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   01-MAY-2013, entry version 59.
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; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACMAD clade; Panicoideae; Andropogoneae; 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
RT   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
CC       progression and developmental events (By similarity).
CC   -!- SUBUNIT: Multimer. Possibly forms a homotrimer with HDT1 and/or
CC       HDT3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- SIMILARITY: Belongs to the histone deacetylase HD2 family.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
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DR   EMBL; AF254072; AAF68624.1; -; mRNA.
DR   RefSeq; NP_001105631.1; NM_001112161.1.
DR   UniGene; Zm.500; -.
DR   ProteinModelPortal; Q9M4U5; -.
DR   PRIDE; Q9M4U5; -.
DR   GeneID; 542636; -.
DR   KEGG; zma:542636; -.
DR   Gramene; Q9M4U5; -.
DR   HOGENOM; HOG000029063; -.
DR   SABIO-RK; Q9M4U5; -.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 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;
KW   Metal-binding; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    303       Histone deacetylase HDT2.
FT                                /FTId=PRO_0000195209.
FT   ZN_FING     277    300       C2H2-type.
FT   COMPBIAS    153    199       Asp-rich.
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
//