ID A7LPD8_CAEEL Unreviewed; 957 AA. AC A7LPD8; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 02-SEP-2026, entry version 130. DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111}; DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111}; GN Name=hda-6 {ECO:0000313|EMBL:CCD71106.1, GN ECO:0000313|WormBase:F41H10.6c}; GN ORFNames=CELE_F41H10.6 {ECO:0000313|EMBL:CCD71106.1}, F41H10.6 GN {ECO:0000313|WormBase:F41H10.6c}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD71106.1, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|EMBL:CCD71106.1, ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD71106.1, RC ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2 CC subfamily. {ECO:0000256|ARBA:ARBA00007738}. 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; BX284604; CCD71106.1; -; Genomic_DNA. DR RefSeq; NP_001122780.1; NM_001129308.4. DR AlphaFoldDB; A7LPD8; -. DR SMR; A7LPD8; -. DR PeptideAtlas; A7LPD8; -. DR GeneID; 177316; -. DR UCSC; F41H10.6c; c. elegans. DR AGR; WB:WBGene00018319; -. DR CTD; 177316; -. DR WormBase; F41H10.6c; CE41132; WBGene00018319; hda-6. DR HOGENOM; CLU_007727_2_1_1; -. DR OMA; HTRSHVN; -. DR OrthoDB; 424012at2759; -. DR PhylomeDB; A7LPD8; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00018319; Expressed in germ line (C elegans) and 4 other cell types or tissues. DR ExpressionAtlas; A7LPD8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; IEA:UniProtKB-EC. DR GO; GO:0033558; F:protein lysine deacetylase activity; ISS:WormBase. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR FunFam; 3.40.800.20:FF:000014; Histone deacetylase 15; 1. DR FunFam; 3.30.40.10:FF:000342; Histone deacetylase 6; 1. DR FunFam; 3.40.800.20:FF:000048; Histone deacetylase 6; 1. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR000286; HDACs. DR InterPro; IPR023801; His_deacetylse_dom. DR InterPro; IPR037138; His_deacetylse_dom_sf. DR InterPro; IPR023696; Ureohydrolase_dom_sf. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR001607; Znf_UBP. DR PANTHER; PTHR10625:SF47; HISTONE DEACETYLASE 6; 1. DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1. DR Pfam; PF00850; Hist_deacetyl; 2. DR Pfam; PF02148; zf-UBP; 1. DR PRINTS; PR01270; HDASUPER. DR SMART; SM00290; ZnF_UBP; 1. DR SUPFAM; SSF52768; Arginase/deacetylase; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50271; ZF_UBP; 1. PE 1: Evidence at protein level; KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A7LPD8}; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Repressor {ECO:0000256|ARBA:ARBA00022491}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00502}. FT DOMAIN 855..953 FT /note="UBP-type" FT /evidence="ECO:0000259|PROSITE:PS50271" FT REGION 817..842 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 820..833 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 957 AA; 107024 MW; C2D025AFB4920FD2 CRC64; MLFEDRQKNR STGPTLIGFN QTQNEHENTV CPTHPESSDR ILKIKEALTK TKILEKCTVL TNFLEIDDAD LEVTHDKSMV KDLMESEKKT QEDINSQCEK YDSVFMTEFQ NSMKVAKDGV ACVRDLTNRI MANEASNGFA VVRPPGHHAD SVSPCGFCLF NNVAQAAEEA FFSGAERILI VDLDVHHGHG TQRIFYDDKR VLYFSIHRHE HGLFWPHLPE SDFDHIGSGK GLGYNANLAL NETGCTDSDY LSIIFHVLLP LATQFDPHFV IISAGFDALL GDPLGGMCLT PDGYSHILYH LKSLAQGRML VVLEGGYNHQ ISAVAVQRCV RVLLGYAPFS IELNEAPKES TVDSCVSLVS VLRHHWNCFD YFPSRTSLRL AQWPIVNTKV IYNYDPTTRR ADTGEIIQDE LASTEFTASD VIPTENMETL IYFNEGDDAH FDLEEDNHPE KPARTRRILK TLRESGVLEK CVDRNCERIA TNEEIRLVHT KKMLEHLRTT ETMKDEELME EAEKEFNSIY LTRDTLKVAR KAVGAVLQSV DEIFEKDAGQ RNALVIVRPP GHHASASKSS GFCIFNNVAV AAKYAQRRHK AKRVLILDWD VHHGNGTQEI FYEDSNVMYM SIHRHDKGNF YPIGEPKDYS DVGEGAGEGM SVNVPFSGVQ MGDNEYQMAF QRVIMPIAYQ FNPDLVLISA GFDAAVDDPL GEYKVTPETF ALMTYQLSSL AGGRIITVLE GGYNLTSISN SAQAVCEVLQ NRSMLRRLRE EKEQFATKPQ KIESSCIKTI REVCAVQQKY WSILKGFQVT PSNYGLDIDD EAYDDDSIDM ADQSSSSGSS SSSTRPSHNL EIMDSGPAHA VVPLATCPHL KEVKPLPPAK INARTACSEC QIGAEVWTCL TCYKYNCGRF VNEHAMMHHL SSSHPMALSM ADLSVWCYPC DSYVHNPALI GAKSAAHESK FGETMPS //