ID D0ULC2_9CRUS Unreviewed; 283 AA.
AC D0ULC2;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE Flags: Fragment;
OS Limnadia lenticularis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Spinicaudata; Limnadiidae; Limnadia.
OX NCBI_TaxID=84336 {ECO:0000313|EMBL:ACY43538.1};
RN [1] {ECO:0000313|EMBL:ACY43538.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20147900; DOI=10.1038/nature08742;
RA Regier J.C., Shultz J.W., Zwick A., Hussey A., Ball B., Wetzer R.,
RA Martin J.W., Cunningham C.W.;
RT "Arthropod relationships revealed by phylogenomic analysis of nuclear
RT protein-coding sequences.";
RL Nature 463:1079-1083(2010).
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};
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR EMBL; GQ885965; ACY43538.1; -; mRNA.
DR AlphaFoldDB; D0ULC2; -.
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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT DOMAIN 1..283
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 237
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACY43538.1"
FT NON_TER 283
FT /evidence="ECO:0000313|EMBL:ACY43538.1"
SQ SEQUENCE 283 AA; 32046 MW; 6F94711DC97B8855 CRC64;
HPMKPHRIRM THNLLLNYGL YRKMEIYRPH KATAEEMTKF HSDDYIRFLR SIRPDNMSEY
NKQMQRFNVG EDCPVFDGLY EFCQLSAGGS VAGAVKLNKQ ATEIAVNWAG GLHHAKKSEA
SGFCYVNDIV LAILELLKYH PRVLYIDIDI HHGDGVEEAF YTTDRVMTVS FHKYGEYFPG
TGDLRDIGAG KGKYYAVNFP LRDGIDDESY EHIFVPIMSK VMETYQPSAV VLQCGADSLS
GDRLGCFNLT LKGHAKCVEF VKKYNLPLLL LGGGGYTIRN VAR
//
