ID A0A0F9ZEW2_9MICR Unreviewed; 417 AA.
AC A0A0F9ZEW2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=AAJ76_800019192 {ECO:0000313|EMBL:KKO75974.1};
OS Vairimorpha ceranae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC Vairimorpha.
OX NCBI_TaxID=40302 {ECO:0000313|EMBL:KKO75974.1, ECO:0000313|Proteomes:UP000034350};
RN [1] {ECO:0000313|EMBL:KKO75974.1, ECO:0000313|Proteomes:UP000034350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA08 1199 {ECO:0000313|EMBL:KKO75974.1,
RC ECO:0000313|Proteomes:UP000034350};
RX PubMed=25914091;
RA Pelin A., Selman M., Aris-Brosou S., Farinelli L., Corradi N.;
RT "Genome analyses suggest the presence of polyploidy and recent human-driven
RT expansions in eight global populations of the honeybee pathogen Nosema
RT ceranae.";
RL Environ. Microbiol. 0:0-0(2015).
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:KKO75974.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPQZ01000008; KKO75974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9ZEW2; -.
DR VEuPathDB; MicrosporidiaDB:AAJ76_800019192; -.
DR VEuPathDB; MicrosporidiaDB:G9O61_00g012180; -.
DR VEuPathDB; MicrosporidiaDB:NCER_100451; -.
DR OMA; RCHTDEY; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000034350; 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 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:SF11; HISTONE DEACETYLASE 19; 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:UP000034350};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 22..311
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 396..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 170
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 258
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 417 AA; 46851 MW; 2F61E6CEFD6057C2 CRC64;
MTKNIVYFYD PEIGIYHYAT GHPMKPLRVR MTHSLIVNYG LYRKMDILKP FMASYKNLTN
FHSIDYINFL SSVTTENMQE ITSDLTKFNV KDDCPVFSGL YDFCRLTAGG TMYAAQKINS
GKYDIAINWS GGLHHAKRNE ASGFCYVNDI VLGILELLKY NKRVLYIDID VHHGDGVEEA
FYTTDRVMTV SFHKHGDYFP GTGSIDDIGL GKGKNYAVNV PLRNGIDDVT YIALFKSIID
KVMDLYRPNA VILQCGADSL AGDKLGCFNL SHIGHSECVK HVKSFNIPLI LLGGGGYTIG
NVSRAWAYDT ATVLNEEIDS DLPFNEFYEY FGPTYKIDVP TSNMTNKNTS DYIDKLIENI
TENLRHVSHA PSAELIVPPK PFVEDDSDYE ELIVKMKESS NGDSGDYKDF NDDSSDG
//
