ID C5I7E7_DROME Unreviewed; 1135 AA.
AC C5I7E7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Histone deacetylase 6 isoform B {ECO:0000313|EMBL:ACN94090.1};
GN Name=HDAC6 {ECO:0000313|EMBL:ACN94090.1};
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:ACN94090.1};
RN [1] {ECO:0000313|EMBL:ACN94090.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A186 {ECO:0000313|EMBL:ACN94090.1}, and A191
RC {ECO:0000313|EMBL:ACN94098.1};
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; FJ764841; ACN94090.1; -; Genomic_DNA.
DR EMBL; FJ764842; ACN94098.1; -; Genomic_DNA.
DR AlphaFoldDB; C5I7E7; -.
DR SMR; C5I7E7; -.
DR VEuPathDB; VectorBase:FBgn0026428; -.
DR HOGENOM; CLU_007727_2_1_1; -.
DR ExpressionAtlas; C5I7E7; 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 1..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 12..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; 125824 MW; 2485423D983AFBFC CRC64;
MLRDIWIQSP PIVTRRSAQQ AKIQTRAMAS KSKTGTTGAA TAAGGTGSSS GSISGGFNAA
DPRKSNKPNA ALLEAKRRAR NNMLKNQGCG SQESVTDIFQ NAVNSKSLVR KPTALIYDES
MSQHCCLWDK EHYECPERFT RVLERCRELN LTERCLELPS RSATKDEILR LHTEEHFERL
KETSGIRDDE RMEELSSRYD SIYIHPSTFE LSLLASGSTI ELVDHLVAGR AQNGMAIIRP
PGHHAMKAEY NGYCFFNNVA LATQHALDVH KLQRILIIDY 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
//