ID A0A091J4F9_EGRGA Unreviewed; 1059 AA.
AC A0A091J4F9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE Flags: Fragment;
GN ORFNames=Z169_16359 {ECO:0000313|EMBL:KFP15859.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP15859.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP15859.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP15859.1};
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; KK501543; KFP15859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091J4F9; -.
DR STRING; 188379.A0A091J4F9; -.
DR Proteomes; UP000053119; 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; cd10163; ClassIIa_HDAC9_Gln-rich-N; 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:UP000053119};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 34..124
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 655..975
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 110..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 786
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 732
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 959
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP15859.1"
FT NON_TER 1059
FT /evidence="ECO:0000313|EMBL:KFP15859.1"
SQ SEQUENCE 1059 AA; 117217 MW; D55C50E42192DE00 CRC64;
FLPTVDVKSE VPVGLEPISP LDLRTDLRMM VPMVDPIMRE KQLQQELLLI QQQQQIQKQL
LIAEFQKQHE NLTRQHQAQL QEHIKLQQEL LAIKQQQELL EKEQKLEQQR QEQELERHRR
EQQLPPLRGK ERSRERAVAS TEVKQKLQEF LLSKSATKDS PANGKNHSMS RHPKLWYTAA
HHTSLDQSSP PLSGASPPYK YTLPGAQDAK DDFPLRKTAS EPNLKVRSRL KQKVTERRSS
PLLRRKDGNV VSSFKKRLFE MTESSASSSS PVSGPSSPSN GQTSSVTENE TSVLPSNIQA
EHLVSQQRLL IQDESVNLLS LYTSPSLPNI TLGLPAVQPQ ISASSSFKEK QKGETQSLRQ
GVALAGQYGG NIPPSSTHPH VALEGKPNSS HQALLQHLLL KEQMRQQKLL VTGAVPLHPQ
SPLAAKERVS PGIRAAHKLP RHRPLNRTQS APLPQSTLAQ LVIQQQHQQF LEKQKQYQQQ
IHMNKMLSKS IEQLKQPGSH LEEAEEELHG DHSMQEERAP ASGASVRAES SSAGADDRIG
QQVGAVKVKE EPPDSDEDVQ TQQMESGEQA AFMQQEFLAH RRVHQLQIYQ AQMATVGMAG
LDKHRPVPRT TSSPADSTLP HPAVDQPSQH VYTTGVVYDS LMLKHQCMCG NYANHPEHAG
RIQSIWSRLQ ETGLLNKCER IRGRKASLEE IQLVHSEHHS LLYGTSPLNR QKLDPRKLLG
NVSQKLFSLL PCGGLGVDSD TVWNELHSAG AARMAVGCSC SLQLRHRKGN CSIENGFAVV
RPPGHHAEES TAMGFCFFNS IAITAKYLRD KLNIGKILIV DLDVHHGNGT QQAFYADPSI
LYVSLHRYDE GNFFPGSGAP NEVGSGPGEG YNINIAWTGG LDPPMGDVEY LTAFRTVIMP
AANEFDPEIV LVSAGFDAVE GHDPPLGGYK VTAKCFGHLT KQLLKLADGR VVLALEGGHD
LTAICDASEA CINALLGNEL EPLPEDIVHQ IPNMNAIASL KKTTEIQSKY WKSVEPYSVP
VDCALAESQK QEREETETVS AMASLSVDVE QCIPQEGGR
//
