ID   A7TRW5_VANPO            Unreviewed;       518 AA.
AC   A7TRW5;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN   ORFNames=Kpol_376p15 {ECO:0000313|EMBL:EDO15002.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO15002.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR   EMBL; DS480489; EDO15002.1; -; Genomic_DNA.
DR   RefSeq; XP_001642860.1; XM_001642810.1.
DR   AlphaFoldDB; A7TRW5; -.
DR   STRING; 436907.A7TRW5; -.
DR   GeneID; 5543047; -.
DR   KEGG; vpo:Kpol_376p15; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_7_8_1; -.
DR   InParanoid; A7TRW5; -.
DR   OMA; MSRFYTY; -.
DR   OrthoDB; 5478215at2759; -.
DR   PhylomeDB; A7TRW5; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProt.
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; PTHR10625:SF39; HISTONE DEACETYLASE 8; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000267}.
FT   DOMAIN          22..401
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          427..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..446
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  59924 MW;  819A4342E8D047D9 CRC64;
     MQYKLVISTS RFQSQVADLL PCNKYKKSQL TYSLLVSYGL LDGFDVIIDD PCCNKKDLLQ
     FHSRDYIDLL LDPVYNRIIQ YDDDESKWSQ LHPYIRDWLD SHPEEVPTSG MIEKRAGLLE
     FYKKYNRFKK KRSISEAFSE SESESESGSG SGSEANEYFQ INNSRERQQD VYKKFNLEGD
     CPLFSFLPLY CEVISGASLM LSDFIEKSSS QRTIAINWDG GRHHAIKNKA SGFCYINDIV
     ILIQKLRKKG ISKVSYIDFD LHHGDGVEKA FRYSSNIQTI SMHMYEPGFF PCTGSLEDTL
     NGKNIVNVPL YHGVDDNYMT EIVNELIKPL IERHSPEVLV IQCGGDGLIG DKFEEWQLTI
     SGLTRNIQNL IEWFPKSDII LLGGGGYNEL VMSRFYTYLT YQIVKKYGSK PIIDLCIPRR
     TITNASDKEE FNSDREDEDE DGDGDGDVLL PEHEFIELYS KEFYKFWVYE LESSNKRKTL
     KNYNDARYLD KLLKFYGMSK PKTDNCSSEI NFRGKREE
//