ID   A0A0C2DB63_9BILA        Unreviewed;       814 AA.
AC   A0A0C2DB63;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Histone deacetylase family protein {ECO:0000313|EMBL:KIH59652.1};
GN   ORFNames=ANCDUO_10107 {ECO:0000313|EMBL:KIH59652.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH59652.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH59652.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH59652.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000256|ARBA:ARBA00001028};
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DR   EMBL; KN731729; KIH59652.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2DB63; -.
DR   Proteomes; UP000054047; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; PTHR10625:SF15; HISTONE DEACETYLASE; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 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:UP000054047}.
FT   DOMAIN          431..744
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          90..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   814 AA;  87434 MW;  D072EB512AC7FB38 CRC64;
     MGAADGMHVV SIAANGEVFK QKQMDLMAHF ERAQQALNMQ HLQQYYQTLQ QHAQQQAANS
     AAQAGPERMD EGLCDAAVQV APLALASSMG SLLGSSQSPT TSREAPAPQR ARSEHRNAST
     NSTSQTISQH TKDRLKNMIA QRNREGSQTN LAGTPPQQHA PMSPQVNVSS PHFEPYRVPA
     SLHTAQAVSS QPSSEYQLRK VNSEPNLKMR IRAKLLSKGS SPVQNQSTFN FTHPQLKRSD
     SETSGNGAAA GNLAMDALLT NAAATAFPPH LIMPSPSLPN LAAPNLAQAP QLPIDLASLM
     AAAQLTPFLS LPSLFKTHIG LGGGLLEEDV ADRAKLAPGV AALGTLSQQL PVFGNPSLLK
     QQLRELVLRR KSLVREEPED DDSLCTQPVL SPGQLPTSLG LGDMSGGKAT GLAYDSSMAR
     HECVCGESSS HVEHGGRVQS IWARLLERGL VQKCERIAAK KASLEQLRMV HSPTYVTFFA
     VSPTACLKME ASQLPLKSFV QLPCGGIGID SDTYFNDATT QTAARVAAGS LIELASQVAE
     NRLRNGFACI RPPGHHSEKD QAMGFCFFNN VAITARYLQN KYPQQCARIA IIDWDVHHGN
     GTQLCFEEDP SVLYLSLHRH DNGNFFPGTG AVTEVGRGAG KGFSVNVPFS GGVMRDADYL
     AAWRVIVQPV LEQFQPTFIL VSAGFDACCG HPNALGGYKI SAEMFGFMTR QLMSFAGGRV
     VLALEGGYDL ASISDAAEQC VKVLCGDDDK AGVLKNEALE GIPCLSAQET IQKVIAIHKG
     YWPALTAEQG LSISELHWQT VGRQFQNLTM GTVS
//