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Database: UniProt
Entry: A0A0D9P4U1_METAN
LinkDB: A0A0D9P4U1_METAN
Original site: A0A0D9P4U1_METAN 
ID   A0A0D9P4U1_METAN        Unreviewed;      1153 AA.
AC   A0A0D9P4U1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-OCT-2025, entry version 37.
DE   RecName: Full=Histone deacetylase domain-containing protein {ECO:0000259|Pfam:PF00850};
GN   ORFNames=H634G_03758 {ECO:0000313|EMBL:KJK81224.1};
OS   Metarhizium anisopliae BRIP 53293.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK81224.1, ECO:0000313|Proteomes:UP000054544};
RN   [1] {ECO:0000313|Proteomes:UP000054544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX   PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA   Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA   Ash G.J.;
RT   "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT   comparative genomics of Metarhizium species.";
RL   BMC Genomics 15:660-660(2014).
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DR   EMBL; KE384727; KJK81224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9P4U1; -.
DR   STRING; 1291518.A0A0D9P4U1; -.
DR   OrthoDB; 5232919at2759; -.
DR   Proteomes; UP000054544; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:TreeGrafter.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProtKB-ARBA.
DR   CDD; cd09998; HDAC_Hos3; 1.
DR   FunFam; 3.40.800.20:FF:000011; Histone deacetylase HOS3; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR053244; HDAC_HD_type_1.
DR   InterPro; IPR000286; HDACs.
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:UP000054544}.
FT   DOMAIN          258..585
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1128..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..40
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..88
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..132
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..854
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        956..976
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1054
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1131..1153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1153 AA;  124067 MW;  0992C4352D0FC1FA CRC64;
     MSHSIHGSLS PRQGPTSPAS NRANDDNSGL TQSLSQLSLT NEPKTLKPLP SPRNSWGTPA
     KPPPRRSSSA SPLPRTPSRS PSNGPGSRRA SHAESPPLLR KASMNSLHSA NGVAPGRPLA
     RRSSSSHIIS TSPANRTPPE EKPPLTARSI ASDYFAAELA EYHGATPTLP TDTVVILNDA
     VYGHRFSRPR TSRSALSTIV ERPERIKAAV LGISTAYVRL GGRHCQGHLP IHPKRNLSDI
     NSIPFRIHKT TRQLSLLSSA VTNVHGTKWM EELKLMCGSA ESILAMGGKE LQRPDISRGP
     EHPAPQKLHE GDLYLCEESL NAMQGALGAV CEAVDTVFGS GPRKAFVGVR PPGHHCSASH
     PSGFCWVNNV HVGIMHAALQ HGLTHAAIID FDLHHGDGSQ AITWQHNARA NAANKSHASW
     KRMSIGYFSL HDINSYPCEM GDEDKVKNAS LCIDSAHGQS IWNIHLQSWK TEQEFWTLYE
     STYAILLEKT RRYLKNETAK LRASNQVPKA AVFFSAGFDA SEWESAGMQR HHVNVPTEFY
     ARLSQDVVKL AAEEGLAVDG RVISVLEGGY SDRALCSGIM SHLSGLVGGS HDKEQSTIET
     EQESSGLAYE MGQRIGAINL NADPIMKPPA SMYDPAWWAT NELDLLEEPE APLAVPRKPR
     NSTPPTYSSP TQASTARVAD PMKMKNSLSG LSASYSKVPQ RPTSPPPPEV PWHIAAKELC
     KTLIPSDRQT DSCTAEDLNA EASRARRDRQ SLLLGNQPPT PSGSDRSLSR MSLRERKSRP
     IGPIDEEMSE VLPKTRRKPA STPISSPAKA GRSTPRPAGA QSARKSSRRL SVASTNLPPP
     REEPPPVPPI PATAPVPSRT ASRPNSRTGR TQSSNKVPVK KTQAVPSRID PAPKGGRNAA
     RASTPAKGAK QSTIAADTPT PATGLPLNAA GNDAKSDIDS LTDGVKKIRI NLITKAQRDG
     KQKAKPEQSV EPHRQLGQDS SIVKSEKPPT PEGMSSIPNA PEQLPTQLAP ASGLPEAPPT
     PSLSGGISTP VEEMYTSNTS SPTPTPSIPT GSSPDVPHVT IQPASDANDV FIPYQPEGPE
     PVTMVQHEHL KWLPPNIQTP SSVTPVHTPL PSATKTKDSL FHYTSGIRFA PRPDTELQGR
     PGSVDKPRTG HEQ
//
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