ID Q5KF65_CRYNJ Unreviewed; 466 AA.
AC Q5KF65; Q55R02;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 123.
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 OrderedLocusNames=CNF02840 {ECO:0000313|EMBL:AAW44291.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW44291.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW44291.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
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DR EMBL; AE017346; AAW44291.1; -; Genomic_DNA.
DR RefSeq; XP_571598.1; XM_571598.1.
DR AlphaFoldDB; Q5KF65; -.
DR STRING; 214684.Q5KF65; -.
DR PaxDb; 214684-Q5KF65; -.
DR EnsemblFungi; AAW44291; AAW44291; CNF02840.
DR GeneID; 3258243; -.
DR KEGG; cne:CNF02840; -.
DR VEuPathDB; FungiDB:CNF02840; -.
DR eggNOG; KOG1342; Eukaryota.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; Q5KF65; -.
DR OMA; GKIMEWY; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000002149; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; 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 GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd10004; RPD3-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 32..320
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 382..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 180
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 182
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 268
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 466 AA; 52756 MW; 674E0DEE1CD0A8AF CRC64;
MGSMEPILGE SKRRVCYFFD SDIGNYHYGP GHPMKPTRIR MCHSLVMNYG LYKKMEIFRA
KPATKREMSQ FHTDEYVDFL YRINPDNAAQ FAKEQVKYNV GDDCPIFDGL FEYCSISAGG
SMEGAARLSR DKCDIAVNWA GGLHHAKKAE ASGFCYVNDI VLGILELLRY HQRVLYIDID
VHHGDGVEEA FYTTDRVMTC SFHKYGEFFP GTGEVRDNGI GKGKGYAINV PLRDGISDDN
YKSIFQPVIK RVIEWYQPGA VVLQCGSDSL SGDRLGSFNL SMKGHAACVQ FVKSFNLPLL
LLGGGGYTVK SVSRTWAYET GLAAGMELGR DLPNNEYWEY YGPDYELDVR SSNMTDQNTP
EYLQKVTEAV FEVLRDKNAA PSVPLQSIPK MMHDDEDEDE GEDNEDRDVR RPARLWAREK
QHETSLSDSE DEGTGGRRHR RSYKESAQKN TMVEDQCNFR VNAGFT
//
