ID   C5I7H9_DROME            Unreviewed;      1135 AA.
AC   C5I7H9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Histone deacetylase 6 isoform B {ECO:0000313|EMBL:ACN94122.1};
GN   Name=HDAC6 {ECO:0000313|EMBL:ACN94122.1};
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:ACN94122.1};
RN   [1] {ECO:0000313|EMBL:ACN94122.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A384 {ECO:0000313|EMBL:ACN94122.1};
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};
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DR   EMBL; FJ764845; ACN94122.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5I7H9; -.
DR   VEuPathDB; VectorBase:FBgn0026428; -.
DR   HOGENOM; CLU_007727_2_1_1; -.
DR   ExpressionAtlas; C5I7H9; 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          991..1090
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   REGION          17..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          941..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        948..962
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1135 AA;  125796 MW;  DFF04E8B5B8C3792 CRC64;
     MLRDIWIQSP PIVTRRSAQQ AKIQTRAMAS KSKTGTTGAA TAAGGTGSSS GSISAGFNAA
     DPRKSNKPNA ALLEAKRRAR NNMLKNQGCG SQESVTDIFQ NAVNSKSLVR KPTALIYDES
     MSQHCCLWDK EHYECPERFT RVLERCRELN LTERCLELPS RSATKDEILR LHTEEHFERL
     KETSGIRDDE RMEELSSRYD SIYIHPSTFE LSLLASGSTI ELVDHLVAGK AQNGMAIIRP
     PGHHAMKAEY NGYCFFNNVA LATQHALDVH KLQRVLIIDY DVHHGQGTQR FFYNDPRVVY
     FSIHRFEHGS FWPHLHESDY HAIGSGAGTG YNFNVPLNAT GMTNGDYLAI FQQLLLPVAL
     EFQPELIIVS AGYDAALGCP EGEMEVTPAC YPHLLNPLLR LADARVAVVL EGGYCLDSLA
     EGAALTLRSL LGDPCPPLVE TVPLPRAELA QALLSCIAVH RPHWRCLQLQ QTYDCVELQD
     RDKEEDLHTV LRHWIGGPPP MDRYPTRDTA IPLPPEKLTS NAARLQVLRA ETKLSVPSFK
     VCYAYDAQML LHCNLNDTGH PEQPSRIQHI HKMHDDYGLL KQMKQLSPRA ATTDEVCLAH
     TRAHVNTVRR LLGREPKELH DAAGIYNSVY LHPRTFDCAT LAAGLVLQAV DSVLRGESRS
     GICNVRPPGH HAEQDHPHGF CIFNNVAIAA QYAIRDFGLE RVLIVDWDVH HGNGTQHIFE
     SNPKVLYISL HRYEHGSFFP KGPDGNFDVV GKGAGRGFNV NIPWNKKGMG DLEYALAFQQ
     LIMPIAYEFN PQLVLVSAGF DAAIGDPLGG CKVTAEGYGM LTHWLSALAS GRIIVCLEGG
     YNVNSISYAM TMCTKTLLGD PVPTPQLGAT ALQKPPTVAF QSCVESLQQC LQVQRNHWRS
     LEFVGRRLPR DPVVGENNNE DFLTASLRHL NISNDDATAA AGGLAGDRPD CGDERPSGSK
     PKVKVKTLSD YLAENKEALE QSEMFAVYPL KTCPHLRLLR PEEAPRSLDS GAECSVCGST
     GENWVCLSCR HVACGRYVNA HMEQHSVEEQ HPLAMSTADL SVWCYACSAY VDHPRLYAYL
     NPLHEDKFQE PMAWTHGCAW REDGCYATGP DGRDEDDDDD NGAGSSICLR LERNN
//