ID A0A369S315_9METZ Unreviewed; 593 AA.
AC A0A369S315;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=TrispH2_006473 {ECO:0000313|EMBL:RDD41316.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD41316.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD41316.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD41316.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD41316.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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:RDD41316.1}.
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DR EMBL; NOWV01000078; RDD41316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369S315; -.
DR STRING; 287889.A0A369S315; -.
DR Proteomes; UP000253843; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000253843};
KW Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT DOMAIN 27..317
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 376..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 67584 MW; 6CB8FC421766AAB8 CRC64;
MAYLERKRKV CYYYDGDIGN YYYGQGHPMK PHRIRMTHNL VLNYGLYRKM EIFRPHKATQ
DEMTKYHSDD YIKFLRSIRP DNMNDYTKQM QRFNVGEDCP VFDGLYEFCQ LSGGGSIAAA
VKVNKQQTDI AVNWAGGLHH AKKSEASGFC YVNDIVLAIL ELLKYHQRVL YIDIDIHHGD
GVEEAFYTTD RVMTVSFHKY GEYFPGTGDI RDIGASKGKY YAVNFPLRDG VDDECYDQIF
SPVISKVMEM YQPSVIVLQC GADSLAGDRL GCFNLSLKGH SACVEFMKKF NLPIVLLGGG
GYTIRNVARC WAQETSAALG VEIPNELPYN DYFEYFGPDF KLNISPTNMT NQNTPDYIDR
IKTRLFENLR MLPHAPGVQM QPIPSDVQYE SDEEENDPDT RISMHDKDKR IACDEEYSDS
EDENEGGRRN RQEYHRHLQK RIKTFSENEV AKMNGSKPVG EVAKPPVPKI EENTQVSATT
ETLQGQRDVQ PMDKESTARE PAAHDNSSQQ MEIEDAQKVK EQEISNNEGG NKEESSAKAA
DLSEVKIEES EIKSQVPEEN STNKDTVEVK NNDGKTQLDQ TERKEASPEP MQH
//
