   ORFNames=A1O9_04759 {ECO:0000313|EMBL:KEF59911.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF59911.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF59911.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF59911.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) 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:KEF59911.1}.
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DR   EMBL; AMGV01000003; KEF59911.1; -; Genomic_DNA.
DR   RefSeq; XP_013262501.1; XM_013407047.1.
DR   AlphaFoldDB; A0A072PJ51; -.
DR   STRING; 1182545.A0A072PJ51; -.
DR   GeneID; 25279688; -.
DR   VEuPathDB; FungiDB:A1O9_04759; -.
DR   HOGENOM; CLU_001880_0_0_1; -.
DR   OrthoDB; 10780at2759; -.
DR   Proteomes; UP000027920; 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:UP000027920}.
FT   DOMAIN          115..447
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          509..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          637..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..1066
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..793
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..839
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..877
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1066 AA;  116336 MW;  FB31A405C168F511 CRC64;
     MNPPERPPVT ANSVAKEYFG KELEAHATLQ SPVVVIVHDA CYGHRFARPR STKNALASIV
     ERPERIHATL LGAATAYVRL GGRHQYGRYM PRPKHDRADV KDVPFQIRKT SRTLPLSHPA
     VTYVHGAKWM EELQIMCDSA EAKLTMNGKE LVRPTGYGKD EGGNALPKLH EGDLYLCRES
     LDALQGCLGG VCDAIDTIFS SNPTKRAFVC IRPPGHHCSS NFPSGFCWLN NVHVGISYAA
     MNHGLTHAVI IDFDLHHGDG SQNVAWDQNR KAQNLPKNAA AHRKTPIGYY SLHDINSYPC
     EWGDEEKVRN ASLCIENAHG QSIWNVHLES WRSHEEFWKL YETKYLVLLE KARVFLRHHS
     AKLRAAGHQE PKAAIFISAG FDASEWESAG MQRHSVNVPT EFYARITADL VKLSQEEDTG
     VEGRLISVLE GGYSDRALTS GVLSHICGLA TDAAPSLPSS SDVSDTPKFQ TINNWIPENS
     ALANGPTLSF TPDWWALDNL EELEAAVAGR QPAGPKSLQD KTGNYSSPTH ASTLKMTENA
     RDRHSLSALQ ARLSLESQYV PPPPDVSWAI ASYELSRVII PCDRQTLSCT HEELNAEATK
     VRRERQSNIG VVAPSDERMQ LRDRRTKVQA AEFGGVRTSS RNGNRRTTIA AVSELPDPTT
     PVPAMPNGRP RRRSSDASSI LSGFQGMKLS DDTSATSVKL PVNGTSHASR APPSVPEKAA
     KPVAVKKTRA APTTKAPVKP KTSPRKPRAT PPIPVNRASA AKSESLNDSN GVNQEFTASG
     RGPSTSSLDS GNAGSKPDDM DVLANGMKKI SIKLKVPTPE EHAAKQQKIL EEKQKKPRAT
     RKPALPKPVK PTKPIQPTSN DTLVSIQPRP TQNPKTEGPA VIDTTAIQNG PPVVTAPVAE
     PVNPSFTSTR VFPALPPVGS LPLGPNQNHD VLNDTALARM QSQFPPSTAL NVEPLRSSNA
     THIDQPPPPM YRQDPAISGN HPVEPVIYSS NTILQQVAPV QGAPWPPSTT MMTPKRSKED
     LPVFTSHSPI PFSAPQRAKG NPTGPESSIW DIPETPHQQY MREDTF
//