ID   C5I7G2_DROME            Unreviewed;      1128 AA.
AC   C5I7G2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Histone deacetylase 6 isoform A {ECO:0000313|EMBL:ACN94103.1};
GN   Name=HDAC6 {ECO:0000313|EMBL:ACN94103.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:ACN94103.1};
RN   [1] {ECO:0000313|EMBL:ACN94103.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A229 {ECO:0000313|EMBL:ACN94103.1};
RX   PubMed=19349642; DOI=10.1093/molbev/msp065;
RA   Svetec N., Pavlidis P., Stephan W.;
RT   "Recent strong positive selection on Drosophila melanogaster HDAC6, a gene
RT   encoding a stress surveillance factor, as revealed by population genomic
RT   analysis.";
RL   Mol. Biol. Evol. 26:1549-1556(2009).
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   ---------------------------------------------------------------------------
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; FJ764843; ACN94103.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5I7G2; -.
DR   VEuPathDB; VectorBase:FBgn0026428; -.
DR   ExpressionAtlas; C5I7G2; baseline and differential.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd10002; HDAC10_HDAC6-dom1; 1.
DR   CDD; cd10003; HDAC6-dom2; 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; His_deacetylse.
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:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 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   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00502};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00502};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT   DOMAIN          984..1083
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..955
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1128 AA;  124941 MW;  E886388D0D92533E CRC64;
     MSPPIVTRRS AQQAKIQTRA MASKSKTGTT GAATAAGGTG SSSGSISGGF NAADPRKSNK
     PNAALLEAKR RARNNMLKNQ GCGSQESVTD IFQNAVNSKS LVRKPTALIY DESMSQHCCL
     WDKEHYECPE RFTRVLERCR ELNLTERCLE LPSRSATKDE ILRLHTEEHF ERLKETSGIR
     DDERMEELSS RYDSIYIHPS TFELSLLASG STIELVDHLV AGRAQNGMAI IRPPGHHAMK
     AEYNGYCFFN NVALATQHAL DVHKLQRILI IDYDVHHGQG TQRFFYNDPR VVYFSIHRFE
     HGSFWPHLHE SDYHAIGSGA GTGYNFNVPL NATGMTNGDY LAIFQQLLLP VALEFQPELI
     IVSAGYDAAL GCPEGEMEVT PACYPHLLNP LLRLADARVA VVLEGGYCLD SLAEGAALTL
     RSLLGDPCPP LVETVPLPRA ELAQALLSCI AVHRPHWRCL QLQQTYDCVE LQDRDKEEDL
     HTVLRHWIGG PPPMDRYPTR DTAIPLPPEK LTSNAARLQV LRAETKLSVP SFKVCYAYDA
     QMLLHCNLND TGHPEQPSRI QHIHKMHDDY GLLKQMKQLS PRAATTDEVC LAHTRAHVNT
     VRRLLGREPK ELHDAAGIYN SVYLHPRTFD CATLAAGLVL QAVDSVLRGE SRSGICNVRP
     PGHHAEQDHP HGFCIFNNVA IAAQYAIRDF GLERVLIVDW DVHHGNGTQH IFESNPKVLY
     ISLHRYEHGS FFPKGPDGNF DVVGKGAGRG FNVNIPWNKK GMGDLEYALA FQQLIMPIAY
     EFNPQLVLVS AGFDAAIGDP LGGCKVTAEG YGMLTHWLSA LASGRIIVCL EGGYNVNSIS
     YAMTMCTKTL LGDPVPTPQL GATALQKPPT VAFQSCVESL QQCLQVQRNH WRSLEFVGRR
     LPRDPVVGEN NNEDFLTASL RHLNISNDDA TAAAGGLAGD RPDCGDERPS GSKPKVKVKT
     LSDYLAENKE ALEQSEMFAV YPLKTCPHLR LLRPEEAPRS LDSGAECSVC GSTGENWVCL
     SCRHVACGRY VNAHMEQHSV EEQHPLAMST ADLSVWCYAC SAYVDHPRLY AYLNPLHEDK
     FQEPMAWTHG CAWREDGCYA TGPDGRDEDD DDDNVAGSSI CLRLERNN
//