ID A0A1J8QZ70_9AGAM Unreviewed; 539 AA.
AC A0A1J8QZ70;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=AZE42_00840 {ECO:0000313|EMBL:OJA18800.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA18800.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA18800.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA18800.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-2016) 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:OJA18800.1}.
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DR EMBL; LVVM01001315; OJA18800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8QZ70; -.
DR STRING; 180088.A0A1J8QZ70; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000183567; 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:SF13; HISTONE DEACETYLASE HDAC1; 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:UP000183567}.
FT DOMAIN 34..303
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 380..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 59325 MW; CA6779DDEB2B4C5D CRC64;
MSENMAPLDG ESQKKRVCYF FDSDIGGFHY GPGHPMKPTR IRMCHSLVMN YGLYKKMEIF
RAKPATKREM TQFHSDEYVD FLNNVGDDCP VFDGLFDYCS ISAGGSMEGA ARLSRDKCDI
AINWAGGLHH AKKSEASGFC YVNDIVLGIL ELLRYHTRVL YIDIDVHHGD GVEEAFYTTD
RVMTVSFHKY GEYFPGTGEL RDIGIGKGKY YSLNFPLRDG ISDENYKSVF EPVIRQVMES
YDPSAIVLQC GTDSLSGDKL GCLNLSMRGH ANCVKFVKSF NKPLLLLGGG GYTMRNVSRA
WAFETGLAAG VELAPEIPVN EYYEYFGPDY ELDVRSSNTE DMNTPEYLER VKNIVLDNLR
HLGGPPSVQM SDVPKMPIDE AMDDSRQDED LIPPDTRRHR RLLDSRIQAD GELSDSDDEG
EGGRRDHAHH RDRDSEPRSH SSEVESAAGR RFGIGVGILS SGAAGSTHGA GPSGHTTVVR
PVLSGHLPME ASTPTTIESG PTPIEPSVVN GTTDHTSGDK SPKTNGMVVD HDNGASGES
//
