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Database: UniProt
Entry: W6MIJ7_9ASCO
LinkDB: W6MIJ7_9ASCO
Original site: W6MIJ7_9ASCO 
ID   W6MIJ7_9ASCO            Unreviewed;       639 AA.
AC   W6MIJ7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Histone deacetylase domain-containing protein {ECO:0000259|Pfam:PF00850};
GN   ORFNames=KUCA_T00000142001 {ECO:0000313|EMBL:CDK24182.1};
OS   Kuraishia capsulata CBS 1993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX   NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK24182.1};
RN   [1] {ECO:0000313|EMBL:CDK24182.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK24182.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK24182.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK24182.1};
RA   Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA   Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA   Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA   Gabaldon T., Wincker P., Dujon B.;
RT   "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT   features among budding yeasts (/Saccharomycotina/).";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HG793125; CDK24182.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6MIJ7; -.
DR   STRING; 1382522.W6MIJ7; -.
DR   HOGENOM; CLU_024583_0_0_1; -.
DR   OrthoDB; 10780at2759; -.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; 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;
FT   DOMAIN          124..496
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          16..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   639 AA;  71144 MW;  09730DD1AF640C8D CRC64;
     MSDDILAGEL ENLKIRDSSP ALASSPPKHE SELSSSPPRT PEIKKENVVK FEESKPEEYV
     GVDELQKFRE TFFEFIEQFP EIVEQQEVCN IQDKALVILS PLSVKHRFGR DWVSKAYISS
     IVERPQRLLA VSIGISAALS MFPSYYTFIS STTLGALDSP HVLKVHGRKW LDQIVELCAK
     STAKLENGEI EVPDEWNSGD IYLTADTLLA LKGVVGAVET AVDQVHSSKA NSGEAPKRAF
     VAIRPPGHHS HPCTPSGFCL INNAQIAILY AHAKFDVTHA VILDIDLHHG DGTQDICWEQ
     GGFKADYGDS EDSEGYDEYE KRAPTGPKVG YFSLHDINSF PTELGYATSE NVKNASLCLM
     GHDMCIWNVH LQPYKTQAEF DDLYYNQYCE LFKRAEMFLK KSKLEHDEKI LEARKRKQPI
     PAPFKALVVM SSGFDGSEFE TQTMQRHKVN VPTSFYARFT SDTVNLANSY SEGRLISFLE
     GGYSDAALSS GVFAHMVGLQ QQKWDESWGK DSLVKELVKG CRPKWTPVKA PRSDVSKWAN
     WVCRMGRDMV PDAVILPTAS KPVSGLSSLS GSNVYATRAT RMTTRSHAQH NESEKENSTP
     AASSEDYPSS PMKIDTPIKN NSVASTMSPL ESARFLDFD
//
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