ID   HDA21_DICDI             Reviewed;        1489 AA.
AC   Q54X15;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Type-2 histone deacetylase 1;
DE            Short=DdHdaD;
DE            EC=3.5.1.98;
GN   Name=hdaD; ORFNames=DDB_G0279267;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=19576222; DOI=10.1016/j.jmb.2009.06.067;
RA   Sawarkar R., Visweswariah S.S., Nellen W., Nanjundiah V.;
RT   "Histone deacetylases regulate multicellular development in the social
RT   amoeba Dictyostelium discoideum.";
RL   J. Mol. Biol. 391:833-848(2009).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation plays an important role in transcriptional regulation,
CC       cell cycle progression and developmental events. Histone deacetylases
CC       act via the formation of large multiprotein complexes (By similarity).
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Down-regulated during terminal differentiation of
CC       cells into spores and stalk. {ECO:0000269|PubMed:19576222}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000030; EAL67782.1; -; Genomic_DNA.
DR   RefSeq; XP_641762.1; XM_636670.1.
DR   AlphaFoldDB; Q54X15; -.
DR   SMR; Q54X15; -.
DR   STRING; 44689.DDB0237655; -.
DR   PaxDb; Q54X15; -.
DR   EnsemblProtists; EAL67782; EAL67782; DDB_G0279267.
DR   GeneID; 8621960; -.
DR   KEGG; ddi:DDB_G0279267; -.
DR   dictyBase; DDB_G0279267; hdaD.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_249274_0_0_1; -.
DR   InParanoid; Q54X15; -.
DR   OMA; QCTIAHL; -.
DR   Reactome; R-DDI-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-DDI-3214815; HDACs deacetylate histones.
DR   Reactome; R-DDI-3371511; HSF1 activation.
DR   Reactome; R-DDI-5617833; Cilium Assembly.
DR   PRO; PR:Q54X15; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR   GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   SUPFAM; SSF52768; SSF52768; 2.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Cytoplasm; Hydrolase; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..1489
FT                   /note="Type-2 histone deacetylase 1"
FT                   /id="PRO_0000331371"
FT   REGION          135..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          915..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1151..1185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1325..1374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..987
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1336..1374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1232
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1489 AA;  165561 MW;  8587B045FDC673B5 CRC64;
     MSTIHQVNEM NSRVGEKPAC CIGAARGHCT AHCPRIEDVL YSQRKGKTNK GAQRWRCKAC
     GTKWTSKGII IQPPVVPDTI VNSIGFGNGP EEISMEQLRA NARPYKKTKT GDNILQTSPF
     PSLFGNSIGM GLGGNNNNIN NNNNSNGSNS SNNSHNGGSS PSGSPIPSPP SPVSFLQRNS
     NVFVPILPQS NGNNINNNNN NNSNSNSNNI NSNSSNSMQL QNNNNNNGQL RSSSSSLSLS
     SSSSQLNSSS NGNGSSRNLL TSQKSAQSLI GNINNNNNNN NIINNNSNNN TNNNNNIMNG
     TTTSTTKPVV VGGPMQILNS VVNNSPTSSK PILSSSSQNL LYNSSGSIPQ PSQSPQNNNN
     TTINNNNNTT NNNNNNNNSN NNNNSNNNNN NSNNNNINNV ANGTPRPSLQ TSRLQGKLPS
     PQQYNTSPSH QQYPSPKNNN NSNNIIPIQS TYGQPTPPPT KPPVSSKAPA VYHNVRVPSP
     NTTVDNNNNN NNNNNNNNNN NNNNNNNNNN NNSNNNNNSN NNNNNINNNN NNNNNSNNNN
     NGNSNNNNNN NSNYQQQHQY FSPNQNYIQQ QVQAVQTQQA QHILAQQQAQ AQQQYIQQLQ
     LQQQTLAHAQ SQAAHQAQTL THSRHNDLLS PIDSQIWAPI QYSWIQTHYN PSSSLLECLK
     RLINSVVVFS NELPVDQRLK MINFLTTLSS PSSESQYNTN ASKQMLNCID NSVFNITKHY
     QMLYQSISKH YSMMEDSFIP LTEVYFDENE INKFIHFSDQ FKIIEEQFEF ILRELSSIRD
     TLIIKRENIE KNIIESSKFL NNSSNNDNGI EEIGLEQAKQ DTTRLLESLA PLETTLNSME
     IKFKSIQKEI SMVIRVFSFF ELLYNIHINC HQTIVEKHSR QLSTYMIDVI QQSLYNCDVI
     SVAYNRLKTG LFNSNNNNNN NNNNNNNNNE EDDQLIDTTN PFINKLSDLL SKYENISKNN
     NNNNNNNNNN NNNNNNNNNN NNNNNNNNRN RDRDREFERD NNSNNNNNNI EKERNRNNRI
     RDRDNMDIDN ISSFISNNQQ QHIGQSQSVQ QSSQLPKERK VMALYHTTCL DHLVPDDHPE
     SPKRLSSVIK AINDFSRQSD RLIIKNDPEE INDKWILTVH SPEYLRLLED LTEKLDANEI
     RPLNVNNDGA STGINQFSTS TPITTTGTAT VTPGSTTSST NGEQCEDGDT FVSKLSLHAA
     KRSAGATCQA IDNVMKGNVT SAFVAARPPG HHAGRDGLTS GTSSQGFCLL NHVCIGAKYA
     QLKYNLDKIA IIDFDVHHGN GTEEILSNDQ GFYFLSIHMF EEGFYPGSGG GVGSIGVVNL
     NEFNEQNDYD DDDNNNDVNN NNNNNNNNNN NNNNNNNNKN NNNNNSNSIT QQSTITNNSN
     CKGNIVNIPL DPKSSASSFL KAFSIIIDKL NDYQPELILI SCGFDAHMED HLASLCLLEE
     NYVEITRSLR RVADRWCKGR LVSILEGGYN INALRQCTIA HLSALSEDD