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Database: UniProt
Entry: A0A0P1AWI2_PLAHL
LinkDB: A0A0P1AWI2_PLAHL
Original site: A0A0P1AWI2_PLAHL 
ID   A0A0P1AWI2_PLAHL        Unreviewed;       447 AA.
AC   A0A0P1AWI2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
OS   Plasmopara halstedii (Downy mildew of sunflower).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Plasmopara.
OX   NCBI_TaxID=4781 {ECO:0000313|EMBL:CEG45902.1, ECO:0000313|Proteomes:UP000054928};
RN   [1] {ECO:0000313|Proteomes:UP000054928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sharma Rahul, Thines Marco;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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:PIRNR037913};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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DR   EMBL; CCYD01001859; CEG45902.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1AWI2; -.
DR   STRING; 4781.A0A0P1AWI2; -.
DR   EnsemblProtists; CEG45902; CEG45902; CEG45902.
DR   OMA; GKIMEWY; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000054928; Unassembled WGS sequence.
DR   GO; GO:1902494; C:catalytic complex; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd09991; HDAC_classI; 1.
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:SF11; HISTONE DEACETYLASE 19; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 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,
KW   ECO:0000256|PIRNR:PIRNR037913}; Hydrolase {ECO:0000256|PIRNR:PIRNR037913};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054928};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT   DOMAIN          40..328
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         188
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         190
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         276
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ   SEQUENCE   447 AA;  50368 MW;  BCA9D3E2B1B81604 CRC64;
     MNSGIGSSVA LTSGGTIASK RRVAYFYDAE IGNYHYGQNH PMKPHRVRMA HNLITNYGLT
     KHMEVFRPRL VDWTELTRFH SDDYIHFLRL VTPDNMHEYL RQLQRFNVGE DCPVFDGLFE
     FCQLYASASI GGAAKLNAGS ADIVINYSGG LHHGKRSEAS GFCYVNDCVL GILELLKSHQ
     RVLYIDIDIH HGDAVEEAFY TTNRVMTCSF HKYGEFFPGT GDIKDIGHED GKHYAVNFPC
     RDGMDDESFT GIFRSIICKV MEHFAPGAVL LQCGTDSLSG DRLGSFNLSA KGHADCVAYV
     KSFNIPTLVV GGGGYTLRNV ARAWCYEASL LVGVDIPDAM PYNDYFEYYG PEYRLHLPVS
     NMENLNTPAY LDEIKRQIHE NLRQIEHVPS VPFTVAPQSA HIQEENEAAA RDHEEDDQLM
     MDVSGERQVQ QELKQIDVPR HAAEFYD
//
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