ID A0A8H3ZQA8_9PEZI Unreviewed; 494 AA.
AC A0A8H3ZQA8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
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=GQ607_012957 {ECO:0000313|EMBL:KAF0319855.1};
OS Colletotrichum asianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=702518 {ECO:0000313|EMBL:KAF0319855.1, ECO:0000313|Proteomes:UP000434172};
RN [1] {ECO:0000313|EMBL:KAF0319855.1, ECO:0000313|Proteomes:UP000434172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 18580 {ECO:0000313|EMBL:KAF0319855.1,
RC ECO:0000313|Proteomes:UP000434172};
RA Meng Y.;
RT "A genome sequence resource for the geographically widespread anthracnose
RT pathogen Colletotrichum asianum.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] +
CC acetate; 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|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037913}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00061569,
CC 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:KAF0319855.1}.
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DR EMBL; WOWK01000090; KAF0319855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H3ZQA8; -.
DR OrthoDB; 1918432at2759; -.
DR Proteomes; UP000434172; Unassembled WGS sequence.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; IEA:TreeGrafter.
DR GO; GO:0034967; C:Set3 complex; IEA:UniProtKB-ARBA.
DR GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:TreeGrafter.
DR FunFam; 3.40.800.20:FF:000007; Histone deacetylase; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR003084; HDAC_I/II.
DR InterPro; IPR000286; HDACs.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF36; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037913};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037913};
KW Reference proteome {ECO:0000313|Proteomes:UP000434172};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 81..379
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 469..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..487
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 494 AA; 55696 MW; 0CA836F636487EF4 CRC64;
MDANAYRFRA PKPNYLPHRA DKDDIVEEYT PLGKASELDE ARYLNKCKRT ALESGITRPK
GYTVSFHCNP EMEKHHFGQT HPMKPWRLTL SKSLIYSYGM SFAMDNYIAR AATYEELNDF
HSDDYLDFLG TVLPEPVPRD VDNANPDLKF NLGGSDCPLF EGLYDYCSMS AGGSLDAARK
ICAQQSDIAV SWGGGLHHAK KAEASGFCYI NDIVLAILQL LRCYPRVLYI DIDVHHGDGV
EEAFYSTDRV MTVSFHKYDP LNFFPGTGGL DDNGPKNEHN PGAHHAINVP LNDGITDEQY
KWLFENVIGQ CMEKFRPSAI ALQCGADSLA GDRLGRFNLQ VQGHGACVEF CKKFNIPMIL
FGGGGYTPRN VARAWAFETS IAIDCQDKID PIIPTHAPWR EQFRYEELFP TLEQILGEPR
ANRNPQKRLN DLVQHVTEQL RFVQAAPSVQ YQVIPPDLGG LREDVEEKLK EEREAENDSI
RKAREEAVGS AMEY
//
