ID   HDA22_DICDI             Reviewed;        1704 AA.
AC   Q54VQ7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Type-2 histone deacetylase 2;
DE            Short=DdHdaC;
DE            EC=3.5.1.98;
GN   Name=hdaC; ORFNames=DDB_G0280195;
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: Expressed after cells enter the multicellular
CC       phase upon starvation. {ECO:0000269|PubMed:19576222}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000035; EAL67324.1; -; Genomic_DNA.
DR   RefSeq; XP_641298.1; XM_636206.1.
DR   AlphaFoldDB; Q54VQ7; -.
DR   SMR; Q54VQ7; -.
DR   STRING; 44689.DDB0237658; -.
DR   PaxDb; Q54VQ7; -.
DR   EnsemblProtists; EAL67324; EAL67324; DDB_G0280195.
DR   GeneID; 8622431; -.
DR   KEGG; ddi:DDB_G0280195; -.
DR   dictyBase; DDB_G0280195; hdaC.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_240787_0_0_1; -.
DR   InParanoid; Q54VQ7; -.
DR   OMA; NSEFETH; -.
DR   Reactome; R-DDI-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-DDI-3214815; HDACs deacetylate histones.
DR   PRO; PR:Q54VQ7; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; SSF52768; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..1704
FT                   /note="Type-2 histone deacetylase 2"
FT                   /id="PRO_0000331372"
FT   REGION          1..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1485..1704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..114
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1485..1643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1650..1704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1256
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         1258
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         1350
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1704 AA;  190816 MW;  84E83B42FB36896E CRC64;
     MSTNNIIEGD EDTKTTITNE SNTDNNNNNN DDNKNNTENT TSPTNNNNTN DNDNNSDNNN
     NKNNNNNNSQ VTEEQQVTLE DSGSEDDINF EEHELSDSAE EDEDEMEDDD EDADGRQNQN
     PNSAGGKRRG RPSKVQQSTN THLSQTTPES PTIFTPDGKV PKRISTSTNN TPNTQSALKT
     NKRPRLTSDE EKDLMLSEES DGGVGEDDDS IMSTNDKPQD ENQSNQNQNN NNNNNNNTTT
     TTTTTNNSNN NNQNLNQNNN NNNNNNNINN NNNNNNSNND NNNNNNRPAR GRPKTNGSRS
     EERKRIQLQQ YIQATQGSST TTSDPNNQNN QINQINQNNQ NNQNNQNNQN NSLGEEEFGE
     EFEEEEEDMG QPKKKTKYKT SKKSVPNHLD IRPCWFVGCV KADRSLKILR PCLIPTCKTH
     AIKSEVRISE ALRRGDFVND ESSGVKDKVC GICGDKKDLH HCGNNGCAFG FCNDCVEIAA
     MKHNNHPNGN KWICWVCQFV RTKAKEKERT RWVKEQLNPG LTSISRKFRR GPELDMAQAQ
     FLQQQQQQQT SPNEKRSSQF NSNNSNNNNN NNSNNNNNNS GFDPSGSPNN QQNQKRLRKK
     INASSDIYET RKYTKKRNDE DSAPPSPTSI IGNSVMVGSS GAAGGGIIKN TTVVVEQQGY
     SATPPSPNTL MVQQQQQLQQ THQQARLSQQ QAQLQQLKAL QQQHQHQQQN NGNFNNLIES
     VLSPNREPLN PIDNFVDQTF TAVKFFSTLS QNPPDEIKER IDNFVDLMMR IKTVRWASDY
     GLVWRMIEEL SNLIKRNLLS SQSVVEMYSE LKSLEEGALE NMTTNARNVP LERAITMVFE
     NHETAGLIGK ECCSTRNALI YSIEVALRAI ADYQHDLEDN LMEESLRSNK VSTEIEQIEH
     QIKANLDEIH KFKYQEVELL DSLSKVRGAI AAHESIRDTL QKKSSELKVD MLLIKNGISD
     KEKETKSQQA TLENEIYALK LLITMVESIY WIHDYFYESR VGECEKLINN KLSQLQNKLE
     TQIPHPPNAL DNAIPNTTTT VMGEDGQPVI VPTTVDIKNK FKTIAIYHKI CMQHKVPNFH
     LEKPDRIQVA VSCINEFASN PLVDIFDNPP EVDMRYVMAV HDANYIKKLE TSLPPENSEF
     ETHLESDKSG AMVTVASHKD FEGDDDNIYD TFVSHRSIKA ALRASGSVCA AVDSVSRSGY
     TRAFCAIRPP GHHAGRYGRT SDAPSQGYCL INNVAIGAKY ASLTAGYSRI AVVDFDVHHG
     NGTQEILSGD DNFLFISIHV CDEKRYFYPG TGQDVGDIDE VSGQFDGNIL NIGLKRNTGS
     AVFLQQWMNK IIPRLEAYKP QLIFLSAGFD GHKDDPTNGL KLNEEDYFVI TKMIKTVAFK
     YCKGRIISVL EGGYGIEKTN SLQRCVNSHL KALIEDTDEE IHLANISYGH FSETQETAIP
     KFNINNFISN PNKRGKKNNL NTINFINNNM NNINNNITNS LSNKQLERQK QLQQQQQQAQ
     QAQQQQSPQQ SQTIENTSIT TTTTTTSTTT TLSTSDSESN NNINNNNNDY NNNNNNNSNN
     NNNNSNNNQP TNFNSSTSSP ILSGNNNNNN NNNNNNNNNN INNNNNNNSN NNNNMNTSNP
     TNQQSSVIIS DDMDDVQTNS NPPNPQYPLS PNSVNRGNNP SNISMSGAQR SAPLIISPKP
     SNSPNSPSTS NNNGTPQNIN NSDN