ID A0A091NIY7_APAVI Unreviewed; 1072 AA.
AC A0A091NIY7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE Flags: Fragment;
GN ORFNames=N311_01001 {ECO:0000313|EMBL:KFP89688.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP89688.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP89688.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP89688.1};
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; KL385224; KFP89688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NIY7; -.
DR Proteomes; UP000054244; 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 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:UP000054244};
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 663..980
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..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 791
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 663
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 964
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP89688.1"
FT NON_TER 1072
FT /evidence="ECO:0000313|EMBL:KFP89688.1"
SQ SEQUENCE 1072 AA; 118758 MW; 89BBA366C545E122 CRC64;
PDGLSGRDQP VELLNPPRVN HMPSSVDVTT ALPLQVAPTS VPMDLRLDHQ FSMPVTEPTL
REQQLQQELL ALKQKQQIQR QILIAEFQRQ HEQLSRQHEA QLHEHIKQQE MLAMKHQQEL
LEHQRKLEQH RQEQELEKQH REQKLQQLKN KEKGSAVAST EVKMKLQEFV LNKKKALAHR
NLNHCISSDP RFWYGKTQHS SLDQSSPPQS GVSGTYNHPV LGMYDSKDDF PLRKTASEPN
LKLRSRLKQK VAERRSSPLL RRKDGPVVTA LKKRPLDVTD SACNSAPGSG PSSPNNSSNN
ISTENGIAGS VTSIQAETSL AHRLVNREGS VTQLPLYTSP SLPNITLGLP ATGPSSGGSA
QQDAERLTIP TLQQRISLFP GTHLTPYLST TTLERDGGTA HNPLLQHMVL LEQPTAQTPL
VTGLPLHAQS LVGGERVSPS IHKLRQHRPL GRTQSAPLPQ NAQALQQLVI QQQHQQFLEK
HKQQFQQQQL HINKIISKPN EPTRQHESHP EETEEELREH QALLEEPYSD RVTSQKEAPG
LANMVQVKQE PIESDEEEAE PQQELESGQR QAEQELLFRQ QALLLEQQRI HQLRNYQASL
EAAGMPVSFG GHRPLSRAQS SPASATFPMS VQEPPTKPRF TTGLVYDTLM LKHQCTCGNT
NSHPEHAGRI QSIWSRLQET GLRGKCECIR GRKATLEELQ TVHSEAHTLL YGTNPLNRQK
LDSKKLLGTI AWAGVSSSWP LTLTLLDTIW NEVHSSGAAR LAVGCVIELV FKVATGELKN
GFAVVRPPGH HAEESTPMGF CYFNSVAIAA KLLQQRLNVS KILIVDWDVH HGNGTQQAFY
NDPNVLYISL HRYDDGNFFP GSGAPDEVGT GAGVGFNVNM AFTGGLDPPM GDTEYLTAFR
TVVMPIANEF APDVVLVSSG FDAVEGHPTP LGGYNLSAKC FGYLTKQLMG LAGGRVVLAL
EGGHDLTAIC DASEACVSAL LGNELDPLPE KVFQQRANAN AVHSMEKVIE IHSKYWHSLQ
RYASTVGYSL VEAQKCENEE AETVTAMASL SVGVKPAEKR PDDEPMEEEP PL
//
