ID G0VD60_NAUCC Unreviewed; 434 AA.
AC G0VD60;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=NCAS0C04320 {ECO:0000313|EMBL:CCC69422.1};
GN OrderedLocusNames=NCAS_0C04320 {ECO:0000313|EMBL:CCC69422.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC69422.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC69422.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) 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; HE576754; CCC69422.1; -; Genomic_DNA.
DR RefSeq; XP_003675786.1; XM_003675738.1.
DR AlphaFoldDB; G0VD60; -.
DR STRING; 1064592.G0VD60; -.
DR GeneID; 11527816; -.
DR KEGG; ncs:NCAS_0C04320; -.
DR eggNOG; KOG1342; Eukaryota.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; G0VD60; -.
DR OMA; GKIMEWY; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000001640; Chromosome 3.
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:0006355; P:regulation of DNA-templated transcription; IEA:UniProt.
DR CDD; cd10004; RPD3-like; 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: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:UP000001640};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 39..325
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 389..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 187
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 189
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 275
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 434 AA; 49215 MW; C44865EF3AA39502 CRC64;
MVYENKPFDP ITIKSSDTKK RVAYFYDADV GNYAYGSGHP MKPHRIRMTH SLVMNYGLYK
KMEIYRAKPA TKQEMCQFHT DEYIDFLSRV TPDNLEMFKK ESVKFNVGDD CPVFDGLYEY
CSISGGGSME GAARLNRGKC DVAINYAGGL HHAKKSEASG FCYLNDIVLG IIELLRFHPR
VLYIDIDVHH GDGVEEAFYT TDRVMTCSFH KYGEFFPGTG ELRDTGVGKG KYYAVNVPLR
DGIDDATYRN VFEPVIKRIM EWYQPSAVVL QCGGDSLSGD RLGCFNLSMQ GHANCVNYVK
SFGIPMMVVG GGGYTMRNVA RTWCFETGLL NNVVLDQELP YNDYYEYYGP DYKLDVRPSN
MFNVNSSEYL DKIMTSIFTN LENTKYAPSV ELTNVPKDPE DLGDQEEDTA EAKDTKGGSQ
YARDQEVEHP NEFY
//
