ID A0A2C5X9Z4_9HYPO Unreviewed; 502 AA.
AC A0A2C5X9Z4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=CDD81_5561 {ECO:0000313|EMBL:PHH63689.1};
OS Ophiocordyceps australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH63689.1, ECO:0000313|Proteomes:UP000226192};
RN [1] {ECO:0000313|EMBL:PHH63689.1, ECO:0000313|Proteomes:UP000226192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map64 {ECO:0000313|EMBL:PHH63689.1,
RC ECO:0000313|Proteomes:UP000226192};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHH63689.1}.
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DR EMBL; NJET01000044; PHH63689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5X9Z4; -.
DR STRING; 1399860.A0A2C5X9Z4; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000226192; 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:0010468; P:regulation of gene expression; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000226192};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 89..388
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT COILED 470..498
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 241
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 243
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 335
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 374
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 502 AA; 56355 MW; BA5A75E05FF2054E CRC64;
MDAPADSPYR FRVPKPNYLP HIVNGDGHGR DDIVQEYVPL GLPGDVENVK FFHKCRRQAE
ESGITRPKGY TVSFHCNPDM ERHHFGMTHP MKPWRLTLSK SLIYSYGMSF AMDNFVSRAA
TYEELADFHS TDYLDFLGTV LPEPVPRDVE NQNPDLRFNL GGSDCPLFEG LYDYCSLSAG
GALDAARKIC THQSDIAIAW GGGLHHAKKA EASGFCYIND IVLAILQLLR QYPRVLYIDI
DVHHGDGVEE AFFSTDRVMT CSFHKYDPHN FFPGTGALDD NGPKNEHNAG AHHAVNVPLN
DGITDEQYDM LFNNIVGNIV DKFRPSAVVL QCGADSLAGD RLGRFNLQVQ GHGACVEFCK
RMSLPLILFG GGGYTPRNVA RAWTYETSIA TGCNDKISPI LPQHAPWREQ FRHDTLFPTL
EQILGEPRQN KNTTKRLQEI VQHVTEQLRF VQAAPSTQMQ QVPPDLGGIR DDVEDRIKEE
AAERNDELRR IREAAVATPM EF
//
