ID A8X7W2_CAEBR Unreviewed; 455 AA. AC A8X7W2; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 93. 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=CBG09063 {ECO:0000313|EMBL:CAP28723.1, GN ECO:0000313|WormBase:CBG09063}, CBG_09063 GN {ECO:0000313|EMBL:CAP28723.1}; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP28723.1, ECO:0000313|Proteomes:UP000008549}; RN [1] {ECO:0000313|EMBL:CAP28723.1, ECO:0000313|Proteomes:UP000008549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16 {ECO:0000313|EMBL:CAP28723.1, RC ECO:0000313|Proteomes:UP000008549}; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., RA Durbin R., Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative RT genomics."; RL PLoS Biol. 1:166-192(2003). 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 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 --------------------------------------------------------------------------- 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 EMBL; HE601284; CAP28723.1; -; Genomic_DNA. DR RefSeq; XP_002641202.1; XM_002641156.1. DR AlphaFoldDB; A8X7W2; -. DR STRING; 6238.A8X7W2; -. DR EnsemblMetazoa; CBG09063.1; CBG09063.1; WBGene00030730. DR GeneID; 8583195; -. DR KEGG; cbr:CBG_09063; -. DR CTD; 8583195; -. DR WormBase; CBG09063; CBP08173; WBGene00030730; -. DR eggNOG; KOG1342; Eukaryota. DR HOGENOM; CLU_007727_7_4_1; -. DR InParanoid; A8X7W2; -. DR OMA; WRSAYWS; -. DR OrthoDB; 1327607at2759; -. DR Proteomes; UP000008549; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0016581; C:NuRD complex; IBA:GO_Central. DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. 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:SF45; HISTONE DEACETYLASE 1; 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}; Hydrolase {ECO:0000256|PIRNR:PIRNR037913}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3}; KW Nucleus {ECO:0000256|PIRNR:PIRNR037913}; KW Reference proteome {ECO:0000313|Proteomes:UP000008549}; KW Repressor {ECO:0000256|ARBA:ARBA00022491}; KW Transcription {ECO:0000256|PIRNR:PIRNR037913}; KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}. FT DOMAIN 32..322 FT /note="Histone deacetylase" FT /evidence="ECO:0000259|Pfam:PF00850" FT REGION 423..455 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 425..446 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 146 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1" FT BINDING 104 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2" FT BINDING 154 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2" FT BINDING 181 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3" FT BINDING 183 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3" FT BINDING 269 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3" FT BINDING 308 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2" SQ SEQUENCE 455 AA; 51696 MW; F47EEA3536489432 CRC64; MVAPAPLRDQ SKRRVCYYYD TNVGNYYYGP GHVMKPHRIR MANELILSYG LYQNLSIYRP RPASFEAMTT FHSDEYITFL RDANIDNLNS FGASKGKFSQ NNDDCPLFDG LYEFCQLSCG GSLAAAIKLN KKKTDIAINW MGGLHHAKKS ESSGFCYTND IVVGILELLK FHKRVLYVDI DIHHGDGVEE AFFDTNRVMT VSFHRFGNFF PGTGDIKDVG IYNGRLYSVN VPLSDGITDE SYERIFVPVM KKVMEMFDPQ AVVLQCGADS LYGDRLGKFN LSLRGHGACA EFFRKYDVPL MMVGGGGYTP RNVARCWAYE TSIAVGIEVP NELPFNNYYE YFGPDYKLHI EPSQVLKNDN PDQKLLELQK EIFENLSQLD KVPSVQMQPM EDDTLPVLEF EDIARDEENP DVRLPMSIMD SCQHNDADFY DDENGGDDHR NEANGLRQAE AENNL //