ID   B9WL19_CANDC            Unreviewed;       869 AA.
AC   B9WL19;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Histone deacetylase, putative {ECO:0000313|EMBL:CAX39722.1};
GN   Name=HDA1 {ECO:0000313|EMBL:CAX39722.1};
GN   OrderedLocusNames=Cd36_26960 {ECO:0000313|CGD:CAL0000168189};
GN   ORFNames=CD36_26960 {ECO:0000313|EMBL:CAX39722.1};
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:CAX39722.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX39722.1, 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; FM992695; CAX39722.1; -; Genomic_DNA.
DR   RefSeq; XP_002421780.1; XM_002421735.1.
DR   AlphaFoldDB; B9WL19; -.
DR   ESTHER; candc-b9wl19; Arb2_domain.
DR   GeneID; 8049879; -.
DR   KEGG; cdu:CD36_26960; -.
DR   CGD; CAL0000168189; Cd36_26960.
DR   VEuPathDB; FungiDB:CD36_26960; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_007727_4_0_1; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000002605; Chromosome R.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; 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; IPR019154; Arb2-like_domain.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR017321; Hist_deAcase_II_yeast.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF09757; Arb2; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          187..497
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          561..794
FT                   /note="Arb2-like"
FT                   /evidence="ECO:0000259|Pfam:PF09757"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          802..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..66
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   869 AA;  97237 MW;  49FDAB697BB352E2 CRC64;
     MSTDKEEHLD SNPENLIPEE EHESQGFSTA TEDSTQASFE EVSEVDYETN PIEMEELSEV
     DDETNPIEME ELSEVDDETN PIEMEELSEV DDETNPIEME EEVTTTTAGT YDTVHPQEPS
     TKKIKLEEPE TESDSNGIIV NEPQVVVVPP KKPQLFYTPL KTGLVYDVRM RYHAKVFTSY
     SEYIDPHPED PRRIYRIYKK LVEAGIVLDP SLAGINEIGP FMLKIPIREA TAEEILEVHS
     EDHLKFIQST EDMSRDQLLK ETETGDSIYV NNDSYLSAKL SCGGTIEACK AVIEGRVKNS
     LAIVRPPGHH AEPNTPAGFC LFSNVAVAAK NMLKTYPESV RKIVIVDWDI HHGNGTQKAF
     YNDPRVLYIS LHRFENGRFY PGTKYGDSNQ VGEGPGEGFT INIPWRSYGM HDGDYVYAFN
     KIIQPVISEF DPDLIIVSSG FDAADGDVIG ACHVTPAGYG YMTHTLKGIA RGKLAVILEG
     GYNLDSISKS ALAVAKVLVG EPPENTITLR PHLETIEVVD EVMKIQSKYF KCLREGFPNS
     IFEDVYDLPD IEKANYKLVN IADPIRSHQV EKLFNEKEFI NIPIISSVPN GEKSPFTTDI
     PDQLEDLVVA SPDIYDCTTI ILTIHDPPEI WANINPTNGV IETNSTMILE HPLVQIMDKI
     QKEKDSDNQE KFGYLDINIP SFQLPIPGTT SESSTYNPII FAQEVLLYIW DNYITYFQQL
     KNLVLVGFGD SYQAIVNLYG KRPSNEVKDL VKGTVAFLNR TTLKPLIPVM DESMVDWYYQ
     NSVIFTSNFN TCWTGGGTGN GTNGNGSNGG GNKPAESNGH DDFSKRPRKK FGRVIKTTSD
     GLCDVIQEKF DEGVDFILDS IEDYSSSED
//