ID A0A135U1E5_9PEZI Unreviewed; 495 AA.
AC A0A135U1E5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
GN ORFNames=CSAL01_12250 {ECO:0000313|EMBL:KXH54187.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH54187.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH54187.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH54187.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000256|PIRNR:PIRNR037913};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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:KXH54187.1}.
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DR EMBL; JFFI01001780; KXH54187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135U1E5; -.
DR STRING; 1209931.A0A135U1E5; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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:SF25; HISTONE DEACETYLASE 3; 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 ECO:0000256|PIRNR:PIRNR037913}; Hydrolase {ECO:0000256|PIRNR:PIRNR037913};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 81..379
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 472..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 233
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 327
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 495 AA; 55696 MW; DC3E8D1BF0490055 CRC64;
MDTDAYRFRV PKPNYLPHRT DKDDIVEEYE PLGQASELDN AKYFAKCKRI AEESGITRPK
GYNVSFHCNP EMEKHHFGQT HPMKPWRLTL SKSLIYSYGM SFAMDNYIAR AATYEELNDF
HSDDYLDFLG TVLPEPVPRD VENANPDLKF NLGGSDCPLF EGLYDYCSMS AGGSLDAARK
ICSNQSDIAV SWGGGLHHAK KAEASGFCYI NDIVLAILQL LRCYPRVLYI DIDVHHGDGV
EEAFYSTDRV MTVSFHKYDP LNFFPGTGGL DDNGPKNEHN PGAHHAINVP LNDGVTDDQY
KWLFENVIGK CMEKFRPSAI ALQCGADSLA GDRLGRFNLQ VQGHGACVEF CKSFGVPMIL
FGGGGYTPRN VARAWAFETS IAIGCQDKID PIIPTHAPWR DQFRYEELFP TLEQILGEPR
VNRNTRKKLD EVLQHVTEQL RFVQSAPSVQ YQTIPPDLGG LRDDVEAALK EQREAENDAV
RKQREEAVGQ AMEYS
//
