ID A0AA39HBM8_9BILA Unreviewed; 401 AA.
AC A0AA39HBM8;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
GN ORFNames=QR680_016582 {ECO:0000313|EMBL:KAK0402865.1};
OS Steinernema hermaphroditum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=289476 {ECO:0000313|EMBL:KAK0402865.1, ECO:0000313|Proteomes:UP001175271};
RN [1] {ECO:0000313|EMBL:KAK0402865.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PS9179 {ECO:0000313|EMBL:KAK0402865.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KAK0402865.1};
RA Schwarz E.M., Heppert J.K., Baniya A., Schwartz H.T., Tan C.-H.,
RA Antoshechkin I., Sternberg P.W., Goodrich-Blair H., Dillman A.R.;
RT "Genomic analysis of the entomopathogenic nematode Steinernema
RT hermaphroditum.";
RL Submitted (JUN-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] +
CC acetate; 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:ARBA00048287,
CC ECO:0000256|PIRNR:PIRNR037913};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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:KAK0402865.1}.
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DR EMBL; JAUCMV010000004; KAK0402865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA39HBM8; -.
DR Proteomes; UP001175271; Unassembled WGS sequence.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-ARBA.
DR GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:TreeGrafter.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR003084; HDAC_I/II.
DR InterPro; IPR000286; HDACs.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF10; HISTONE DEACETYLASE HDAC1; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 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 ECO:0000256|PIRNR:PIRNR037913};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037913};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW Reference proteome {ECO:0000313|Proteomes:UP001175271};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 24..315
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 261
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 401 AA; 45459 MW; 854A7A54D2BF1B15 CRC64;
MPRKDQISYF YHPNIGRFNY NRDHPMKPVR LAAVHDLVTR FGLQEHMTCV ESPLASATDM
KRFHTSEYID FLRTVTPRRA TLYKDQISEF NLNVDSPLVS GIFDFCSMYT GGTIAAAQRL
NRKESEIAIN WSGGLHHAKR SAASGFCYVN DIVIGIIELL KRHERVLYID IDVHHGDGVE
QAFANTDRVM TLSFHQYGRF FFPESGCMYD VGHGKGQFYA VNVPLKPGID DACYHALFKP
IVRKAIEAYD PMVIVMQCGA DSLQDDELGG FNLTIDGHAE CVRFVKGFCI PMLVLGGGGY
TPNNVAKCWT YETAVLIEKE QAIPRQIPAE SEYAAFFHPD YELRTINAER IEDLNTVQYM
NAIRIFTESN LSLVKGPPSV QMRPIVEDYY DNDEIAKMYI G
//
