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Database: UniProt
Entry: E3RX11_PYRTT
LinkDB: E3RX11_PYRTT
Original site: E3RX11_PYRTT 
ID   E3RX11_PYRTT            Unreviewed;       884 AA.
AC   E3RX11;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Histone deacetylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PTT_13889 {ECO:0000313|EMBL:EFQ89752.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ89752.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ89752.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; GL535578; EFQ89752.1; -; Genomic_DNA.
DR   RefSeq; XP_003302166.1; XM_003302118.1.
DR   AlphaFoldDB; E3RX11; -.
DR   STRING; 861557.E3RX11; -.
DR   ESTHER; pyrtt-e3rx11; Arb2_domain.
DR   EnsemblFungi; EFQ89752; EFQ89752; PTT_13889.
DR   KEGG; pte:PTT_13889; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_007727_4_1_1; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0099115; C:chromosome, subtelomeric region; IEA:EnsemblFungi.
DR   GO; GO:1990342; C:heterochromatin island; IEA:EnsemblFungi.
DR   GO; GO:0031934; C:mating-type region heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0070824; C:SHREC complex; IEA:EnsemblFungi.
DR   GO; GO:0110129; C:SHREC2 complex; IEA:EnsemblFungi.
DR   GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:EnsemblFungi.
DR   GO; GO:0090053; P:positive regulation of pericentric heterochromatin formation; IEA:EnsemblFungi.
DR   GO; GO:0000183; P:rDNA heterochromatin formation; IEA:EnsemblFungi.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IEA:EnsemblFungi.
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; IPR017320; Histone_deAcase_II_euk.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR45364:SF10; HISTONE DEACETYLASE; 1.
DR   PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR   Pfam; PF09757; Arb2; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT   DOMAIN          143..441
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          495..758
FT                   /note="Arb2-like"
FT                   /evidence="ECO:0000259|Pfam:PF09757"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          863..884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   884 AA;  99156 MW;  756DAE3B2DE17CD0 CRC64;
     MEDEDCTMGD DSIIVSTEPN GDHAPNTVDP SDTFGNSKGL TLSKREQLPF HSPSKAPSLL
     QPSAQQSSPG PHRTTKSPSA WSDKMSMSRP TPTRRTSPQV RIPPKPSSSA LAYATSKTGL
     VYDPRMRFHA ELPDMNINPD DIHPEDPRRI HSIFEEIKQA GLVASSTSEE DQQDHCWRIA
     TRFATKPEIL LIHTEEHYDF LKEQAEGLDS IYFNHSTYEC AKLAAGGAIE ACKAVVEGHV
     RNAIAIIRPP GHHAETDSPS GFCIFNNVPI ATRVCQKAYP ETCRKVLILD WDVHHGNGIQ
     HAFYDDPNVL YISLHVFKDG NFYPNLPDGN LNYCGEGLGE GKNVNIPWAE HGMGDAEYLY
     AFQEVVMPIA TEFDPDLVII SAGFDAAEGD LLGGCFVTPA CYGHMTHMLM RLAKGKLVVC
     LEGGYNLRSI ARSALAVTRV LMLEPPDRLH IDLPGPKDSA VHTVENVKRE HSRYWKSLYP
     KHLDKADPGY KDACRLHEII REWQSRRLAS EHSMVPLPPL YINKAGLTQT FSHNIIATPR
     FMDRYPLLVI FHDPPGFQDH PDPVTGKNEL HNTWLTDVTK RYIDWAITND FQVIDVNIPK
     IVTVEDADYG FVRADDSTVR ARQTRELATY LWENYIEPNE ASQVFFMGIG DAYLGLVDLL
     SHNENCTDPG SRVECLIGFV AETTIQSIKR AADDFISTWY YEHSMIFVKD SHFVWDPSRQ
     RKVRKKLGNL RKSPKDTLDE MLEEHLEEVQ AMLLRKKSEL DEMSDISSRT DDGPQAMDTG
     LRSPPLPIAS QTPKHFEAGG RQENASKLLR SPNMPTVGAG EMQKLGTRLR TRQVVSSSLA
     DKDFLSHHPR ARLQALQHNL TPHASHGYLG RKKSMLSQAT DAPR
//
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