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Database: UniProt
Entry: S7W9G1_SPRLO
LinkDB: S7W9G1_SPRLO
Original site: S7W9G1_SPRLO 
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
//
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