ID   C3Z354_BRAFL            Unreviewed;       926 AA.
AC   C3Z354;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037911};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037911};
GN   ORFNames=BRAFLDRAFT_103129 {ECO:0000313|EMBL:EEN52898.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN52898.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN52898.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN52898.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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 gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events. {ECO:0000256|PIRNR:PIRNR037911}.
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         Evidence={ECO:0000256|PIRNR:PIRNR037911};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037911}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|ARBA:ARBA00007738,
CC       ECO:0000256|PIRNR:PIRNR037911}.
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DR   EMBL; GG666576; EEN52898.1; -; Genomic_DNA.
DR   RefSeq; XP_002596886.1; XM_002596840.1.
DR   AlphaFoldDB; C3Z354; -.
DR   STRING; 7739.C3Z354; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   InParanoid; C3Z354; -.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd11681; HDAC_classIIa; 1.
DR   Gene3D; 6.10.250.1550; -; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR046949; HDAC4/5/7/9.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF15; HISTONE DEACETYLASE; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF12203; HDAC4_Gln; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037911; HDAC_II_euk; 3.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW   Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037911};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037911};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   DOMAIN          19..86
FT                   /note="Histone deacetylase glutamine rich N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12203"
FT   DOMAIN          507..824
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          73..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..439
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        635
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT   BINDING         499
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT   BINDING         501
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT   BINDING         507
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT   BINDING         583
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
SQ   SEQUENCE   926 AA;  101141 MW;  F1ECED084036E917 CRC64;
     MVIDGREQQG SAGGEVEDRL NYIKQQQALQ RELLHQHFRQ QEEQLARQHQ AELQQHLHLQ
     KLQALREQQE LAQARGKLQE KQSERQKQLL AGKKKENSAM ASTEVKEKLQ TFILSKKQRE
     AAANSLHQSP SLSMAHWPHG SLGHMPMSGD LAAAAAYKGH PMLGTYGSNA DFPLRKTASE
     PNLKVRSRLK QKVAERRSSP LLRRRDGIGG SFKTRKPLSN KIHIQVPQSA PGSGPSSPRS
     SHSNMVIAGN HEESGVQPAV VPGRMVGGNA ADFTLYTSPS LPNISLGLAN SSSSAETTQT
     GEKVVQSALS REAELRAMAA ARLGQPLTVV PAREPQPAPR SDEGLGTAGH SPSNCAASAS
     RPLGRTHSAP LPGTHMHHLQ QQVLHPQHYM QALLRQHVVN KQQLGNGDIA KQPRPEPHPE
     ETEEELKEHT QVTVKQEPLD SDEENEEEES CRQLDMNIDG TSTHRPLSRA QSSPATYNSV
     KSVFTTGVVY DPLMLKHSCS CGNNSYHPEH SGRIQSVWSR LQETGLVNRC ERVRSRKATI
     DELKTCHSEQ HVYLYGTNPL HRQKQDSKKL AGGLQKSFKY LPCGGLGVDA DTIWNELHSP
     SALRMAAGCV IELAFKVAQG ELKNGFAVVR PPGHHAEVDQ AMGFCFFNSI AVTARLLVQR
     LKLNKVLIVD WDVHHGNGTQ QMFYEDGQVL YVSLHRWDSG NFFPGTGAPD ECGNGAGLGK
     NVNISFSGGL EPPMGDAEYM AAFRTVVMPI AVEFSPDLVL VSAGFDTAEG HAPQLGGYKV
     TPKCFGHMTK QLMSVAGGRV VLALEGGYDL AAICDCSEMC VQALLGDELP PLPKEIIEQP
     PNKNAVTSLE ETIRRQTPHW SSLSRYASTV GYSLYEAYER EKEEADTVSA LASLSVASAP
     GVGMPASANS ERNHKPQPLE DTINGL
//