ID E9BF59_LEIDO Unreviewed; 430 AA. AC E9BF59; A0A3S7WWE6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 64. 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=LDBPK_210740 {ECO:0000313|EMBL:CBZ33885.1}, LdCL_210012300 GN {ECO:0000313|EMBL:AYU78534.1}; OS Leishmania donovani. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania. OX NCBI_TaxID=5661 {ECO:0000313|EMBL:CBZ33885.1, ECO:0000313|Proteomes:UP000008980}; RN [1] {ECO:0000313|EMBL:CBZ33885.1, ECO:0000313|Proteomes:UP000008980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BPK282A1 {ECO:0000313|EMBL:CBZ33885.1, RC ECO:0000313|Proteomes:UP000008980}; RX PubMed=22038251; DOI=10.1101/gr.123430.111; RA Downing T., Imamura H., Decuypere S., Clark T.G., Coombs G.H., Cotton J.A., RA Hilley J.D., de Doncker S., Maes I., Mottram J.C., Quail M.A., Rijal S., RA Sanders M., Schonian G., Stark O., Sundar S., Vanaerschot M., RA Hertz-Fowler C., Dujardin J.C., Berriman M.; RT "Whole genome sequencing of multiple Leishmania donovani clinical isolates RT provides insights into population structure and mechanisms of drug RT resistance."; RL Genome Res. 21:2143-2156(2011). RN [2] {ECO:0000313|EMBL:CBZ33885.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BPK282A1 {ECO:0000313|EMBL:CBZ33885.1}; RA Zhao B.P., Ren Z.A., Li C.D.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000008980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BPK282A1 {ECO:0000313|Proteomes:UP000008980}; RA Downing T., Imamura H., Sanders M., Decuypere S., Hertz-Fowler C., RA Clark T.G., Rijal S., Sundar S., Quail M.A., De Doncker S., Maes I., RA Vanaerschot M., Stark O., Schonian G., Dujardin J.C., Berriman M.; RT "Whole genome sequencing of Leishmania donovani clinical lines reveals RT dynamic variation related to drug resistance."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:AYU78534.1, ECO:0000313|Proteomes:UP000274082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LdCL {ECO:0000313|EMBL:AYU78534.1, RC ECO:0000313|Proteomes:UP000274082}; RX PubMed=30409989; DOI=10.1038/s41598-018-34812-x; RA Lypaczewski P., Hoshizaki J., Zhang W.-W., McCall L.-I., RA Torcivia-Rodriguez J., Simonyan V., Kaur A., Dewar K., Matlashewski G.; RT "A complete Leishmania donovani reference genome identifies novel genetic RT variations associated with virulence."; RL Sci. Rep. 8:16549-16549(2018). 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|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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP029520; AYU78534.1; -; Genomic_DNA. DR EMBL; FR799608; CBZ33885.1; -; Genomic_DNA. DR RefSeq; XP_003860591.1; XM_003860543.1. DR AlphaFoldDB; E9BF59; -. DR SMR; E9BF59; -. DR EnsemblProtists; CBZ33885; CBZ33885; LDBPK_210740. DR GeneID; 13386404; -. DR KEGG; ldo:LDBPK_210740; -. DR VEuPathDB; TriTrypDB:LdBPK_210740.1; -. DR VEuPathDB; TriTrypDB:LdCL_210012300; -. DR VEuPathDB; TriTrypDB:LDHU3_21.0800; -. DR OMA; FHSEEYM; -. DR OrthoDB; 1327607at2759; -. DR PhylomeDB; E9BF59; -. DR Proteomes; UP000008980; Chromosome 21. DR Proteomes; UP000274082; Chromosome ldcl_21. 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 Transcription {ECO:0000256|PIRNR:PIRNR037913}; KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}. FT DOMAIN 43..333 FT /note="Histone deacetylase" FT /evidence="ECO:0000259|Pfam:PF00850" FT ACT_SITE 155 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1" FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2" FT BINDING 163 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2" FT BINDING 190 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3" FT BINDING 192 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3" FT BINDING 279 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3" FT BINDING 318 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2" SQ SEQUENCE 430 AA; 47389 MW; 0E5EA4D37A4C8459 CRC64; MHAVHKDDAR APLLNTESRC RVALIDTSGY ASDMNISAFV PQHAMKPYRV LAAMEIVRSL KIDAHCRTVV PPLVKVEELM AYHTDTYLAN LGLHSCRSWL WNAETSKVFF SGDCPPVEGL MEHSIATASG TLMGAVLLNS GQVDVAVHWG GGMHHSKCGE CSGFCYVNDI VLGILELLKC HDRVLYVDID MHHGDGVDEA FCTSDRVFTL SLHKFGESFF PGTGHPRDVG YGRGRYYSMN LAVWDGITDF YYLGVFEHAL HSIVRRYSPD VIVLQCGADS LAGDRLGLLN LSSFGHGQCV QAVRDLGIPM LALGGGGYTI RNVAKLWAYE TSILTGHPLP PNTVLPVAEM PLSGWLFQDS PLLIVAQDRS NHVLPGLHCQ RAYQMMTEQI DRHVPHIQPH PRLQKASTEA AAVDKQVEDG TTAVEDFKRQ //