ID   A3LR32_PICST            Unreviewed;       807 AA.
AC   A3LR32;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN   ORFNames=PICST_71431 {ECO:0000313|EMBL:ABN65316.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65316.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN65316.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events. {ECO:0000256|PIRNR:PIRNR037919}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037919};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR037919}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037919}.
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DR   EMBL; CP000497; ABN65316.2; -; Genomic_DNA.
DR   RefSeq; XP_001383345.2; XM_001383308.1.
DR   AlphaFoldDB; A3LR32; -.
DR   STRING; 322104.A3LR32; -.
DR   ESTHER; picst-a3lr32; Arb2_domain.
DR   GeneID; 4838284; -.
DR   KEGG; pic:PICST_71431; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_007727_4_0_1; -.
DR   InParanoid; A3LR32; -.
DR   OMA; FVSPACY; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000002258; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; 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; IPR017321; Hist_deAcase_II_yeast.
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   PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037919};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037919};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037919};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW   Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT   DOMAIN          128..438
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          503..799
FT                   /note="Arb2-like"
FT                   /evidence="ECO:0000259|Pfam:PF09757"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   807 AA;  89455 MW;  AF6E4974DE1C5DEE CRC64;
     MSEEPTGVAP ESAPKKRLLE DADTDTKSTS NTSVSGTVEN STDINFHPDT NSTEASKGNP
     DQIPVSNGDD HKRIKLEPKV GNESSIVVVP PTKPQLFYSP LKTGLVYDVR MRYHAKIFTS
     YFEYIDPHPE DPRRIYRIYK KLAEAGLIVD SSLSGVEDIG PLMVKIPIRE ATAEEILEVH
     SESHLKFIQS TETMSRERLL EETEKGDSIY VNNDSYFSAK LSCGGTIEAC KAVIEGRVKN
     SLAIVRPPGH HAEPETPGGF CLFSNVAVAA KNILKAYPES VRKIVIVDWD IHHGNGTQKS
     FYDDPRVLYI SLHRYENGRF YPGTKYGGAD QVGEKDGEGY NLNIPWRNPG MHDGDYIYAF
     NRVVLPVILE FDPDLIIVSS GFDAADGDII GGCHVTPAGY GYMTHLLKGI AKGKLAVILE
     GGYNLDSISK SALGVAKVLV GEPPEATVSM QPHLETIEVI DEVVKVQSRY WKSLRYGVPT
     TSFDDVYDLN GTGSNYQLLN IGEPIRANQV NELFNKYSFV NLPIISSATE GGEKNGIFST
     DLPSHLDDII IASPDIYEST VVVLTIHDPP EIWANINPIN GSIEGNSSVI LEHPLMQIME
     KMKKETDKSD SKEKIGYIDI NVPSYQLPIP FGNSKQTSTY NPTFFAQELL LYIWDNYLAY
     FSQLKKLVFV GFGDSYQAIV HLYGKRPSQD IKDLVKGTVA FVNRSNLKAL VPVMDESMVD
     WYYQNSVIFT SCSNPCWVNS NGTTRLGNGS TEANGGDDSN KRPRRKFGRV LKASVDGLYD
     IIAERFDEGV DFILDSIEEY SSSESSN
//