ID V2WWE7_MONRO Unreviewed; 589 AA.
AC V2WWE7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Histone deacetylase {ECO:0000313|EMBL:ESK85912.1};
GN ORFNames=Moror_2298 {ECO:0000313|EMBL:ESK85912.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK85912.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK85912.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK85912.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK85912.1}.
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DR EMBL; AWSO01001000; ESK85912.1; -; Genomic_DNA.
DR RefSeq; XP_007854781.1; XM_007856590.1.
DR AlphaFoldDB; V2WWE7; -.
DR STRING; 1381753.V2WWE7; -.
DR KEGG; mrr:Moror_2298; -.
DR HOGENOM; CLU_013370_2_1_1; -.
DR OrthoDB; 10780at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR47558; HISTONE DEACETYLASE HOS3; 1.
DR PANTHER; PTHR47558:SF1; HISTONE DEACETYLASE HOS3; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 122..433
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 510..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 63267 MW; 27651455F256C330 CRC64;
MPSIPGNFAV FIQDVCYKHK FIRSRDTSTI VERPERLRAV KVGLAAALSR LEEVHSASSS
KTSNRSDDPD ILAAALDKMK LEGSSTSQST FGPITVVHSA ATMPLLDSPA VKFVHGDIEG
DVYLENVSKW AAESAEKIGR GESEIPEGLP QGDLYLCPES IIAMEGAIGT TCEAVDVVMS
GTLPSSATEA AASSGIKRAF VAVRPPGHHC GEDTPCGFCF VNNVAVAAAH AHLKHGIKRA
VIFDIDLHHG NGTQSIIWQI NEETYRQTVE AEADAPITDP GPKVYYGSIH DILSFPCEDG
KPELVQAASV SIHDAHGQWI ENIHLKPYDN EEGFHALYEK EYRKIIERAE HFLDNTGGAG
EDVLVFISCG MDACEHEYTS MSRHNRKVPV SFFDRFTQDA CAFADRYAKG RLVSVLEGGY
SDRALISGTL AHICGLVDIP SESREALKDS WSLDNLIKLE KATKKRAARS ARPSGVGASS
EPWLERAVAI FTSIDANGAA ILAASPKAAS RSKVVPPSSR TLRERKKPKG SHAVPVAQED
ASDASLLSSL SDSEGDQVVA PALGGGVSGT EKKLPRVILR LGPDPLSKQ
//
