ID U4LD59_PYROM Unreviewed; 590 AA.
AC U4LD59;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=PCON_04446 {ECO:0000313|EMBL:CCX17442.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX17442.1};
RN [1] {ECO:0000313|EMBL:CCX17442.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX17442.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX17442.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR EMBL; HF936646; CCX17442.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LD59; -.
DR STRING; 1076935.U4LD59; -.
DR eggNOG; KOG1342; Eukaryota.
DR OMA; MEYYQPT; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000018144; 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}.
FT DOMAIN 3..281
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 338..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..484
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 65199 MW; F96D438589401BB7 CRC64;
MTHSLIMNYG LYKKMEIYRA KPATKQEMCQ FHTDEYIDFL SKVTPDNMEA YQKEQGKYNV
GDDCPVFDGL FEFCGISGGG SMEGAARLNR AKCDIAINWA GGLHHAKKSE ASGFCYLNDI
VLGIIELLRY KQRVLYIDID VHHGDGVEEA FYTTDRVMTC SFHKYGEYFP GTGELRDIGV
GSGKYYAVNF PLRDGITDVT YKEVFEPVIS HIMEFYRPEA VVLQCGADSL SGDRLGCFNL
SMRGHANCVE FVKKFNLPTL VVGGGGYTMR NVSRAWCYET GVLVDQIVGP ELPYSDFYEY
FGPDYELDVK PSNMENLNSK EYLEKIKIQV LSNLERTRHT PSVQMSDVGR GLTEHQEEQD
AMLDDLEEDT VGMDRRHTQR TWDREIEKPG ELSESEDEEI NESMGIRRQP GRKRRRNQQN
YKESNVSGSG SAAATPQPGA SGSASDAGAP ASTTLLAGYN GEHDEELEAL AKEADDDGDV
DMDQAEEPQE KRTKLDTPVA ADADDEVMAD AEPAKETPAP AEKEEVPAET ESSDAAPAAA
ATSTEAPKEV ATEPETSSTG AAEKPATPEE KPVEKAEEKA SAEGKPEEKP
//
