HDA19_MAIZE
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 03-AUG-2022, entry version 110.
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.GRMZM2G172883_P01; -.
DR PaxDb; P56521; -.
DR MaizeGDB; 2665840; -.
DR eggNOG; KOG1342; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P56521; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.40.800.20; -; 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 Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; SSF52768; 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