ID D8QAG8_SCHCM Unreviewed; 554 AA.
AC D8QAG8;
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};
GN ORFNames=SCHCODRAFT_77889 {ECO:0000313|EMBL:EFI95399.1};
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:EFI95399.1, 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}.
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DR EMBL; GL377308; EFI95399.1; -; Genomic_DNA.
DR RefSeq; XP_003030302.1; XM_003030256.1.
DR AlphaFoldDB; D8QAG8; -.
DR STRING; 578458.D8QAG8; -.
DR GeneID; 9592477; -.
DR KEGG; scm:SCHCO_02630612; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02630612; -.
DR eggNOG; KOG1342; Eukaryota.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; D8QAG8; -.
DR OMA; WTFETAC; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000007431; Unassembled WGS sequence.
DR GO; GO:1902494; C:catalytic complex; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
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:SF5; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 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 Reference proteome {ECO:0000313|Proteomes:UP000007431}.
FT DOMAIN 23..312
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 374..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 62216 MW; 29A20F8BF49564A3 CRC64;
MSKRRVTYYY DPDVGAYTYG LGHPMKPHRI RVAHELISAY GMLDKMHVLK AKRATPERMT
AFHTDEYVDF LNKVSPETVR ELTYNGSRFL VGDDNPAFEG VFEYCQTSAG GSIAAANRIA
SGATDIAINW AGGLHHAKKR EASGFCYIND IVLGIIELLR TYPRVLYVDI DCHHGDGVEE
AFYTTDRVMT CSFHKYGEYF PGTGTQEDTG VGRGTGYAVN VPFKDGLTDE SLASVFEPII
DKILEVFQPS AVVLQCGSDS LSGDKLGCFN LTMQGHAHCV QFLRSKNIPL ILLGGGGYTV
KNVGRTWAYE TACALGIEDT IDPNLPWNEY FEWFGPRYRL EVVASNMEDL NVKEGSLETV
KNIALKNLNA IKGPPSVQMQ DVPRQPLGDH LKTKRTEDEE DDERDNLDRR LAQHARYVYD
LQQSSMASSS QSDSSYDSDD SEQPISTSVH RRAAAQKTKQ RMSIRTNRYF DVPAEPEYAH
YDCGALPGNK AKRRFFRMGS RMEDDMGMGE RMRPNGTVKL FDVHSTMTNG GRTPEREWDR
HEDEDESDMD VDGP
//
