ID   D8QXJ8_SELML            Unreviewed;       410 AA.
AC   D8QXJ8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
GN   ORFNames=SELMODRAFT_114783 {ECO:0000313|EMBL:EFJ17426.1},
GN   SELMODRAFT_80012 {ECO:0000313|EMBL:EFJ35052.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ35052.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000256|ARBA:ARBA00001028,
CC         ECO:0000256|PIRNR:PIRNR037913};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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DR   EMBL; GL377614; EFJ17426.1; -; Genomic_DNA.
DR   EMBL; GL377568; EFJ35052.1; -; Genomic_DNA.
DR   RefSeq; XP_002963181.1; XM_002963135.1.
DR   RefSeq; XP_002981611.1; XM_002981565.1.
DR   AlphaFoldDB; D8QXJ8; -.
DR   STRING; 88036.D8QXJ8; -.
DR   EnsemblPlants; EFJ17426; EFJ17426; SELMODRAFT_114783.
DR   EnsemblPlants; EFJ35052; EFJ35052; SELMODRAFT_80012.
DR   GeneID; 9643773; -.
DR   GeneID; 9648109; -.
DR   Gramene; EFJ17426; EFJ17426; SELMODRAFT_114783.
DR   Gramene; EFJ35052; EFJ35052; SELMODRAFT_80012.
DR   KEGG; smo:SELMODRAFT_114783; -.
DR   KEGG; smo:SELMODRAFT_80012; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_7_4_1; -.
DR   InParanoid; D8QXJ8; -.
DR   OMA; RCHTDEY; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:1902494; C:catalytic complex; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; PTHR10625:SF11; HISTONE DEACETYLASE 19; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 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   ECO:0000256|PIRNR:PIRNR037913}; Hydrolase {ECO:0000256|PIRNR:PIRNR037913};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT   DOMAIN          36..325
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          386..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         184
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         186
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         272
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ   SEQUENCE   410 AA;  46017 MW;  D3D1938E0B41C4C1 CRC64;
     MDGSGNSLAS GPEGRSKRVA YFYDPEVGNY YYGQGHPMKP HRIRMTHSLL VHYGIHNKLE
     VLKPLPAKDR DLCRFHADDY VAFLRVITPE TQHEHLRALK RFNVGEDCPV FDGLYSFCQT
     YAGGSVGGAV KLNHGHSDIA VNWSGGLHHA KKCEASGFCY VNDIVLAILE LLKYHARVLY
     IDIDIHHGDG VEEAFYTTDR VMTVSFHKFG DYFPGTGDVR DMGHAKGKYY SLNVPLNDGI
     DDESYHSLFK PIITKVMEVF QPGAVVLQCG ADSLSGDRLG CFNLSIKGHA QCVKFMRSFN
     VPLLLLGGGG YTIRNVARCW CYETAVAVGV ELEDKMPYNE YYEYFGPDYT LHVTPSNMEN
     QNSAQYLESI RNRLLENLSN LQHVPSVPFQ ERPPDTDLPE EVSLSVASTW
//