ID E9AWY0_LEIMU Unreviewed; 545 AA.
AC E9AWY0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=LMXM_24_1370 {ECO:0000313|EMBL:CBZ27466.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ27466.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR EMBL; FR799577; CBZ27466.1; -; Genomic_DNA.
DR RefSeq; XP_003875952.1; XM_003875903.1.
DR AlphaFoldDB; E9AWY0; -.
DR GeneID; 13448879; -.
DR KEGG; lmi:LMXM_24_1370; -.
DR VEuPathDB; TriTrypDB:LmxM.24.1370; -.
DR OMA; GWLRAFH; -.
DR OrthoDB; 168126at2759; -.
DR PhylomeDB; E9AWY0; -.
DR Proteomes; UP000007259; Chromosome 24.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR CDD; cd09991; HDAC_classI; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF13; HISTONE DEACETYLASE HDAC1; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853}.
FT DOMAIN 102..402
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 58645 MW; D30B798D6266359E CRC64;
MSSPEQLPAL SAGGSPSSGG ASSHHSPHEA SLPFPASAIT GDASAESPRA SSVPPSSTAS
EESAATSPLE RKPDAAASRP GRRKVVYFVD HSVTAIAYAE GHLMRPSRVR ALHALVHSLG
LDSAEYMTVC HARPATAEEM GAFHRSAYLE CLRQAPVICG NPLDEISLAF QKEFDVPFAS
QNGDCPLFPE VWALVSSQAG ASLACAEALV RGDATVAMNW AGGMHHAAAA HASGFCFVND
IVLCIRRLLR HYQRVLYVDL DVHHGDGVEG AFYGNHRVMT LSLHQFGNGF FPGTGDYPTR
ETADSFAINV PLPTRTGDAA YLLSFRTALS SVVQCFDPEA MVVQCGADTI AGDLIGRLCV
TTLAHTQCVA DVLSLERPTV LLGGGGYHVF HTARCWAIHT ATALGRTAAQ LPLYIPRTDP
YYMDYRRECT PKRPTLHVFL DPDVDDPLPL GDSLAFWRQL CRSIQWQMRT ARLVRQGFSR
TVQLCRQRRA ALLRQFATQE AGRDSGIGVS ASKRQRSANV TDRDAKEGGG GQSGLGVMVA
EEECT
//
