ID K3YHJ1_SETIT Unreviewed; 458 AA.
AC K3YHJ1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 Name=101754782 {ECO:0000313|EnsemblPlants:KQL01448};
GN ORFNames=SETIT_6G118400v2 {ECO:0000313|EMBL:RCV30727.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL01448, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EMBL:RCV30727.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL01448,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV30727.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV30727.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV30727.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQL01448}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL01448};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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; AGNK02003739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003533; RCV30727.1; -; Genomic_DNA.
DR RefSeq; XP_004973247.1; XM_004973190.2.
DR AlphaFoldDB; K3YHJ1; -.
DR STRING; 4555.K3YHJ1; -.
DR EnsemblPlants; KQL01448; KQL01448; SETIT_013709mg.
DR GeneID; 101754782; -.
DR Gramene; KQL01448; KQL01448; SETIT_013709mg.
DR KEGG; sita:101754782; -.
DR eggNOG; KOG1342; Eukaryota.
DR HOGENOM; CLU_007727_7_12_1; -.
DR InParanoid; K3YHJ1; -.
DR OMA; GKIMEWY; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000004995; Chromosome VI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF14; HISTONE DEACETYLASE 6; 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|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037913-3}; Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 41..330
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 387..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 189
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 191
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 277
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 458 AA; 50904 MW; B4786E0AA7875B92 CRC64;
MAASGEGASL PSPAGGEDAH RRRVSYFYEP SIGDYYYGQG HPMKPHRIRM AHSLVVHYGL
HRLLELSRPY PASDADIRRF HSDEYVAFLA SATGNPGMLD PRAVKRFNVG EDCPVFDGLF
PFCQASAGGS IGAAVKLNRG DADITINWAG GLHHAKKSEA SGFCYVNDIV LAILELLKFH
RRVLYVDIDV HHGDGVEEAF FTTNRVMTVS FHKYGDFFPG TGHITDVGAA EGKHYALNVP
LSDGIDDATF RDLFQCIMKK VMEVYQPDVV VLQCGADSLA GDRLGCFNLS VKGHADCLRF
LRSYNVPLMV LGGGGYTIRN VARCWCYETA VAVGVEPDNK LPYNDYYEYF GPDYTLHIQP
KSVENTNTTK DLENIKNMIL ENLSRIEHVP STQFHDRPSD PEAPEEKEED MDKRPPQRSR
LWSGGAYDSD TEDPDNVKSE GNDLIANSHM KEEPNDGL
//