ID   G2RFA7_THETT            Unreviewed;       496 AA.
AC   G2RFA7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-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=THITE_46814 {ECO:0000313|EMBL:AEO70390.1};
OS   Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126) (Thielavia
OS   terrestris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides;
OC   Thermothielavioides terrestris.
OX   NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO70390.1, ECO:0000313|Proteomes:UP000008181};
RN   [1] {ECO:0000313|EMBL:AEO70390.1, ECO:0000313|Proteomes:UP000008181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA   Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA   Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA   Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA   Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA   Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA   Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA   Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT   Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
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; CP003013; AEO70390.1; -; Genomic_DNA.
DR   RefSeq; XP_003656726.1; XM_003656678.1.
DR   AlphaFoldDB; G2RFA7; -.
DR   STRING; 578455.G2RFA7; -.
DR   GeneID; 11522540; -.
DR   KEGG; ttt:THITE_46814; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_7_4_1; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000008181; Chromosome 5.
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}; 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:UP000008181};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT   DOMAIN          83..382
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          471..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         235
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         237
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         329
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ   SEQUENCE   496 AA;  56105 MW;  2ABFAA87E4EE8842 CRC64;
     MDVSAYRYRP PKPNYLPHDI EVDDPIVEEY TIPLGKADDR ENAIFFNKMK LAAQEYGIVR
     PKGYTVSYHA TPEMEKHHFG QTHPMKPWRL TLTKSLVTAY GMPFAMDNYL TREATYEELN
     SFHSNDYLDY LITAAPEDQP RDIDNPDKEV KFNLGGSDCP LFHGLYNYCS MSAGSSLDAA
     RKICSNQSDI AIAWGGGLHH AKRSEASGFC YINDIVLAIL QLLRIYPRVL YIDIDVHHGD
     GVEEAFFSTD RVMTVSFHKY QPDQFFPGTG ALEDNGPKNE HNPGAHHAIN VPLNDGITDE
     QYEALFKNII GPINERYRPS AIALQCGADS LAGDRLGRFN LRVQGHGACV RYCKSLGLPM
     ILFGGGGYTP RNVARAWAYE TSIAIGADTR IPETIPEHTP WRAHFIHDTL FPSLEQSMHE
     PRHNRNSEKR LREIVAHVHE QLRFVEHAPS VQSQIIPPDL EGIRDEVEAR LKEESEEKDD
     GLRKIREEGV GQAMEF
//