ID A0A484BXD3_DRONA Unreviewed; 525 AA.
AC A0A484BXD3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 08-NOV-2023, entry version 19.
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=AWZ03_000149 {ECO:0000313|EMBL:TDG53334.1};
OS Drosophila navojoa (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG53334.1, ECO:0000313|Proteomes:UP000295192};
RN [1] {ECO:0000313|EMBL:TDG53334.1, ECO:0000313|Proteomes:UP000295192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG53334.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:TDG53334.1};
RX PubMed=30423125; DOI=.1093/jhered/esy059;
RA Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT the mojavensis Cluster.";
RL J. Hered. 110:118-123(2019).
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 -!- 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:TDG53334.1}.
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DR EMBL; LSRL02000001; TDG53334.1; -; Genomic_DNA.
DR RefSeq; XP_017957153.1; XM_018101664.1.
DR AlphaFoldDB; A0A484BXD3; -.
DR STRING; 7232.A0A484BXD3; -.
DR GeneID; 108651775; -.
DR KEGG; dnv:108651775; -.
DR OMA; GYNPWSV; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000295192; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; PTHR48252; HISTONE DEACETYLASE 2-RELATED; 1.
DR PANTHER; PTHR48252:SF57; HISTONE DEACETYLASE HDAC1; 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:UP000295192};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 26..315
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 381..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 176
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 525 AA; 58645 MW; 7B075A7DC405969D CRC64;
MQSHSKKRVC YYYDSDIGNY YYGQGHPMKP HRIRMTHNLL LNYGLYRKME IYRPHKATAD
EMTKFHSDEY VRFLRSIRPD NMTEYNKQMQ RFNVGEDCPV FDGLYEFCQL SAGGSVAAAV
KLNKQASEIC INWGGGLHHA KKSEASGFCY VNDIVLGILE LLKYHQRVLY IDIDVHHGDG
VEEAFYTTDR VMTVSFHKYG EYFPGTGDLR DIGAGKGKYY AVNIPLRDGM DDDAYESIFV
PIISKVMETF QPAAVVLQCG ADSLTGDRLG CFNLTVKGHG KCVEFVKKYN LPFLMVGGGG
YTIRNVSRCW TYETSVALNV EIANELPYND YFEYFGPDFK LHISPSNMTN QNTAEYLEKI
KNKLFDNLRL LPHAPGVQIQ AIPEDAINDE SEDEDKVDKD ERLPQSDKDK RIVPENEYSD
SEDEGEGGRR DNRNYKGQRK RPRLDKEPII SNASSKASAE SSETKDEKEK AEAEGEESAT
ANNTNSGSSN SGGSNSNKDD AATPTAGGGG SGAAAASKGA KENNI
//