ID A0A8X7PVJ6_BRACI Unreviewed; 411 AA.
AC A0A8X7PVJ6;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
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};
GN ORFNames=Bca52824_076781 {ECO:0000313|EMBL:KAG2257487.1};
OS Brassica carinata (Ethiopian mustard) (Abyssinian cabbage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=52824 {ECO:0000313|EMBL:KAG2257487.1, ECO:0000313|Proteomes:UP000886595};
RN [1] {ECO:0000313|EMBL:KAG2257487.1, ECO:0000313|Proteomes:UP000886595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sxm20200214 {ECO:0000313|EMBL:KAG2257487.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2257487.1};
RA Ma Q., Huang Y., Song X., Pei D.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] +
CC acetate; 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|ARBA:ARBA00048287,
CC ECO:0000256|PIRNR:PIRNR037913};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG2257487.1}.
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DR EMBL; JAAMPC010000015; KAG2257487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8X7PVJ6; -.
DR OrthoDB; 1090410at2759; -.
DR Proteomes; UP000886595; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:TreeGrafter.
DR CDD; cd09991; HDAC_classI; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR003084; HDAC_I/II.
DR InterPro; IPR000286; HDACs.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF24; HISTONE DEACETYLASE; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037913};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW Reference proteome {ECO:0000313|Proteomes:UP000886595};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 38..327
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT BINDING 274
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
SQ SEQUENCE 411 AA; 45856 MW; 6E72D09D244C4580 CRC64;
MGKENTASLA SGTDGKKRRV TYYYEPYIGD GSQRVSQQIT TTHNLIRSYN LHNDMDIIRP
SLAKDSDFVR FHSPEYITCL ATLTPEYVDM ANKSENVAET SLELFDLDEW DTPFFPGLID
YCRLYAGGSI CAAAKLNRRE ADITINWSGG MHRAKRDEAR GFGYVNDVVL GILELLKVFK
RVLYIDIGYY HGDAVQEAFY KTDRVMTVSF HESVVQSRGD ITDNGVEKGE YYSLNAPLKN
GLNDASFVNL LVPVIHKAME VYQPEAIVLQ CGPDSLAGDA LGKFNLTIKG HAACLQYIRS
FNVPLMLLGG QGHTLGNVAR CWCYETAVSV GKEIDDDLDT NVSDACFAPG YQLHIEPNRM
KNLNTDGYIA KIKKTLLNQL SQVIHAPSVQ FQDTPPISQV TEAAEEDMET R
//
