ID E1ZDQ1_CHLVA Unreviewed; 453 AA.
AC E1ZDQ1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
GN ORFNames=CHLNCDRAFT_145535 {ECO:0000313|EMBL:EFN56062.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN [1] {ECO:0000313|EMBL:EFN56062.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN56062.1,
RC ECO:0000313|Proteomes:UP000008141};
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
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:PIRNR037913};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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DR EMBL; GL433843; EFN56062.1; -; Genomic_DNA.
DR RefSeq; XP_005848164.1; XM_005848102.1.
DR AlphaFoldDB; E1ZDQ1; -.
DR STRING; 554065.E1ZDQ1; -.
DR GeneID; 17355208; -.
DR KEGG; cvr:CHLNCDRAFT_145535; -.
DR eggNOG; KOG1342; Eukaryota.
DR InParanoid; E1ZDQ1; -.
DR OMA; QYIAYGF; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000008141; 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 CDD; cd09991; HDAC_classI; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF13; HISTONE DEACETYLASE HDAC1; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR037913}; Hydrolase {ECO:0000256|PIRNR:PIRNR037913};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW Reference proteome {ECO:0000313|Proteomes:UP000008141};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 25..340
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 193
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 195
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 286
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 453 AA; 51696 MW; 715608C3CE636497 CRC64;
MSGRKNKIAY FYDNDYTGYY YGPDHPMKPQ RIAMTHQLVL GYGLHKHLDV YRPRLAQYDE
LTAFHSEEFI DMLRSTTPEM QARRRAQGQA LHSMHSMHSM LKAKWDSYLR WGIEYDCPIF
HGLFKFCRQY AAASIDGAYK LNHGQADIAI NWAGGLHHAK KAEASGFCYI NDCVLGILEL
LKHNPRVLYI DIDIHHGDGV EEAFYTTDRV MCVSFHLKQE WGGQPFFPGT GALEEIGEYQ
GKGYSLNVPL VQGIDTEQYL GLFKPIISKV MEVFQPGAIV LQCGADSLVG DRLGMFNLTL
EGHAEAVRYV KSFGLPILVL GGGGYTKTTV ARAWTLETAV LCEQEVEDAL PQQMYLDYFS
PEYRLHYNRR PTWPNQNKKE EVERIKTTLL QQLQQLQGAP GFAMRERPPD ALLPEFAAED
EDQVHSRLKG YVKMHFEHNL KCVEKGLIDP YNA
//
