ID A0A0A0LS04_CUCSA Unreviewed; 465 AA.
AC A0A0A0LS04;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=Csa_1G004130 {ECO:0000313|EMBL:KGN63547.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN63547.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN63547.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
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; CM002922; KGN63547.1; -; Genomic_DNA.
DR RefSeq; XP_004138094.1; XM_004138046.2.
DR AlphaFoldDB; A0A0A0LS04; -.
DR STRING; 3659.A0A0A0LS04; -.
DR EnsemblPlants; KGN63547; KGN63547; Csa_1G004130.
DR GeneID; 101204443; -.
DR Gramene; KGN63547; KGN63547; Csa_1G004130.
DR KEGG; csv:101204443; -.
DR eggNOG; KOG1342; Eukaryota.
DR OMA; GKIMEWY; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000029981; Chromosome 1.
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 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: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|PIRSR:PIRSR037913-3};
KW Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981};
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 39..330
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 390..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
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 465 AA; 52309 MW; 6B455456E309D70F CRC64;
MSDDIHGGAS LPSGPDGRKR RVTYFYEPTI GDYYYGQGHP MKPHRIRMAH NLIVHYGLHR
RMEINRPYPA GPEDIRRFHS DDYVDFLASV SPETLSDHAF SRHLKRFNVG EDCPVFDGLF
GFCQASAGGS IGAAVKLNRG DADIAINWAG GLHHAKKSEA SGFCYVNDIV LGILELLKYH
KRVLYIDIDV HHGDGVEEAF YTTDRVMTVS FHKFGDFFPG TGHIKDVGVG TGKNYALNVP
LNDGMDDDSF RGLFRPLIQK VMEVYQPDAV VLQCGADSLS GDRLGCFNLS VKGHADCLRF
LRSFNVPLMV LGGGGYTIRN VARCWCYETA VAVGVEPDNK LPYNEYFEYF GPDYALHIEP
SNMENLNSPK DMEKIRNTLL EQLSRLPHAP SVPFQMTPSS EIPEEVEESI ERRPKRRIWN
GEDYDSDSEE NRKRPNISEG TGVNNLTRDV VDDMEEDKNM GHQCC
//
