ID A5DJS0_PICGU Unreviewed; 452 AA. AC A5DJS0; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 2. DT 27-MAR-2024, entry version 92. 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=PGUG_03521 {ECO:0000313|EMBL:EDK39423.2}; OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Meyerozyma. OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK39423.2, ECO:0000313|Proteomes:UP000001997}; RN [1] {ECO:0000313|EMBL:EDK39423.2, ECO:0000313|Proteomes:UP000001997} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL RC Y-324 {ECO:0000313|Proteomes:UP000001997}; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C., RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M., RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R., RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M., RA Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(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|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; CH408158; EDK39423.2; -; Genomic_DNA. DR RefSeq; XP_001484140.1; XM_001484090.1. DR AlphaFoldDB; A5DJS0; -. DR STRING; 294746.A5DJS0; -. DR GeneID; 5126380; -. DR KEGG; pgu:PGUG_03521; -. DR VEuPathDB; FungiDB:PGUG_03521; -. DR eggNOG; KOG1342; Eukaryota. DR HOGENOM; CLU_007727_7_4_1; -. DR InParanoid; A5DJS0; -. DR OMA; GWLRAFH; -. DR OrthoDB; 1327607at2759; -. DR Proteomes; UP000001997; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProt. 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:SF25; HISTONE DEACETYLASE 3; 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:UP000001997}; KW Transcription {ECO:0000256|PIRNR:PIRNR037913}; KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}. FT DOMAIN 50..342 FT /note="Histone deacetylase" FT /evidence="ECO:0000259|Pfam:PF00850" FT REGION 428..452 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 164 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2" FT BINDING 172 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2" FT BINDING 199 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3" FT BINDING 201 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3" FT BINDING 288 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3" FT BINDING 327 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2" SQ SEQUENCE 452 AA; 51577 MW; 10390C4AB77FC29A CRC64; MSVPVSETDT FSPDKKTAEN TPFYDSICKQ SNVSYHFNPE VSQYHFGPYH PMKPFRLMLT DHLVISYKLY EKMDLYTPRR ATKEELLEFH SDDYIDFLAK VTPETVTKLP ESTLAHFNIG DDCPVFDGMY DYSTIYAGAT LDASRKLISG MSDIAINWSG GLHHAKKYEP SGFCYVNDIV LSIINLLRVH PRVMYIDIDL HHGDGVQEAF YATDRVMTVS FHKYNGEFFP GTGSIDERGM DKGKNFAINV PLKDGIDDES YVRLFKSIME PLITKFQPTC IVQQCGADSL GYDRLGCFNL NIKAHGECVK FIKSFEIPML VLGGGGYTPR NVSRLWCYET SVLTDVTLNH KIPNYLPSYD WFGPDFSLHP QLDGRIDNKN SKKYLESVKQ DILEQLRYLA YAPSVQMQEI PPDITGLTED EDQIIKELNE EQDGTRETQN TKDEARVGEL RE //