ID S7W9G1_SPRLO Unreviewed; 353 AA.
AC S7W9G1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=SLOPH_426 {ECO:0000313|EMBL:EPR79560.1};
OS Spraguea lophii (strain 42_110) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Spraguidae;
OC Spraguea.
OX NCBI_TaxID=1358809 {ECO:0000313|EMBL:EPR79560.1, ECO:0000313|Proteomes:UP000014978};
RN [1] {ECO:0000313|Proteomes:UP000014978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=42_110 {ECO:0000313|Proteomes:UP000014978};
RX PubMed=23990793; DOI=10.1371/journal.pgen.1003676;
RA Campbell S.E., Williams T.A., Yousuf A., Soanes D.M., Paszkiewicz K.H.,
RA Williams B.A.P.;
RT "The genome of Spraguea lophii and the basis of host-microsporidian
RT interactions.";
RL PLoS Genet. 9:E1003676-E1003676(2013).
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:EPR79560.1}.
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DR EMBL; ATCN01000199; EPR79560.1; -; Genomic_DNA.
DR AlphaFoldDB; S7W9G1; -.
DR STRING; 1358809.S7W9G1; -.
DR VEuPathDB; MicrosporidiaDB:SLOPH_426; -.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; S7W9G1; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000014978; Unassembled WGS sequence.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; PTHR48252; HISTONE DEACETYLASE 2-RELATED; 1.
DR PANTHER; PTHR48252:SF69; HISTONE DEACETYLASE 3; 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 Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000014978}.
FT DOMAIN 20..296
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT ACT_SITE 119
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 243
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 353 AA; 40141 MW; 99D964B8AF5F333E CRC64;
MKIAYMYDKE VGNFFYGEDH PMKPHRVAIT HTLVKNYGLD KHMDIIEPEI LYDNNVFSVF
HTKNYINTIT NETLEPSDDC PCFPGLGIFS KRYSSATINC SKLLNEYDIA INWGGGLHHA
KKEEPSGFCY FNDIVMGIQE ILKYKERVLY IDIDIHHGDG VEEAFYHSDR VMTLSFHKFG
EGYYPGTGDL FTNGDEEGLG YAVNVPLKNG IDDHSYHYVF KPIVDQAIKK FKPSAIVLQC
GADSLAEDTL GCFNLSIQGH GECVKTVKSY NIPLLILGGG GYNIKNVSRA WVNETAIACD
VQIKNEIDKN QYSAYFEPSQ SLYPRLKKKY DNVNSKKYLD VVVNYNLELM DNY
//