ID A0A5P1ELN9_ASPOF Unreviewed; 356 AA.
AC A0A5P1ELN9;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 08-OCT-2025, entry version 23.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=A4U43_C06F11000 {ECO:0000313|EMBL:ONK66694.1};
OS Asparagus officinalis (Garden asparagus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC Asparagoideae; Asparagus.
OX NCBI_TaxID=4686 {ECO:0000313|EMBL:ONK66694.1, ECO:0000313|Proteomes:UP000243459};
RN [1] {ECO:0000313|Proteomes:UP000243459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH0086 {ECO:0000313|Proteomes:UP000243459};
RX PubMed=29093472; DOI=10.1038/s41467-017-01064-8;
RA Harkess A., Zhou J., Xu C., Bowers J.E., Van der Hulst R., Ayyampalayam S.,
RA Mercati F., Riccardi P., McKain M.R., Kakrana A., Tang H., Ray J.,
RA Groenendijk J., Arikit S., Mathioni S.M., Nakano M., Shan H.,
RA Telgmann-Rauber A., Kanno A., Yue Z., Chen H., Li W., Chen Y., Xu X.,
RA Zhang Y., Luo S., Chen H., Gao J., Mao Z., Pires J.C., Luo M., Kudrna D.,
RA Wing R.A., Meyers B.C., Yi K., Kong H., Lavrijsen P., Sunseri F.,
RA Falavigna A., Ye Y., Leebens-Mack J.H., Chen G.;
RT "The asparagus genome sheds light on the origin and evolution of a young Y
RT chromosome.";
RL Nat. Commun. 8:1279-1279(2017).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM007386; ONK66694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5P1ELN9; -.
DR Gramene; ONK66694; ONK66694; A4U43_C06F11000.
DR OMA; EIGFPWS; -.
DR OrthoDB; 437693at2759; -.
DR Proteomes; UP000243459; Chromosome 6.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:TreeGrafter.
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 4: Predicted;
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:UP000243459};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 58..340
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
SQ SEQUENCE 356 AA; 40011 MW; D68CF76D9C94CA43 CRC64;
MATASSSIPQ PRLPAATETV RRNRILSSKL YFDVPLAKVP VIYSPSYDIA FLGIEKLHPF
DSSKWGRICQ FLIKEGVLDK NRIVEPLEAL KDDLLVVHSE SYLASLKSSL NVSIIVEVPP
VAFLPNWLVQ KKVLYPFRKQ VGGSILAAKL AKERGWAINV GGGFHHCSAE KGGGFCVYAD
ITLCIQYAFV RLNISRVMII DLDAHQGNGY EIDFSNDSRV YVLDMYNSQI YPFDYEAKRY
IDHKVELVSG TKTKEYLEEL DKALEVARNN FDPQLVIYNA GTDILDGDPL GRLKISPEGV
AIRDEKVFRF AREKDIPLLM LTSGGYMKTS ARVIADSITN LSKKRLIDME VLQSRK
//
