GenomeNet

Database: UniProt/TrEMBL
Entry: Q8SS80_ENCCU
LinkDB: Q8SS80_ENCCU
Original site: Q8SS80_ENCCU 
ID   Q8SS80_ENCCU            Unreviewed;       416 AA.
AC   Q8SS80;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   23-MAY-2018, entry version 89.
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=ECU03_1370 {ECO:0000313|EMBL:CAD26280.1};
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD26280.1, ECO:0000313|Proteomes:UP000000819};
RN   [1] {ECO:0000313|EMBL:CAD26280.1, ECO:0000313|Proteomes:UP000000819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1 {ECO:0000313|EMBL:CAD26280.1,
RC   ECO:0000313|Proteomes:UP000000819};
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M.,
RA   Weissenbach J., Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL590443; CAD26280.1; -; Genomic_DNA.
DR   RefSeq; NP_597645.1; NM_001041009.1.
DR   ProteinModelPortal; Q8SS80; -.
DR   STRING; 284813.NP_597645.1; -.
DR   EnsemblFungi; CAD26280; CAD26280; CAD26280.
DR   GeneID; 858807; -.
DR   KEGG; ecu:ECU03_1370; -.
DR   EuPathDB; MicrosporidiaDB:ECU03_1370; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   HOGENOM; HOG000225180; -.
DR   InParanoid; Q8SS80; -.
DR   KO; K06067; -.
DR   OMA; RMTHHLL; -.
DR   OrthoDB; EOG092C1END; -.
DR   Proteomes; UP000000819; 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:UP000000819};
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   Reference proteome {ECO:0000313|Proteomes:UP000000819};
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   416 AA;  46782 MW;  75CFCAF108EFE7FA CRC64;
     MNNKRVVYFY DPEIGCFSYA MGHPMKPLRV KMTHTLLVGY ELYKYMDVLR PFQASYENLT
     NFHAVDYINF LSSVSSENME EMIKDLHKFN IRDDCPVFPG LYDYCRLTSG GSIYAAQKIN
     SGKYDVAINW AGGLHHAKRG EASGFCYVND IVLGILELLK YNKRILYIDI DIHHGDGVEE
     AFYTTDRVMT VSFHKYGDYF PGTGMVTDTG LAKGKGYSVN VPLKDGIDDE SYFSIFKPIV
     SKVIETYQPN AIVLQSGADS LSGDKLGCFN LSHLGHSRCI KFVQSFNIPL ILLGGGGYTI
     GNVSKAWAYG TSVVLDVDIP REIPYNEYFD YYAPTYRIDV PTSNMANQNT REGLEDIIAK
     VYENLRSLSH APSVQMVSIP PSFISDESDE DEVSKKKAEA EDSDDYKAFS DSKDED
//
DBGET integrated database retrieval system