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
//