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Database: UniProt/TrEMBL
Entry: A9UNJ7_MONBE
LinkDB: A9UNJ7_MONBE
Original site: A9UNJ7_MONBE 
ID   A9UNJ7_MONBE            Unreviewed;       462 AA.
AC   A9UNJ7;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   22-NOV-2017, entry version 52.
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   ORFNames=34892 {ECO:0000313|EMBL:EDQ93150.1};
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellida; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824 {ECO:0000313|Proteomes:UP000001357};
RN   [1] {ECO:0000313|EMBL:EDQ93150.1, ECO:0000313|Proteomes:UP000001357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the
RT   origin of metazoans.";
RL   Nature 451:783-788(2008).
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; CH991543; EDQ93150.1; -; Genomic_DNA.
DR   RefSeq; XP_001742912.1; XM_001742860.1.
DR   ProteinModelPortal; A9UNJ7; -.
DR   STRING; 431895.XP_001742912.1; -.
DR   EnsemblProtists; EDQ93150; EDQ93150; MONBRDRAFT_34892.
DR   GeneID; 5887443; -.
DR   KEGG; mbr:MONBRDRAFT_34892; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   InParanoid; A9UNJ7; -.
DR   KO; K06067; -.
DR   OMA; KRVCYFF; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
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:UP000001357};
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:UP000001357};
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       24    314       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
FT   ACT_SITE    137    137       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037913-1}.
FT   METAL       172    172       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       174    174       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       260    260       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   BINDING      95     95       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
FT   BINDING     145    145       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR037913-2}.
FT   BINDING     299    299       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
SQ   SEQUENCE   462 AA;  53068 MW;  1C4D9A07B8F2D353 CRC64;
     MASKKHVSYY YDGDVGNYYY GPGHPMKPHR IRMTHNLLLN YGLYKKMEIY RPHKASMEDM
     TRFHSDDYIN FLRTISPDAT NEETKNMSRF NVGEDCPVFD GLFEFCQISA GGSLAGAAKL
     NSQQSDICIN WAGGLHHAKR SEASGFCYVN DIVLGILELL KRHERVLYID IDIHHGDGVE
     EAFYCTDRVM TVSFHKYGEY FPGTGDIKDI GTQDGRHYAV NFPLKDHIDD DSYQRIFRQV
     IEKVMDWYDP GAVVLQCGAD SLTGDRLGCF NLSLKGHAAC VEYVKSFNKP LLLLGGGGYT
     IRNVARCWTY ETSVALDTPI EDELPFNDYF EYFGPDFRLH ISPSNHDNQN SEEYLENSVK
     QIIENLRHTA SRPSVQMHSM VDTLSAYEED EDQVDPDDRR AQQLVDRKIS HDADLSDSED
     EGGRRDQQSF KKKKKKKKKK KKKTKTRRVI REEGRPKESI KK
//
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