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Database: UniProt/TrEMBL
Entry: Q17I08_AEDAE
LinkDB: Q17I08_AEDAE
Original site: Q17I08_AEDAE 
ID   Q17I08_AEDAE            Unreviewed;      1112 AA.
AC   Q17I08;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   22-NOV-2017, entry version 82.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037911, ECO:0000256|SAAS:SAAS00894283};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037911, ECO:0000256|SAAS:SAAS00894283};
GN   Name=5574971 {ECO:0000313|VectorBase:AAEL002528-PA};
GN   ORFNames=AAEL002528 {ECO:0000313|EMBL:EAT46268.1};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT46268.1, ECO:0000313|Proteomes:UP000008820};
RN   [1] {ECO:0000313|EMBL:EAT46268.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT46268.1};
RA   Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA   Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA   Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G.,
RA   Utterback T., Rogers Y.-H., Kravitz S., Fraser C.M.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAT46268.1, ECO:0000313|Proteomes:UP000008820, ECO:0000313|VectorBase:AAEL002528-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT46268.1}, and Liverpool/LVPib12
RC   {ECO:0000313|Proteomes:UP000008820,
RC   ECO:0000313|VectorBase:AAEL002528-PA};
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M.,
RA   Lobo N.F., Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J.,
RA   Sinkins S.P., Hogenkamp D.G., Amedeo P., Arensburger P.,
RA   Atkinson P.W., Bidwell S.L., Biedler J., Birney E., Bruggner R.V.,
RA   Costas J., Coy M.R., Crabtree J., Crawford M., DeBruyn B.,
RA   DeCaprio D., Eiglmeier K., Eisenstadt E., El-Dorry H., Gelbart W.M.,
RA   Gomes S.L., Hammond M., Hannick L.I., Hogan J.R., Holmes M.H.,
RA   Jaffe D., Johnston S.J., Kennedy R.C., Koo H., Kravitz S.,
RA   Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., Lovin D.D.,
RA   Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., Mori A.,
RA   Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D.,
RA   White O.R., Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A.,
RA   Raikhel A.S., Soares M.B., Knudson D.L., Lee N.H., Galagan J.,
RA   Salzberg S.L., Paulsen I.T., Dimopoulos G., Collins F.H., Bruce B.,
RA   Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
RN   [3] {ECO:0000313|EMBL:EAT46268.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT46268.1};
RG   VectorBase;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|VectorBase:AAEL002528-PA}
RP   IDENTIFICATION.
RC   STRAIN=Liverpool/LVPib12 {ECO:0000313|VectorBase:AAEL002528-PA};
RG   VectorBase;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events.
CC       {ECO:0000256|PIRNR:PIRNR037911}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC       {ECO:0000256|PIRNR:PIRNR037911, ECO:0000256|SAAS:SAAS00894227}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037911,
CC       ECO:0000256|SAAS:SAAS00894298}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037911}.
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DR   EMBL; CH477244; EAT46268.1; -; Genomic_DNA.
DR   RefSeq; XP_001655442.1; XM_001655392.1.
DR   ProteinModelPortal; Q17I08; -.
DR   STRING; 7159.AAEL002528-PA; -.
DR   EnsemblMetazoa; AAEL002528-RA; AAEL002528-PA; AAEL002528.
DR   KEGG; aag:AaeL_AAEL002528; -.
DR   VectorBase; AAEL002528-RA; AAEL002528-PA; AAEL002528.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   HOGENOM; HOG000232065; -.
DR   InParanoid; Q17I08; -.
DR   KO; K11406; -.
DR   OMA; KCENEEA; -.
DR   OrthoDB; EOG091G0EQO; -.
DR   PhylomeDB; Q17I08; -.
DR   Proteomes; UP000008820; Unassembled WGS sequence.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR017320; Histone_deAcase_II_euk.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625; PTHR10625; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00894233}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008820};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00870288};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW   Nucleus {ECO:0000256|SAAS:SAAS00894277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008820};
KW   Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00894309};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00894290};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   DOMAIN      699   1011       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
FT   COILED       73    117       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    821    821       {ECO:0000256|PIRSR:PIRSR037911-1}.
FT   METAL       691    691       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   METAL       693    693       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   METAL       699    699       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   METAL       769    769       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
SQ   SEQUENCE   1112 AA;  120699 MW;  49CFD834071B065F CRC64;
     MKSPREALLV SRCRPQYLDS LEAPRNQSLD RDLTHTSHLI LSFRSISLSI SQLRKEQELQ
     KQKLWHAFQE KNKELELQHR QQLEHKFQEL RDQRLAEEAA QQRERREREA MKRKEKQDFS
     ANASSEVKQK LQTFLIQKKQ AAASNGMNSP SFYRNLGVVK SSSGESIPAG AVVASSHPYK
     IPPPPPSSMA KYDSDFPLRK TASESNLLKI RIKQRVIEKR AMTGPLAAAR RQERLQQAAQ
     RRMQQKQAQL SGSGAGQPPT HPHLSTLAAQ HPANCAAGTP DSGPNSPPAL GSRGSPSNAP
     IQEENEDPQY GPGGRSSIND LSLFSSPSMP NISLGRPHLA DAHSTNHLVL SPQSMVPLRP
     HQMVAAGQPP PMSHHPPPFG HPSMLDQLTE QQLQAAAAAA AVASGLSINP THLGGIHAGV
     PPVYGHPITD AQVAQARLHK QGHRPLGRTQ SAPLPLGHPM LTGTGSGVVN IGQTHYENSD
     AERQAYEQHL LMKQKIRQTA LSRANCVREP QLKEEVESGE VIDLTDKKQP PKTTVITSNS
     VIKSTSHTTL LRDPAESLQQ QQHVEFLQSQ ALMRHSMQIG MLEDAYNRSL LRPLSRTSSS
     PLVHLGTPAS SNHPVAHSDT GQDDIPPPVN LTIQNRSRSM LSYTNEGLAS SGPLQLTTSS
     SASAIPIRLV QQNGKPTTGL AFDSLMLKHT CVCGDNAAHP EHSGRLQSIW ARLMETGLAA
     RCDKLRSRKA TQEELQSVHS EAHSLLFGTN QINRQKVDAS GVSFVRLGCG GVGVDLDTTW
     NEHHTAAAAR MAAGCVIDLC YKAAKGEIRN GFAVVRPPGH HAEPNAAMGF CFFNSIAIAA
     KLLRQRLSSE IQRVLVVDWD VHHGNGTQQV FYDDPSVLYL SIHRHDDGNF FPGTGGPTEC
     GAGPGLGFNV NIAWSGGLNP PLGDAEYLAA FRTIVMPIAR DFQPDIVLVS AGFDAAFGHP
     APLGGYMVSP ACFGYLTREL MKLADGKVIL ALEGGYDLAA ICDSAQECVR ALLGDDLAPI
     AATELSRPPC QTAVETLQKT IAIQMTHWPC VKRLAHTVSF SAMQAVSGAT GPDREESDTV
     TAMAGLSMQP PNRTSDISRE DSEEPMDQDE SK
//
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