ID   HDA2_CAEEL              Reviewed;         507 AA.
AC   Q09440;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Putative histone deacetylase 2;
DE            EC=3.5.1.98;
GN   Name=hda-2; ORFNames=C08B11.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Probably responsible for the deacetylation of lysine
CC       residues on the N-terminal part of the core histones (H2A, H2B, H3
CC       and H4). Histone deacetylation gives a tag for epigenetic
CC       repression and plays an important role in transcriptional
CC       regulation, cell cycle progression and developmental events.
CC       Histone deacetylases act via the formation of large multiprotein
CC       complexes (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. Type 1
CC       subfamily.
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DR   EMBL; Z46676; CAA86662.1; -; Genomic_DNA.
DR   PIR; T19067; T19067.
DR   RefSeq; NP_495678.1; -.
DR   UniGene; Cel.14857; -.
DR   HSSP; O67135; 1C3P.
DR   IntAct; Q09440; 1.
DR   Ensembl; C08B11.2; Caenorhabditis elegans.
DR   GeneID; 174285; -.
DR   KEGG; cel:C08B11.2; -.
DR   NMPDR; fig|6239.3.peg.6436; -.
DR   WormBase; WBGene00001835; hda-2.
DR   WormPep; C08B11.2; CE01472.
DR   OMA; Q09440; HAFCAAR.
DR   NextBio; 883367; -.
DR   ArrayExpress; Q09440; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:InterPro.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
DR   GO; GO:0040007; P:growth; IMP:WormBase.
DR   GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR   GO; GO:0040011; P:locomotion; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   PANTHER; PTHR10625:SF28; His_deacetylse_1; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Complete proteome; Hydrolase; Nucleus; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    507       Putative histone deacetylase 2.
FT                                /FTId=PRO_0000114720.
FT   REGION       29    342       Histone deacetylase.
FT   ACT_SITE    162    162       By similarity.
SQ   SEQUENCE   507 AA;  57138 MW;  F500D405F7595BAF CRC64;
     MSSDKFKLDT LFDDNDEIIE PDGADVKKRN VAYYYHKDVG HFHYGQLHPM KPQRLVVCND
     LVVSYEMPKY MTVVESPKLD AADISVFHTE DYVNFLQTVT PKLGLTMPDD VLRQFNIGED
     CPIFAGLWDY CTLYAGGSVE GARRLNHKMN DIVINWPGGL HHAKKSEASG FCYVNDIVLG
     ILELLKYHKR VLYIDIDIHH GDGVQEAFNN SDRVMTVSFH RFGQYFPGSG SIMDKGVGPG
     KYFAINVPLM AAIRDEPYLK LFESVISGVE ENFNPEAIVL QCGSDSLCED RLGQFALSFN
     AHARAVKYVK SLGKPLMVLG GGGYTLRNVA RCWALETGVI LGLRMDDEIP GTSLYSHYFT
     PRLLRPNLVP KMNDANSAAY LASIEKETLA CLRMIRGAPS VQMQNIVGIR LDEIEQIEEN
     ERLQKSSKSS IEYEVGKVSE KMEEECFVEE DSKPPSFPPG QDPRRIGQYW GYDRSGLAPP
     RSHSDVIEEA KYEDRDRRKD LNIPGIP
//