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Database: UniProt
Entry: A0A2S5B427_9BASI
LinkDB: A0A2S5B427_9BASI
Original site: A0A2S5B427_9BASI 
ID   A0A2S5B427_9BASI        Unreviewed;       922 AA.
AC   A0A2S5B427;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Histone deacetylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BMF94_5454 {ECO:0000313|EMBL:POY71533.1};
OS   Rhodotorula taiwanensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=741276 {ECO:0000313|EMBL:POY71533.1, ECO:0000313|Proteomes:UP000237144};
RN   [1] {ECO:0000313|EMBL:POY71533.1, ECO:0000313|Proteomes:UP000237144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD1149 {ECO:0000313|EMBL:POY71533.1,
RC   ECO:0000313|Proteomes:UP000237144};
RX   PubMed=29375494;
RA   Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA   Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA   Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA   Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT   "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT   Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL   Front. Microbiol. 8:2528-2528(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:POY71533.1}.
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DR   EMBL; PJQD01000083; POY71533.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5B427; -.
DR   STRING; 741276.A0A2S5B427; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000237144; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR019154; Arb2-like_domain.
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; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF09757; Arb2; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237144}.
FT   DOMAIN          223..537
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          593..846
FT                   /note="Arb2-like"
FT                   /evidence="ECO:0000259|Pfam:PF09757"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          847..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   922 AA;  98549 MW;  415AD86170952FD3 CRC64;
     MDGASQPIFT QAIDPAESQT ETTRSPVAAP VVTVAAPAAA PPPVPFVPET TPGLANATSQ
     LAAAHIQADG AAPASSEPPI ASSSAPLEPG QAVFHPFPEQ DPAGLPLTGF ASIPSRAAVL
     PNAQPYTRPG RYSPPQVQLG KGLSRDPPQR RFVNDHELKA SLTNGNSELA RLPGVVHEDE
     VKTLSVDDLK KMGLGRLPSG FCYSARMTLH APLPRTVDSN DPHPEQPARI TGIFNKLLNG
     GLTSRMVRVQ VREALREEVM LVHSEGHWDR VRATGFQTIE YLETCKEFFE RLSLYVNPDS
     AFCARLSCGG VIEMARAVAE GQIRNGFAIV RPPGHHAEPE EAMGFCFFNN AAVVAKWLRT
     VYGARPGQPL QRDVNGKEIK MERILILDWD VHHGNGTQRA FEDDKDILYI SLHRHGNGFY
     PGGDYGALES AGSGPGRGFS VNIPFMNEGM GDADYLYAFQ QIVMPIAYEF APDLVIVSAG
     YDAAKGDELG KMLVSPDGYA HMTHMLSALA GGKLLLALEG GYNVNSIAES AYACVKVIVG
     DELPAMPSLG SASLAATNTV ADVKRFQAQH WKSMGCAVES DAELTKAGKI ESLSDILKAH
     RVYHLFHEYG LFNVELSSPG LEEAFHDQLL VSEDVYDAEV LLVFMHDLGS MKAAYTAATL
     DTDLERTQLL DTSCEVLDWA MEDHAFGVID VNFLSHLATV KGQGVDPSRD RAKEKELALH
     VWDNIVGMSA AQHVILFGSG AGCHALMDII RNRPAVTDRV RACISILGLE PPPELDAASG
     VRPWYKQQSL VLLPSTHPLH EDARRAGKHQ KKFGNIYRAT AEDESRPTHL LHASMPKVKE
     FVATKIPQDA LDRRPAASST SAGSEGDAGS AGEGAKPAPV GVEANGTAAE AAAAGDGVAP
     AVTALSTSDN GGDVVMNGAG NA
//
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