ID   G4MUC7_PYRO7            Unreviewed;       496 AA.
AC   G4MUC7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=MGG_01633 {ECO:0000313|EMBL:EHA54814.1};
OS   Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Magnaporthe oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507 {ECO:0000313|EMBL:EHA54814.1, ECO:0000313|Proteomes:UP000009058};
RN   [1] {ECO:0000313|EMBL:EHA54814.1, ECO:0000313|Proteomes:UP000009058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958
RC   {ECO:0000313|Proteomes:UP000009058};
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M., Kulkarni R., Xu J.R., Pan H., Read N.D., Lee Y.H.,
RA   Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., Soanes D.M.,
RA   Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., Kim S.,
RA   Lebrun M.H., Bohnert H., Coughlan S., Butler J., Calvo S., Ma L.J.,
RA   Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=70-15;
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Magnaporthe oryzae 70-15.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR037913};
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; CM001232; EHA54814.1; -; Genomic_DNA.
DR   RefSeq; XP_003714621.1; XM_003714573.1.
DR   AlphaFoldDB; G4MUC7; -.
DR   SMR; G4MUC7; -.
DR   STRING; 242507.G4MUC7; -.
DR   EnsemblFungi; MGG_01633T0; MGG_01633T0; MGG_01633.
DR   GeneID; 2679107; -.
DR   KEGG; mgr:MGG_01633; -.
DR   VEuPathDB; FungiDB:MGG_01633; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_7_11_1; -.
DR   InParanoid; G4MUC7; -.
DR   OMA; FHSEEYM; -.
DR   OrthoDB; 1327607at2759; -.
DR   PHI-base; PHI:2005; -.
DR   PHI-base; PHI:9766; -.
DR   Proteomes; UP000009058; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; IEA:EnsemblFungi.
DR   GO; GO:0034967; C:Set3 complex; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045129; F:NAD-independent histone deacetylase activity; IEA:EnsemblFungi.
DR   GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:EnsemblFungi.
DR   GO; GO:0045835; P:negative regulation of meiotic nuclear division; IEA:EnsemblFungi.
DR   GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IEA:EnsemblFungi.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:EnsemblFungi.
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:SF25; HISTONE DEACETYLASE 3; 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:UP000009058};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT   DOMAIN          83..382
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          474..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         235
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         237
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         329
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ   SEQUENCE   496 AA;  55787 MW;  B9A8E8E0C3B47BD1 CRC64;
     MDADSYRYRP PRPNYLPRDV EVDKPIVEDY VDPLDVVSDA DNAAFYNKIK RVAETYNITR
     PKGHNVSFHV NPEMEKHHFG QTHPMKPWRL TLSKALISSY GMNFAMDNYV SRAATYDELT
     MFHASDYIQF LGTVLPEPIP RDVDNPYPDL KFNLGGSDCP LFEGLYDYCS MSAGGSLDAA
     RKICNNQSDI AIAWGGGLHH AKRSEASGFC YINDIVIAIL QLLRCHPRVL YIDIDVHHGD
     GVEEAFYSTD RVMTVSFHKY DPVNFFPGTG PLDENGPKNE LNPGAHHAIN VPLNDGITDD
     QYSALFENVI GQCVAKFRPT AIALQCGADS LAGDRLGRFN LQVQGHGSCV EFCKKLGIPM
     ILFGGGGYTP RNVARAWAYE TSIAIDCHDK IDPVIPLHTP WRDKFRQDTL LPTLQQVVGE
     PRQNRNTQKR LQEIVQHVTE QLRFVNNAPS VQYSVIPPDL QGLRDEVEAR IKEEMEEKDE
     RSRKAAEEGV GQAMEF
//