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Database: UniProt
Entry: A0A182GHI8_AEDAL
LinkDB: A0A182GHI8_AEDAL
Original site: A0A182GHI8_AEDAL 
ID   A0A182GHI8_AEDAL        Unreviewed;       299 AA.
AC   A0A182GHI8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Histone deacetylase 8 {ECO:0000256|ARBA:ARBA00040347};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE   AltName: Full=Protein deacetylase HDAC8 {ECO:0000256|ARBA:ARBA00041964};
DE   AltName: Full=Protein decrotonylase HDAC8 {ECO:0000256|ARBA:ARBA00042783};
GN   ORFNames=RP20_CCG009997 {ECO:0000313|EMBL:KXJ82970.1};
OS   Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7160 {ECO:0000313|EMBL:KXJ82970.1};
RN   [1] {ECO:0000313|EMBL:KXJ82970.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Foshan {ECO:0000313|EMBL:KXJ82970.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KXJ82970.1};
RX   PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA   Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA   Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA   Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA   Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA   Yan G., Tu Z.J., Fang X., James A.A.;
RT   "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT   insights into its biology, genetics, and evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN   [2] {ECO:0000313|EMBL:KXJ82970.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Foshan {ECO:0000313|EMBL:KXJ82970.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KXJ82970.1};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate
CC         + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:35899, ChEBI:CHEBI:137954;
CC         Evidence={ECO:0000256|ARBA:ARBA00029357};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC         Evidence={ECO:0000256|ARBA:ARBA00029357};
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:ARBA00029372};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC         Evidence={ECO:0000256|ARBA:ARBA00029372};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-
CC         [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; Evidence={ECO:0000256|ARBA:ARBA00029349};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC         Evidence={ECO:0000256|ARBA:ARBA00029349};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR   EMBL; KQ560338; KXJ82970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A182GHI8; -.
DR   STRING; 7160.A0A182GHI8; -.
DR   VEuPathDB; VectorBase:AALC636_004562; -.
DR   VEuPathDB; VectorBase:AALF009997; -.
DR   VEuPathDB; VectorBase:AALFPA_057216; -.
DR   Proteomes; UP000249989; Unassembled WGS sequence.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
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:SF66; HISTONE DEACETYLASE 8; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
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   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249989};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491}.
SQ   SEQUENCE   299 AA;  33234 MW;  8712313DA9FC8FD1 CRC64;
     MELYILRILI LKLDYLIVLA YDCPMIEKVY DFATSIVGTT LAAVDAILAG ATIAINWHGG
     WHHAQRDKAA GFCYVNDIVI GIHRLRTRFQ KVLYLDLDVH HGDGVEDAFS FSKYVMTVSF
     HQHEPGYFPG TGAVSSIGIG PGKGYTVNAP YSRDITGDMF VPYFQNISSA VYNAFRPDVC
     IVQCGADVIV GDHLGGTSLI PEDCLKCVQQ VLSWNTPTIF LGGGGYNVIN TAKYWTQLTA
     LILQKTISRD IPDNAFFPDF GPDFTLDIYR RNVKDGNTKD NLFRIETFIK ENLKLNVAS
//
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