ID F8Q8R3_SERL3 Unreviewed; 541 AA.
AC F8Q8R3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=SERLA73DRAFT_95597 {ECO:0000313|EMBL:EGN94968.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR EMBL; GL945486; EGN94968.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q8R3; -.
DR STRING; 936435.F8Q8R3; -.
DR eggNOG; KOG1342; Eukaryota.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; F8Q8R3; -.
DR OMA; RCHTDEY; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000008063; 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 CDD; cd09991; HDAC_classI; 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: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:UP000008063}.
FT DOMAIN 23..312
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 369..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 61017 MW; D165561F4CED3831 CRC64;
MSKRRVAYYY DGDVGSFTYG LGHPMKPHRI RITHDLVSAY DMLDKMHILR PKRASPEAMT
SFHTDEYVHF LNRVTPETAE QLTYHGTRFL MGEDNPAFEG VFDFCTISAG GSICAAQRIS
SGAVDIAINW AGGLHHAKKR EASGFCYIND IVLGILELLR TYSRVLYIDI DCHHGDGVEE
AFYTTDRVMT CSFHKFGEYF PGTGTQDDCG RGKGKGYAVN VPLKDGLTDE AFKSIFEPIV
SKCMQVFAPS VVVLQCGADS LAGDKLGCFN ITMHGHAHCV QFLRKQNIPL ILLGGGGYTI
KNVARVWTYE TACALGIEDT IDEKLPWNEY FEWFGPRYRL EVPENNMEDL NVRDGSLDKV
RTTALEQLGA LPGPPSVGMH DVPRESLGQH LGYWDDGDEN SRNELDERLA QYSRLVYNLQ
EEEESDESDD TDPYQWESDD DSADRRRRHR TRMSILTNKH VDVDPDGHPG RKGRRRFFRS
DTQWDETYKR ALARSANPEA FGLRTVGIMD IPGAMERGGR AGSIIEGDMN IDDEWEDNTS
L
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