ID A0A2X0PIA9_9BASI Unreviewed; 552 AA.
AC A0A2X0PIA9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Name=BQ5605_C030g10815 {ECO:0000313|EMBL:SGZ08768.1};
GN ORFNames=BQ5605_C030G10815 {ECO:0000313|EMBL:SGZ08768.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGZ08768.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGZ08768.1, ECO:0000313|Proteomes:UP000249464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQNC01000069; SGZ08768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0PIA9; -.
DR STRING; 796604.A0A2X0PIA9; -.
DR Proteomes; UP000249464; 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 GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
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:SF13; HISTONE DEACETYLASE HDAC1; 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:UP000249464};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 37..342
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 402..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 204
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 206
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 292
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 552 AA; 60252 MW; 84C8EB1093495DC6 CRC64;
MSSTAAAGIM TPVTGAKKRT CYFFDSDIGN YHYGPSHPMK PHRIRMTHSL VMNYGLYKKM
EIFRAKPATR KEMAQFHTDE YVDFLSRVTP DLIEQAAEGM GVTGAGTGAA RAGGISREMG
KFNVGDDCPV FDGLFEYCSI SAGGSMEGAA RLSRDKCDIA INWAGGLHHA KKAEASGFCY
INDIVLGILE LLRYHPRVLY VDIDVHHGDG VEEAFYTTDR VMTCSFHKYG EFFPGTGDIK
DIGYGKGRNY SVNFPLRDGI TDEAYKSVFE PVISQIMEWY RPSAVVLQCG GDSLSGDKIG
TLNLSMRGHA NCVQYIKSFG LPLLLLGGGG YTIRNVSRTW AFETGLAAGQ ELGGNIPMNE
YYEYYGPTYQ LDVPQCNMDD LNTREYLEKI KTQVFETLRH TGAAPSVQLQ PIPRTAMDLD
SDDEEEDTRD PNQRRSQHSR DAQIQRDDEF SDSEDEGEGG RRDRQSWQSL GTDVKGNGSV
AAGSANGAKM MGGTPSIEAL TTPGQAEAED VEVPKGGPGE EENLTVSAAR RTTVAGEGED
DGQGGDGDVS MS
//
