GenomeNet

Database: UniProt/TrEMBL
Entry: B4L202_DROMO
LinkDB: B4L202_DROMO
Original site: B4L202_DROMO 
ID   B4L202_DROMO            Unreviewed;      1227 AA.
AC   B4L202;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   27-SEP-2017, entry version 62.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037911, ECO:0000256|SAAS:SAAS00818223};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037911, ECO:0000256|SAAS:SAAS00818223};
GN   Name=Dmoj\GI15905 {ECO:0000313|EMBL:EDW07723.2};
GN   ORFNames=Dmoj_GI15905 {ECO:0000313|EMBL:EDW07723.2}, GI15905
GN   {ECO:0000313|FlyBase:FBgn0138654};
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230 {ECO:0000313|EMBL:EDW07723.2, ECO:0000313|Proteomes:UP000009192};
RN   [1] {ECO:0000313|EMBL:EDW07723.2, ECO:0000313|Proteomes:UP000009192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 Genomes Consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B.,
RA   Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N.,
RA   Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P.,
RA   Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W.,
RA   Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A.,
RA   Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D.,
RA   Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D.,
RA   Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A.,
RA   Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H.,
RA   Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S.,
RA   Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A.,
RA   Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S.,
RA   Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J.,
RA   Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W.,
RA   Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A.,
RA   Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S.,
RA   Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H.,
RA   Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F.,
RA   Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S.,
RA   Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J.,
RA   Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A.,
RA   Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A.,
RA   Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B.,
RA   McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P.,
RA   Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B.,
RA   Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S.,
RA   Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D.,
RA   Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H.,
RA   Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A.,
RA   Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H.,
RA   Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L.,
RA   Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C.,
RA   Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M.,
RA   Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E.,
RA   Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D.,
RA   Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N.,
RA   Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C.,
RA   Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B.,
RA   Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A.,
RA   Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D.,
RA   Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P.,
RA   Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A.,
RA   An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P.,
RA   Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J.,
RA   Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A.,
RA   Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M.,
RA   Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G.,
RA   DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M.,
RA   Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D.,
RA   Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F.,
RA   LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T.,
RA   Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V.,
RA   Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J.,
RA   Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V.,
RA   Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T.,
RA   Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B.,
RA   Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P.,
RA   Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C.,
RA   Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L.,
RA   Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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:SAAS00818219}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037911,
CC       ECO:0000256|SAAS:SAAS00818221}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037911}.
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DR   EMBL; CH933810; EDW07723.2; -; Genomic_DNA.
DR   RefSeq; XP_002010406.2; XM_002010370.2.
DR   GeneID; 6584764; -.
DR   KEGG; dmo:Dmoj_GI15905; -.
DR   FlyBase; FBgn0138654; Dmoj\GI15905.
DR   InParanoid; B4L202; -.
DR   KO; K11406; -.
DR   OrthoDB; EOG091G0EQO; -.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
DR   Bgee; FBgn0138654; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblMetazoa.
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:0016573; P:histone acetylation; IEA:EnsemblMetazoa.
DR   GO; GO:0007616; P:long-term memory; IEA:EnsemblMetazoa.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; IEA:InterPro.
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; 2.130.10.10; -; 1.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR017320; Histone_deAcase_II_euk.
DR   InterPro; IPR030703; Histone_deacetylase_5.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   PANTHER; PTHR10625; PTHR10625; 1.
DR   PANTHER; PTHR10625:SF159; PTHR10625:SF159; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037911; HDAC_II_euk; 2.
DR   PRINTS; PR01270; HDASUPER.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00818226}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009192};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00490343};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW   Nucleus {ECO:0000256|SAAS:SAAS00818233};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009192};
KW   Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00818215};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00818213};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   DOMAIN      818   1132       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
FT   COILED      112    156       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    943    943       {ECO:0000256|PIRSR:PIRSR037911-1}.
FT   METAL       810    810       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   METAL       812    812       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   METAL       818    818       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   METAL       891    891       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
SQ   SEQUENCE   1227 AA;  132891 MW;  878F5BE326745BCB CRC64;
     MSSPDDRIPI RDLPPEAGND ERLLHITPGV LSLDFKPHQV DIDQQILELK KSQELQKQRL
     FHSYQEQTKQ MELEHKLQLE HKYHFAVHSH GAFQELREQS MVTAAAVVEE QHRQHQHQQH
     QQQQQLQQQQ QQQQQQQQQQ QQRERKEREV MKRKENCSAN ASPEVKQILS CFLMSRKSQA
     VAPNGTTTTS PYRNRGVVKS SSGESLPAGT VTSAHPYKIP QPPTSLLKYE SDFPLRKTAS
     EPNLLKIRLK QSVIERKARI GGPAGARRHE RLLQAAQRRH QKNSVLTNCN STTDSGPNSP
     PSSTTLSVGV VGSRGSPTSA PIQEENEEGS QYQPGQRSSI NNLPLFSSPS LPNISLGRPH
     LTNAQAGQAN YAMFAALQQH AAAAAAGPGA PPVNVAGVGV APTYYNPLAM SFGGRQPAPP
     LSMMPATGIA PQPSPVVRSA SATSTSSSQA SLVGDTAPPQ AHAASLTSAS SYLHLSGTTA
     VNLHAAAAAV AAAAAAAAAG SLPPSNSHSH SHSHSHSHAH ALYNAHQQQA QAQAQQVAHA
     HAPITDAQVA QVHLHKQGHR PLGRTQSAPL PLGHPMLTGA SQLSVVQTHY ENSEAERQAY
     EHQVLTQKLR QKVLTRSDAA AAAAVVAGIR EPQLQLREEE DDTAAEVMDL TDKKKPPKTV
     LTSTIATSTS QNLPEALAAA SYRAAAKSSK LRDQEYLQQQ RELLYLHEEE LAKDLMRPLS
     RTLSSPLVPG HGLSQIPDTG QHPTPIATSS SADHIPPVNL SLPHKRQLFS NVYAAQLRQH
     QQSSVESGLP AHKKITTGLA YDPLMLKHAC ICGDNAPHPE HSGRLQSVWA RLNETDLVKR
     CDRLRARKAT QEELQTVHTE AHAMLFGSNQ GQLTRPKLES TLSASFVRLS CGGLGVDLDT
     TWNEHHTATA ARMAAGCVID LAFKTAKGEL RNGFAVVRPP GHHAEANLAM GFCFFNSIAI
     AAKLLRQRVP EMKRILIVDW DVHHGNGTQQ AFYQSPDILY LSIHRHDDGN FFPGTGGPTE
     CGSGAGLGYN VNISWSGALN PPLGDAEYIA AFRTVVMPIA KCFNPDIVLV SSGFDAATGH
     PAPLGGYHVS PACFGLMTRE LLQLANGKVV LALEGGYDLA AICDSAQECV RALLGDPAAP
     IAPSELERPP CQNAINTLQK TIAIQQTHWP CVRLLEHTVC LSALDALKIE HDESETVNAM
     AGLSMQSLHR TLSRDDSEEP MDQDETK
//
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