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Database: UniProt/TrEMBL
Entry: D7MEW2_ARALL
LinkDB: D7MEW2_ARALL
Original site: D7MEW2_ARALL 
ID   D7MEW2_ARALL            Unreviewed;       500 AA.
AC   D7MEW2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 66.
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=ARALYDRAFT_327775 {ECO:0000313|EMBL:EFH45092.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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; GL348719; EFH45092.1; -; Genomic_DNA.
DR   RefSeq; XP_002868833.1; XM_002868787.1.
DR   AlphaFoldDB; D7MEW2; -.
DR   STRING; 81972.D7MEW2; -.
DR   EnsemblPlants; fgenesh1_pm.C_scaffold_7000002; fgenesh1_pm.C_scaffold_7000002; fgenesh1_pm.C_scaffold_7000002.
DR   GeneID; 9304905; -.
DR   Gramene; fgenesh1_pm.C_scaffold_7000002; fgenesh1_pm.C_scaffold_7000002; fgenesh1_pm.C_scaffold_7000002.
DR   KEGG; aly:9304905; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_7_12_1; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0016580; C:Sin3 complex; IEA:EnsemblPlants.
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:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR   GO; GO:0009294; P:DNA-mediated transformation; IEA:EnsemblPlants.
DR   GO; GO:0009861; P:jasmonic acid and ethylene-dependent systemic resistance; IEA:EnsemblPlants.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:EnsemblPlants.
DR   GO; GO:1901001; P:negative regulation of response to salt stress; IEA:EnsemblPlants.
DR   GO; GO:1902459; P:positive regulation of stem cell population maintenance; IEA:EnsemblPlants.
DR   GO; GO:2000026; P:regulation of multicellular organismal development; IEA:EnsemblPlants.
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; PTHR48252:SF19; HISTONE DEACETYLASE 19; 1.
DR   PANTHER; PTHR48252; HISTONE DEACETYLASE 2-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:UP000008694};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR037913};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR037913}.
FT   DOMAIN          36..324
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          383..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         184
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         186
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         272
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ   SEQUENCE   500 AA;  55867 MW;  771CE99F2454C6C7 CRC64;
     MDTGGNSLAS GPDGVKRKVC YFYDPEVGNY YYGQGHPMKP HRIRMTHALL AHYGLLQHMQ
     VLKPFPARDR DLCRFHADDY VSFLRSITPE TQQDQIRQLK RFNVGEDCPV FDGLYSFCQT
     YAGGSVGGSV KLNHGLCDIA INWAGGLHHA KKCEASGFCY VNDIVLAILE LLKQHERVLY
     VDIDIHHGDG VEEAFYATDR VMTVSFHKFG DYFPGTGHIQ DIGYGNGKYY SLNVPLDDGI
     DDESYHLLFK PIMGKVMEVF RPGAVVLQCG ADSLSGDRLG CFNLSIKGHA ECVKFMRSFN
     VPLLLLGGGG YTIRNVARCW CYETGVALGV EVEDKMPEHE YYEYFGPDYT LHVAPSNMEN
     KNSRQMLEEI RNDLLHNLSK LQHAPSVPFQ ERPPDTEAPE VDEDQEDGDK RWDPDSDMDV
     DDDRKPIPSR VKREAVEPDT KDKDGLKGVM ERGKGCEVGV DESGSSKVTG VNPVGMEEAS
     VKMEEEGTNK GGADQVFPKI
//
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