GenomeNet

Database: UniProt
Entry: D8QG88_SCHCM
LinkDB: D8QG88_SCHCM
Original site: D8QG88_SCHCM 
ID   D8QG88_SCHCM            Unreviewed;       411 AA.
AC   D8QG88;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE   Flags: Fragment;
GN   ORFNames=SCHCODRAFT_36526 {ECO:0000313|EMBL:EFI93249.1};
OS   Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN   [1] {ECO:0000313|EMBL:EFI93249.1, ECO:0000313|Proteomes:UP000007431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX   PubMed=20622885; DOI=10.1038/nbt.1643;
RA   Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA   de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA   Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA   Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA   Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA   Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA   Woesten H.A.B.;
RT   "Genome sequence of the model mushroom Schizophyllum commune.";
RL   Nat. Biotechnol. 28:957-963(2010).
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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; GL377311; EFI93249.1; -; Genomic_DNA.
DR   RefSeq; XP_003028152.1; XM_003028106.1.
DR   AlphaFoldDB; D8QG88; -.
DR   STRING; 578458.D8QG88; -.
DR   GeneID; 9596872; -.
DR   KEGG; scm:SCHCO_02639326; -.
DR   VEuPathDB; FungiDB:SCHCODRAFT_02639326; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_7_4_1; -.
DR   InParanoid; D8QG88; -.
DR   OMA; GWLRAFH; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000007431; Unassembled WGS sequence.
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   CDD; cd11598; HDAC_Hos2; 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: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   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007431}.
FT   DOMAIN          26..318
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         175
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         177
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         264
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EFI93249.1"
FT   NON_TER         411
FT                   /evidence="ECO:0000313|EMBL:EFI93249.1"
SQ   SEQUENCE   411 AA;  45356 MW;  A6D24049DE6DCE1C CRC64;
     LQPHSRPAVS YYFPKGVGSY HFGELHPMKP HRLTLTNALV MGYGLDKQIH EIFDARPATR
     EELEVYHDAD YIEYLSKVTP QNQKSMKAEV EAHNCGEDCP IFAGMYDFCQ KYAGGTLAAA
     RKLCSGKTDI AINWSGGLHH AKRGEASGFC YVNDIVLGIL ELLRYYPRVL YIDIDIHHGD
     GVELAFYHTN RVMTLSFHKY TGEFFPGTGK LDDNGIGLGK HFALNVPLQD GIDDKMYLDL
     FKSIVNDVRD KYQPSAIVLQ CGADSLGCDR LGAFNLSIAA HGACVGHVRA FGIPLLVVGG
     GGYTLNNVSR CWTYETAVLA GATVPDALPR TPYDSFFADS RWTLHPPLTG RVDNQNTPQS
     LAKITSAIRG KLRYLEGAPS VQMQEIPPDL EGLLAEEVRT AEEQAEERGA E
//
DBGET integrated database retrieval system