ID A0A1Y2DU77_9BASI Unreviewed; 842 AA.
AC A0A1Y2DU77;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Histone deacetylase clr3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCR35DRAFT_283352 {ECO:0000313|EMBL:ORY62719.1};
OS Leucosporidium creatinivorum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY62719.1, ECO:0000313|Proteomes:UP000193467};
RN [1] {ECO:0000313|EMBL:ORY62719.1, ECO:0000313|Proteomes:UP000193467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62-1032 {ECO:0000313|EMBL:ORY62719.1,
RC ECO:0000313|Proteomes:UP000193467};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:ORY62719.1}.
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DR EMBL; MCGR01000070; ORY62719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DU77; -.
DR STRING; 106004.A0A1Y2DU77; -.
DR InParanoid; A0A1Y2DU77; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000193467; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
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; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000193467}.
FT DOMAIN 191..502
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 558..785
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 92154 MW; 2F6B4387DD596407 CRC64;
MEQSTQPFTQ AIEQSSLPLL SNSDQPLPPI ASSSTLAADP SQTAAPPVPA APETSQAESQ
PAVVLSGFAA AQSLAAAKPN PVPYIEPPPY VAPALTSTAA TGPSTGVAAL SHPKQFLTNE
EREKMTPDQL RETSKSRGVP VAELLSEDEV QKFDTATLRR MGLGRTPSGY CFSSRMTLHK
QLDSASKDDP HPEQPTRITG IFNRLSLAGL TDRMERIAVR EVVRDEVMLV HSEGHWDRVR
ATGYQTVDYL ASCSEYFDRL SLYVNPETSR CARLSCGGVI EMCRAVAEGQ IRNGFAIVRP
PGHHAEPEDA MGFCFFNNVA VAAKWLRTIY DGQQEGASGQ KVKKMDKILI LDWDVHHGNG
TQKAFWDDPN VLYISIHRHG DGFYPGGNYG AAEMVGEGAG VGFSVNVPFT ETGMGDADYI
YAFQQVIMPI AYEFAPDIVL VSAGYDAAEG DKLGQFKVSP EGFAHMTHML SVLANGKLVL
ALEGGYNVDS IVKSAHACVE VLVGDEPRHL QLGPASASAT TAVQEVIKIQ AKHWKCMGFA
MEPAEELKSA GKVVPVAEML KAHRVYELYH EYELFNVEIS KPELEEAYKD QLLCSPNIYD
AETLLIFMHD IGSIKSSHTA ATMDVDLERT LLLDTSREVL DWAMKDNKWG VIDVNFLAHL
PSIKGQVPDR ARDVKLEKEF ATFIWDHIAR LSSAQNIVLF ASGAGCSAMM EIVSKRPDTR
ERVRACISVL GLEAPPELDA ASGMRSWYKE RSLVMLPSTH VLHDDARKAG KHQKKYGNVY
RATAEDEGRP IHLLRASLPR IRQFVDERLP APRMMEVDES AAGPAPPKGD GDVEMKSGDI
VV
//