ID A0A093BY19_TAUER Unreviewed; 1074 AA.
AC A0A093BY19;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE Flags: Fragment;
GN ORFNames=N340_07651 {ECO:0000313|EMBL:KFV04897.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV04897.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV04897.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV04897.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738}.
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DR EMBL; KL449972; KFV04897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093BY19; -.
DR Proteomes; UP000053661; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
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; cd10162; ClassIIa_HDAC4_Gln-rich-N; 1.
DR CDD; cd10006; HDAC4; 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; PTHR45364:SF11; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053661};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 57..145
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 665..982
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 793
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 665
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 741
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 966
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV04897.1"
FT NON_TER 1074
FT /evidence="ECO:0000313|EMBL:KFV04897.1"
SQ SEQUENCE 1074 AA; 118832 MW; E7E2A4999D67F92F CRC64;
PDGLSGRDQP VELLNPPRVN HMPSSVDVTT ALPLQVAPTS VPMDLRLDHQ FSMPVTEPTL
REQQLQQELL ALKQKQQIQR QILIAEFQRQ HEQLSRQHEA QLHEHIKQQE MLAMKHQQEL
LEHQRKLEQH RQEQELEKQH REQKLQQLKN KEKGKESAVA STEVKMKLQE FVLNKKKALA
HRNLNHCISS DPRFWYGKTQ HSSLDQSSPP QSGVSGTYNH PVLGMYDSKD DFPLRKTASE
PNLKLRSRLK QKVAERRSSP LLRRKDGPVV TALKKRPLDV TDSACNSAPG SGPSSPNNSS
NNISAENGIA GSVTSIQAET SLAHRLVNRE GSVTQLPLYT SPSLPNITLG LPATGPSSGG
SAQQDAERLT IPTLQQRISL FPGTHLTPYL STTTLERDGG TAHNPLLQHM VLLEQPTAQT
PLVTGLPLHA QSLVGGERVS PSIHKLRQHR PLGRTQSAPL PQNAQALQQL VIQQQHQQFL
EKHKQQFQQQ QLHINKIISK PNEPARQHES HPEETEEELR EHQALLEEPY TDRVSSQKEA
PGLANVVQVK QEPIESDEEE GEPQQELESG QRQAEQELLF RQQALLLEQQ RIHQLRNYQA
SLEAAGMPVS FGGHRPLSRA QSSPASATFP MSVQEPPTKP RFTTGLVYDT LMLKHQCTCG
NTNSHPEHAG RIQSIWSRLQ ETGLRGKCEC IRGRKATLEE LQTVHSEAHT LLYGTNPLNR
QKLDSKKLLG SLTSMFVRLP CGGVGVDSDT IWNEVHSSGA ARLAVGCVIE LVFKVATGEL
KNGFAVVRPP GHHAEESTPM GFCYFNSVAI AAKLLQQRLN VSKILIVDWD VHHGNGTQQA
FYNDPNVLYI SLHRYDDGNF FPGSGAPDEV GTGAGVGFNV NMAFTGGLDP PMGDTEYLTA
FRTVVMPIAN EFAPDVVLVS SGFDAVEGHP TPLGGYNLSA KCFGYLTKQL MGLAGGRIVL
ALEGGHDLTA ICDASEACVS ALLGNELDPL PEKVFQQRAN ANAVHSMEKV IEIHSKYWHS
LQRYASTVGY SLVEAQKCEN EEAETVTAMA SLSVGVKPAE KRPDDEPMEE EPPL
//
