ID T1GKI2_MEGSC Unreviewed; 407 AA.
AC T1GKI2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 08-NOV-2023, entry version 53.
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};
OS Megaselia scalaris (Humpbacked fly) (Phora scalaris).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Platypezoidea;
OC Phoridae; Megaseliini; Megaselia.
OX NCBI_TaxID=36166 {ECO:0000313|EnsemblMetazoa:MESCA004006-PA, ECO:0000313|Proteomes:UP000015102};
RN [1] {ECO:0000313|Proteomes:UP000015102}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Durham, NC isolate 2 -- Noor lab
RC {ECO:0000313|Proteomes:UP000015102};
RA Hughes D.;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:MESCA004006-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR EMBL; CAQQ02007907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAQQ02007908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAQQ02007909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 36166.T1GKI2; -.
DR EnsemblMetazoa; MESCA004006-RA; MESCA004006-PA; MESCA004006.
DR HOGENOM; CLU_007727_7_6_1; -.
DR Proteomes; UP000015102; 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:SF69; HISTONE DEACETYLASE 3; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 2.
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:UP000015102};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 2..285
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 297..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 232
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 407 AA; 45758 MW; CF89A84632A8C98D CRC64;
MVRFHSDEYI EFLQTVTPQN VQCNSVGYTK YLSHFSVGDD CPVFDGLFDF CAMYTGASLE
GAQKLXXXXX XXXXXXXXXX XXXXXXXXXX XXXNHSDICI NWSGGLHHAK KFEASGFCYV
NDIVIGILEL LKYHPRVLYI DIDVHHGDGV QEAFYLTDRV MTVSFHKYGN WFFPGTGDMY
EIGAESGRYY SVNVPLKEGI DDLSYYSVFK PVISHVMEFY RPTAIVLQCG ADSLAGDRLG
CFSLSTRGHG DCVKFVKEFN VPTLVVGGGG YTPRNVARCW TYETSLLVEE DISNELPKTE
SSIXPDGVLH PDVNSRQDNA NSKQYLELIV KHVYENLKML QHAPSVQMFN IPEDALDPQE
QEPDPDVRIN QDEEDKMVEP KNEFFDGDND NDKGDESERQ KADGAGS
//