ID   HDA19_MAIZE             Reviewed;         513 AA.
AC   P56521;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Probable histone deacetylase 19;
DE            EC=3.5.1.98;
DE   AltName: Full=RPD3 homolog;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wisconsin 22;
RX   PubMed=9645435; DOI=10.1007/s004380050733;
RA   Rossi V., Hartings H., Motto M.;
RT   "Identification and characterisation of an RPD3 homologue from maize (Zea
RT   mays L.) that is able to complement an rpd3 null mutant of Saccharomyces
RT   cerevisiae.";
RL   Mol. Gen. Genet. 258:288-296(1998).
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. Histone deacetylases act via the formation of
CC       large multiprotein complexes. {ECO:0000250|UniProtKB:O22446}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q8GXJ1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8GXJ1};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF035815; AAC50038.1; -; mRNA.
DR   PIR; T01413; T01413.
DR   AlphaFoldDB; P56521; -.
DR   SMR; P56521; -.
DR   STRING; 4577.P56521; -.
DR   PaxDb; 4577-GRMZM2G172883_P01; -.
DR   MaizeGDB; 2665840; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   InParanoid; P56521; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P56521; baseline and differential.
DR   GO; GO:1902494; C:catalytic complex; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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:SF25; HISTONE DEACETYLASE 3; 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   2: Evidence at transcript level;
KW   Chromatin regulator; Hydrolase; Metal-binding; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..513
FT                   /note="Probable histone deacetylase 19"
FT                   /id="PRO_0000114722"
FT   REGION          23..334
FT                   /note="Histone deacetylase"
FT   REGION          384..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..416
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   BINDING         277
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   SITE            316
FT                   /note="Polarizes the scissile carbonyl of the substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
SQ   SEQUENCE   513 AA;  57546 MW;  C45387CF3A38906F CRC64;
     MDPSSAGSGG NSLPSVGPDG QKRRVCYFYD PDVGNYYYGQ GHPMKPHRIR MTHSLLARYG
     LLNQMQVYRP NPARERELCR FHAEEYINFL RSVTPETQQD QIRLLKRFNV GEECPVLDGL
     YSFCQTYAGA SVGGAVKFNH GHDIAINWSG GLHHAKKCEA SGFCYVNDIV LAILELLKHH
     ERVLYVDIDI HHGDGVEEAF YTTDRVMTVS FHKFGDYFPG TGDIRDIGHS KGKYYSLNVP
     LDDGIDDESY QSLFKPIMGK VMEVFRPGAV VLQCGADSLS GDRLGCFNLS IKGHAECVRY
     MRSFNVPLLL LGGGGYTIRN VARCWCYETG VALGQEPEDK MPVNEYYEYF GPDYTLHVAP
     SNMENKNTRQ QLDDIRSKLS KLRHAPSVHF QERVPDTEIP EQDEDQDDPD ERHDPDSDME
     VDDHKAVEES SRRSILGIKI KREFGENATR VQDGGRVASE HRGLEPMAED IGSSKQAPQA
     DASAMAIDEP SNVKNEPESS TKLQGQAAAY HKP
//