ID   B9WD52_CANDC            Unreviewed;       454 AA.
AC   B9WD52;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
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   OrderedLocusNames=Cd36_80710 {ECO:0000313|CGD:CAL0000168217};
GN   ORFNames=CD36_80710 {ECO:0000313|EMBL:CAX42601.1};
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX42601.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX42601.1, ECO:0000313|Proteomes:UP000002605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC   {ECO:0000313|Proteomes:UP000002605};
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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; FM992690; CAX42601.1; -; Genomic_DNA.
DR   RefSeq; XP_002419019.1; XM_002418974.1.
DR   AlphaFoldDB; B9WD52; -.
DR   GeneID; 8046801; -.
DR   KEGG; cdu:CD36_80710; -.
DR   CGD; CAL0000168217; Cd36_80710.
DR   VEuPathDB; FungiDB:CD36_80710; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_7_4_1; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000002605; Chromosome 3.
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   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:SF25; HISTONE DEACETYLASE 3; 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   Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT   DOMAIN          54..346
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         203
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         205
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   454 AA;  51764 MW;  C5A9008799A170F6 CRC64;
     MTISISETDT FTTDSKTREN TPIYDPNHPG TNNKYNVSYH YNPEVSRFHY GALHPMKPFR
     LMLTDHLVIS YKLYEKMDLY TPRRATKEEL LEFHSEDYIN FLQSITPEKC KTIGNDTLAQ
     FNIGDDCPIF DGMYDYSAIY AGASLDATRK LISGMSDIAI NWSGGLHHAK KFEPSGFCYV
     NDIVLSIINL LRVHPRVMYI DIDLHHGDGV QEAFYNTDRV MTVSFHKYNG EFFPGTGSVD
     EVGIGSGKNY AINVPLRDGI DDESYIRLFK SIMEPLITKF QPTCIVQQCG ADSLGYDRLG
     CFNLNIRAHG ECVKFIKSFG IPMLVVGGGG YTPRNVSRLW CYETSVLNDV SLDHKIPNYL
     PTYDWFGPDY SLHPQLDGRI DNKNSKKYLQ SVQTTIMEQI RYLNHAPSVQ MYEIPPDLTG
     LTEDEDKAIQ ELNEDMERDE KIMKDEAKPG ELMT
//