ID   A0A1I8I2V2_9PLAT        Unreviewed;      1289 AA.
AC   A0A1I8I2V2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0009383-snap-gene-0.5-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0009383-snap-gene-0.5-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006457}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   WBParaSite; maker-uti_cns_0009383-snap-gene-0.5-mRNA-1; maker-uti_cns_0009383-snap-gene-0.5-mRNA-1; maker-uti_cns_0009383-snap-gene-0.5.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:1902494; C:catalytic complex; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
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};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT   DOMAIN          1..288
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          365..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1020..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1125..1156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..455
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..840
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..910
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1048
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1289 AA;  139432 MW;  3467563E47241813 CRC64;
     MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA TAEEMTRFHS DDYIKFLRSI RPDNMHEFNK
     QMQRFNVGED CPVFDGLYEF CQLSTGGSIA GAVKLNKGAT DIAINWGGGL HHAKKSEASG
     FCYVNDIVLA ILELLKYHQR VLYVDIDIHH GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG
     DLKDIGAGRG KHYAVNFPLR DGIDDEAFEQ IFAPVITKVM EHYRPSATVL QCGADSLAGD
     RLGCFNLSLK GHGRCVQFMK KFDTPLLLLG GGGYTIRNVA RCWTYETAIA LGQEIPNELP
     YNDYFEYFGP DFKLHIQPSN MSNQNTPEYL EKIKTRLLEN LRMLPNSPGV QMQDIPEDGM
     AVDEDVAQEE AEQDRGKRDE QRVSIRSSDK RVSGDNELSD SEDEAGDGRR DSRSGTAGAR
     RPPPLPLARP PRTETAQRPR PTPGPPSPPP PRQTAKRKAK PMLINERDPY SPDFCCIGGT
     LHQTEAHRGG HRSNCPDTDD GQQGRSDAQA KVTAANADSR LAVKLAISAG ELRNLAKPLA
     LPSLPLPQKT VVAESGATKL TVSSPVAETF MPLAARRRSL LARMLALPPL PPSLLLETLA
     DGQQVAKFQR QKSAMAVSSG GSRARQRLGH CWKGCTQNWP EHPLEPLVPT GTQRPSRQRG
     RALLQPLQDG PAVTAEGQPT RTEQLRDSPH GQNSRGAAHT DRTAEGQPTW TKQLRDSPHG
     QNSRGAAHTD RTASPVSLGC KTILTSWFML AASGSTDLLS RLCSSTMPWC SAKTCTGRNQ
     KLAPPTHITA QLTHTGTADT YTRATDTHTG TTDTHTSATD TYTRATDTHT GTTDTHTSAT
     DTHTHATDTH TGDADTHTGT TDTYTGAADS HTGATDTYTG ANDTHTGATD THTGANDTHT
     GATDTYTGAN DTHTGATDTY TGANDTHTGA IPTLIPATDT HDTHTGATDT HTGATDTHTG
     ATALIRQTQP QYSSHSSVVN TNEAADPVPS PRKEAHQRAV QFGILNLGCG GASSHAQSAQ
     VTVAKAEQAD KDGQSGVRSE RWRDRPLPPG LRLSDTANTM NTDRAGQAKS DSARRQVAGW
     PDSDRLLPAD GRLESPNSEP CTRAAPMFTA ITEAMVHQKK ACCRSPRLNP AARSRPPRRS
     SPAAAARADD GVSASRTAPA CSEHALAARA HDNEFHILLF GQIHNGLAGT AGDAFKKADV
     LGAQAAAKFF DVYGQLLGLS DLADFGHGRS GHAEAQSNFR RLGHVHKHQL VGWPVQLAQI
     PADGPLAVLA AINSDQDATN VANISNCFC
//