ID M7WZI6_RHOT1 Unreviewed; 601 AA.
AC M7WZI6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=RHTO_07240 {ECO:0000313|EMBL:EMS23506.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS23506.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS23506.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS23506.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR EMBL; KB722647; EMS23506.1; -; Genomic_DNA.
DR RefSeq; XP_016274625.1; XM_016420898.1.
DR AlphaFoldDB; M7WZI6; -.
DR GeneID; 27371253; -.
DR eggNOG; KOG1342; Eukaryota.
DR HOGENOM; CLU_007727_0_2_1; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000016926; 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 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}.
FT DOMAIN 33..331
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 389..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 65036 MW; EEB3CD39A2CDBEA1 CRC64;
MSGILTPIAG EAKKRTCYFF DSDIGNYHYG PSHPMKPHRV RMTHSLVMNY GLYKKMEIFR
AKPATRKEMA QFHTDEYVDF LARVTPDLVE AAAEGSGGPK VAGLAREMGR FNLGDDCPVF
DGLFEYCSIS AGGSMEGAAR LSRDKCDIAI NWAGGLHHAK KAEASGFCYV NDIVLGILEL
LRYHPRVLYV DIDVHHGDGV EEAFYTTDRV MTASFHKYGE FFPGTGDLKD IGYGKGRNYS
VNVPLRDGIT DENYRSVFEP VISQIMEWYR PSAVVLQCGG DSLSGDRLGT LNLSMRGHAN
CVQFIKSFGL PLLVLGGGGY TIRNVARTWA FETGLAAGME LGVNIPMNEY YEYFGPTYRL
DVPQSNTEDM NTSEYLEKIK AQVFENLRQT GGGSAPSVQS QPIPRTAMDE DDDLEEDERD
PNVRRHQAEV DRRIQRDDEF SDSEDEGEGG RRDRQSHRRE SPKARSKSPA PAAPADAASA
APAIPLETTS ASAAAPTDAP VTTTQAPLPA NITCGAEEPL APLKPAGESS SNATEAALAE
TAPEAEEKAG AIAEANGDAI GGTVEMPVQG TSAARMTTTA GPGEDDARAE DVEMQEASGS
A
//
