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Database: UniProt
Entry: T1GKI2_MEGSC
LinkDB: T1GKI2_MEGSC
Original site: T1GKI2_MEGSC 
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
//
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