ID A0A060SXK1_PYCCI Unreviewed; 268 AA.
AC A0A060SXK1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=BN946_scf184747.g61 {ECO:0000313|EMBL:CDO77248.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO77248.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO77248.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO77248.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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:CDO77248.1}.
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DR EMBL; CCBP010000446; CDO77248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SXK1; -.
DR STRING; 5643.A0A060SXK1; -.
DR HOGENOM; CLU_007727_5_0_1; -.
DR OMA; RIALTHC; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000029665; 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; 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 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:UP000029665}.
FT DOMAIN 23..258
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 188
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 190
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
SQ SEQUENCE 268 AA; 30469 MW; 56ACEAAF772FE6F2 CRC64;
MSKKRVAYYY DPDVGSYTYG LTHAMKPQRM RITHELVSAY DLLPKMHVLV RTTPSTRMYS
FLTRPQRPKR ATAETMTRFH TDEYIDFLSK VTPENSRRLT YQGTRFLVGD DNPPFEGVFE
FSSISAGGSI AAAKRLMEGQ ADIAINWAGG LHHAKKREAS GFCYINDIVL AILEMLRYVP
RVLYIDIDCH HGDGVEEAFY TTDRVMTCSF HKYGEFFPGT GQIEDRGRGP GRGYALNVPL
KDGITDEAYK SIFVPVRLPF SVHCFHTP
//
