ID   HDT2_MAIZE              Reviewed;         303 AA.
AC   Q9M4U5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Histone deacetylase HDT2;
DE   AltName: Full=Histone deacetylase 2b;
DE            Short=HD2b;
DE   AltName: Full=Zm-HD2b;
GN   Name=HDT2; Synonyms=HD2B;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11469594; DOI=10.1007/s004250000506;
RA   Dangl M., Brosch G., Haas H., Loidl P., Lusser A.;
RT   "Comparative analysis of HD2 type histone deacetylases in higher plants.";
RL   Planta 213:280-285(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 81-91.
RX   PubMed=8961957; DOI=10.1021/bi961294x;
RA   Brosch G., Lusser A., Goralik-Schramel M., Loidl P.;
RT   "Purification and characterization of a high molecular weight histone
RT   deacetylase complex (HD2) of maize embryos.";
RL   Biochemistry 35:15907-15914(1996).
CC   -!- FUNCTION: Mediates the deacetylation of lysine residues on the N-
CC       terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Multimer. Possibly forms a homotrimer with HDT1 and/or HDT3
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase HD2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF254072; AAF68624.1; -; mRNA.
DR   RefSeq; NP_001105631.1; NM_001112161.1.
DR   AlphaFoldDB; Q9M4U5; -.
DR   SMR; Q9M4U5; -.
DR   STRING; 4577.GRMZM2G100146_P01; -.
DR   iPTMnet; Q9M4U5; -.
DR   PaxDb; Q9M4U5; -.
DR   PRIDE; Q9M4U5; -.
DR   GeneID; 542636; -.
DR   KEGG; zma:542636; -.
DR   eggNOG; ENOG502QVH6; Eukaryota.
DR   OrthoDB; 1260281at2759; -.
DR   SABIO-RK; Q9M4U5; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q9M4U5; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   InterPro; IPR041232; NPL.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF17800; NPL; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..303
FT                   /note="Histone deacetylase HDT2"
FT                   /id="PRO_0000195209"
FT   ZN_FING         277..300
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          100..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..200
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  32613 MW;  708E4627101BB67C CRC64;
     MEFWGLEVKP GSTVKCEPGH GFILHVSQAA LGESKKSDSA LMYVKVDDKK LAIGTLSIDK
     YPQIQFDLVF NKEFELSHTS KTTSVFFSGY KVEQPIEGDE MDLDSEDEEE ELNIPVIKEN
     GKADGKEEQK NQEKAVAATA SKSSLGLEKK SKDDSDDSDE DESDDSDEDD SDDSDEGEGL
     SPDEGDDDSS DEDDTSDDDE EETPTPKKPE AGKKRGAENA LKTPLSDKKA KVATPPAQKT
     GGKKGATHVA TPHPAKGKTP ANNDKLTEKS PKSGGSVPCK SCSKTFNSEM ALQAHSKAKH
     GAK