ID A0A7L2GWP6_NYCGR Unreviewed; 353 AA.
AC A0A7L2GWP6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=Histone deacetylase 11 {ECO:0000256|ARBA:ARBA00072450};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE Flags: Fragment;
GN Name=Hdac11 {ECO:0000313|EMBL:NXQ91507.1};
GN ORFNames=NYCGRA_R04290 {ECO:0000313|EMBL:NXQ91507.1};
OS Nyctibius grandis (Great potoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Strisores; Caprimulgiformes;
OC Nyctibiidae; Nyctibius.
OX NCBI_TaxID=48427 {ECO:0000313|EMBL:NXQ91507.1, ECO:0000313|Proteomes:UP000567826};
RN [1] {ECO:0000313|EMBL:NXQ91507.1, ECO:0000313|Proteomes:UP000567826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-56 {ECO:0000313|EMBL:NXQ91507.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXQ91507.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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. Histone deacetylases act via the formation of
CC large multiprotein complexes. {ECO:0000256|ARBA:ARBA00059784}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] +
CC acetate; 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:ARBA00048287};
CC -!- SUBUNIT: Interacts with HDAC6. {ECO:0000256|ARBA:ARBA00065154}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family.
CC {ECO:0000256|ARBA:ARBA00005947}.
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:NXQ91507.1}.
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DR EMBL; VWYG01024714; NXQ91507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L2GWP6; -.
DR OrthoDB; 437693at2759; -.
DR Proteomes; UP000567826; Unassembled WGS sequence.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-ARBA.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProtKB-ARBA.
DR GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; IEA:UniProtKB-EC.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:TreeGrafter.
DR CDD; cd09993; HDAC_classIV; 1.
DR FunFam; 3.40.800.20:FF:000009; Histone deacetylase 11; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR044150; HDAC_classIV.
DR InterPro; IPR000286; HDACs.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF23; HISTONE DEACETYLASE 11; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000567826};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 34..314
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXQ91507.1"
FT NON_TER 353
FT /evidence="ECO:0000313|EMBL:NXQ91507.1"
SQ SEQUENCE 353 AA; 39329 MW; FAFD47285CBAB436 CRC64;
PHRTELYEDP PSTCWPIVYS PDYNITFVGL EKLHPFDAGK WGKVINFLKE EKLVADDLIV
QAREATDEDL LVVHTRRYLN KLKWSFVVAT ITEIPPVAFL PNFLVQRKVL KPLRTQTGGT
IMAGKLAVDR GWAINVGGGF HHCSSDKGGG FCAYADITLA IKFLFERVPG VSKATIIDLD
AHQGNGHERD FMDDHRVYIM DAYNRYIYPG DGDAKRAIKR KVELEWGTED TEYLQKVHTH
VEGALNELKP DIIVYNAGTD ILDGDPLGGL AISPQGIVKR DEVVFKAARS RRIPILMVTS
GGYQRRTARI IADSILNLHN LGLIDKELAA SGAGNPRVEQ MIRDSAKGLN KLS
//
