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Database: UniProt/TrEMBL
Entry: I6ZT13_ENCRO
LinkDB: I6ZT13_ENCRO
Original site: I6ZT13_ENCRO 
ID   I6ZT13_ENCRO            Unreviewed;       415 AA.
AC   I6ZT13;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   23-MAY-2018, entry version 32.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894283};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894283};
GN   OrderedLocusNames=EROM_031240 {ECO:0000313|EMBL:AFN82746.1};
OS   Encephalitozoon romaleae (strain SJ-2008) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=1178016 {ECO:0000313|EMBL:AFN82746.1, ECO:0000313|Proteomes:UP000010094};
RN   [1] {ECO:0000313|EMBL:AFN82746.1, ECO:0000313|Proteomes:UP000010094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJ-2008 {ECO:0000313|EMBL:AFN82746.1,
RC   ECO:0000313|Proteomes:UP000010094};
RX   PubMed=22802648; DOI=10.1073/pnas.1205020109;
RA   Pombert J.-F., Selman M., Burki F., Bardell F.T., Farinelli L.,
RA   Solter L.F., Whitman D.W., Weiss L.M., Corradi N., Keeling P.J.;
RT   "Gain and loss of multiple functionally related, horizontally
RT   transferred genes in the reduced genomes of two microsporidian
RT   parasites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12638-12643(2012).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC       {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894227}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913,
CC       ECO:0000256|SAAS:SAAS00894298}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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DR   EMBL; CP003520; AFN82746.1; -; Genomic_DNA.
DR   RefSeq; XP_009264243.1; XM_009265968.1.
DR   ProteinModelPortal; I6ZT13; -.
DR   EnsemblFungi; AFN82746; AFN82746; EROM_031240.
DR   GeneID; 20521038; -.
DR   KEGG; ero:EROM_031240; -.
DR   EuPathDB; MicrosporidiaDB:EROM_031240; -.
DR   KO; K06067; -.
DR   OrthoDB; EOG092C1END; -.
DR   Proteomes; UP000010094; Chromosome III.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; -; 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; PTHR10625; 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; SSF52768; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894233};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010094};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00870288};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894277};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894309};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894290}.
FT   DOMAIN       23    312       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
FT   ACT_SITE    136    136       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037913-1}.
FT   METAL       171    171       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       173    173       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       259    259       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   BINDING      94     94       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
FT   BINDING     144    144       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR037913-2}.
FT   BINDING     298    298       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
SQ   SEQUENCE   415 AA;  46665 MW;  D21A3DDD3BD46AEB CRC64;
     MNNKRVVYFY DPEIGTFSYA MGHPMKPLRV KMTHTLLVGY ELYKYMDVLR PFQASYENLT
     NFHAVDYINF LSSVSSENME EMIKDLHKFN IRDDCPVFPG LYDYCKLTSG GSIYAAQKIN
     SGKYDVAINW AGGLHHAKRS EASGFCYVND IVLGILELLK YNKRVLYIDI DVHHGDGVEE
     AFYTTDRVMT VSFHKYGDYF PGTGMVTDIG LAKGKGYSVN VPLRDGIDDE SYFSIFKPVV
     SKVIEVYRPD AIVLQSGADS LSGDKLGCFN LSHLGHSRCI KFVQSFNIPL ILLGGGGYTI
     GNVSKAWAYG TSVVLDVEIP REIPYNEYFD YYAPTYKIDV PTSNMKNQNT KESLEDIVAK
     VHENLRGVSH APSVQMSTIP PSFISDESDD EEISKKKIGE DSDDYKAFSG SREEL
//
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