ID A0A212FEG2_DANPL Unreviewed; 853 AA.
AC A0A212FEG2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037911};
GN ORFNames=KGM_205707 {ECO:0000313|EMBL:OWR52155.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR52155.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR52155.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR52155.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
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|ARBA:ARBA00001028,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWR52155.1}.
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DR EMBL; AGBW02008930; OWR52155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212FEG2; -.
DR STRING; 278856.A0A212FEG2; -.
DR KEGG; dpl:KGM_205707; -.
DR eggNOG; KOG1343; Eukaryota.
DR InParanoid; A0A212FEG2; -.
DR Proteomes; UP000007151; Unassembled WGS sequence.
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 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; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF15; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 4.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151};
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 423..731
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 209..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..88
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 838..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 544
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 492
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
SQ SEQUENCE 853 AA; 91458 MW; 1111D18D8DE71D1E CRC64;
MRIPFQLKKQ QQLQQEILLQ HFQQQRQQLA EQHEQQIRHH LKLWEQQKAM EEAALREARE
AREAREARER HERDRVELMR KKDKHEHSAN ASTQVKQKLQ EFLKKKQAAA SANGTVPGSP
YRNWGIVKSS SGESITSTSA VAGVHPYRLT AAPLPLAPNA AAPQPSPADF PLRKTASEPN
MLKVRLKARV IERRASPLAR RPLKTRIKHR NCEGGSPRGS PPGSLAAPIR EEEEGRANEL
LFSSPSLPNI SLGRPHAAPR HVPPAHAPHV GQVPPAVLPP VSEAEAYSGA AALGARLAKR
PLGRTHSAPL PLGDPALTPH THPHPPSAHH YLRDQIRKTV LTRAHDAAAA QLREEEGEVI
DLTSRRPPSP SAPPAPGPAL GAAPLARALS SPLVGARPPA TGLAYDALML KHGCACGAHA
PTHPEHGGRL QSVWARLCET GLAARTERTR ARKATLEELQ SVHGEAHVAA WAGRGRPGAG
DGRAVRLVRL ACGGLGVDAD TAFSDAHTPP AARLAAGALI DLATRTATNE LRNGFAIVRP
PGHHAEPNQA MGFCFFNNVA IAARILHTRL GLQRILIVDW DVHHGNGTQQ IFYEDPHVLY
ISLHRHDDGN FFPGTGAASE CGAGPGLGYT VNVAWPGSPP LADAEYLAAF RTVVMPIAKE
YDPELVLVSC GFDAAAGHPA PMGGYNVSAA CFAHMTRELM SLAGGKVVLS LEGGYDLAAM
CDCAQECVRA LLGERLAAPS LSELARAPAP HAQAALRTAL AAQSPHWPVL KRYSSLIGVS
ALEAGPSALA RRGRAHAQRD DDTAAAMATL SMQHAHRSLA PPPPPQTQPL ALDRSADSSR
SVSEEPMEQD EVK
//
