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Database: UniProt
Entry: E9EDT7_METAQ
LinkDB: E9EDT7_METAQ
Original site: E9EDT7_METAQ 
ID   E9EDT7_METAQ            Unreviewed;       737 AA.
AC   E9EDT7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN   ORFNames=MAC_08042 {ECO:0000313|EMBL:EFY85896.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY85896.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY85896.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events. {ECO:0000256|PIRNR:PIRNR037919}.
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:PIRNR037919};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR037919}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037919}.
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DR   EMBL; GL698562; EFY85896.1; -; Genomic_DNA.
DR   RefSeq; XP_007814382.1; XM_007816191.1.
DR   AlphaFoldDB; E9EDT7; -.
DR   STRING; 655827.E9EDT7; -.
DR   ESTHER; metaq-e9edt7; Arb2_domain.
DR   GeneID; 19252353; -.
DR   KEGG; maw:MAC_08042; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_007727_4_0_1; -.
DR   InParanoid; E9EDT7; -.
DR   OMA; FVSPACY; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000002499; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR019154; Arb2-like_domain.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR017321; Hist_deAcase_II_yeast.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF09757; Arb2; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037919};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037919};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037919};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW   Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT   DOMAIN          77..402
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          455..712
FT                   /note="Arb2-like"
FT                   /evidence="ECO:0000259|Pfam:PF09757"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   737 AA;  82287 MW;  9E05D9719021C6F2 CRC64;
     MGDADLTNGT SHDNSVRPED DDDTASEEAS YDDGVYPDLQ DLALEQLRRR GLLPTGCCYD
     DRMKLHMNAD FSPNTHHPED PRRIHEIFKA FKRAGLVYTG PEAELPKIIK ECPTRYMWRI
     PARPATSQEI CLAHSSEHMT WVEHLDKLST AELRELTKRY DQGRESLYVG SMSYPAALLS
     AGGAIDTCKN VVAGQVKNAF AVIRPPGHHA EFDAPMGFCF FNNVPVAVRV CQQDYSDICR
     KVLVLDWDVH HGNGIQNIFY EDPNVLYISI HVYQNGHFYP GKPPNPETPD GGIENCGAGP
     GLGKNINIGW HDQGMGDGEY MAAFQKIIMP IAKEFNPDLV VISAGFDAAD GDELGGCFVT
     PPCYAHMTHM LMSLADGKVA VCLEGGYNLS AISSSAVAVA QTLMGEPPPK MTIPKLNKEA
     ARTLAKVQAY QAPYWECMRP GIVDVPAVQS LNANRLHDVI RSAQRLVLQE KHNMIPLYVQ
     RDQLYKSFEN QVLVTPNLHN SRRMLVIIHD PPQLLAQPDP IDSSLQPHNA WVVDGVTRYI
     DWAISQKFGI MDINVPAYIT NDEDTDSYIP GYRERILQEQ VQQLMNYLWD NFLQLYDADE
     IFLMGVGNAY LGVKVLLINR DCKSKLSGVV NFVTGNLRPV KSDIDPDLSL WYKENSRVYV
     AGDHACWSDH DLTKKVQKRR FGTVIRSPKL GLNKMMQEHA DEVQGWILSR VSATSRGDTT
     EEEDEDDGNG IGGVRAG
//
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