ID B5RJR1_DROME Unreviewed; 1244 AA. AC B5RJR1; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 23-MAY-2018, entry version 74. DE SubName: Full=Dachs, isoform D {ECO:0000313|EMBL:ADV36979.1}; DE EC=3.6.1.3 {ECO:0000313|EMBL:ADV36979.1}; DE SubName: Full=LP16090p {ECO:0000313|EMBL:ACH95309.1}; GN Name=d {ECO:0000313|EMBL:ADV36979.1, ECO:0000313|FlyBase:FBgn0262029}; GN Synonyms=29C3-D1 {ECO:0000313|EMBL:ADV36979.1}, 29CD GN {ECO:0000313|EMBL:ADV36979.1}, AAF52683 {ECO:0000313|EMBL:ADV36979.1}, GN anon-EST:Liang-1.78 {ECO:0000313|EMBL:ADV36979.1}, CG10595 GN {ECO:0000313|EMBL:ADV36979.1}, CG13087 {ECO:0000313|EMBL:ADV36979.1}, GN CG31610 {ECO:0000313|EMBL:ADV36979.1}, clone 1.78 GN {ECO:0000313|EMBL:ADV36979.1}, D {ECO:0000313|EMBL:ADV36979.1}, d-RA GN {ECO:0000313|EMBL:ACH95309.1}, Dmel\CG42840 GN {ECO:0000313|EMBL:ADV36979.1}, DmMyo20 {ECO:0000313|EMBL:ADV36979.1}, GN Ds {ECO:0000313|EMBL:ADV36979.1}, l(2)c00146 GN {ECO:0000313|EMBL:ADV36979.1}, Myo29D {ECO:0000313|EMBL:ADV36979.1}, GN Myo3A {ECO:0000313|EMBL:ADV36979.1}; GN ORFNames=CG42840 {ECO:0000313|EMBL:ADV36979.1, GN ECO:0000313|FlyBase:FBgn0262029}, Dmel_CG42840 GN {ECO:0000313|EMBL:ADV36979.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:ACH95309.1}; RN [1] {ECO:0000313|EMBL:ADV36979.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., RA Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., RA Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:ADV36979.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:ADV36979.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:ADV36979.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:ADV36979.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:ADV36979.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:ADV36979.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:ADV36979.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., RA Yu C., Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:ADV36979.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [10] {ECO:0000313|EMBL:ADV36979.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [11] {ECO:0000313|EMBL:ACH95309.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley {ECO:0000313|EMBL:ACH95309.1}; RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:ADV36979.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {ECO:0000256|PROSITE- CC ProRule:PRU00782}. 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; BT044535; ACH95309.1; -; mRNA. DR EMBL; AE014134; ADV36979.1; -; Genomic_DNA. DR RefSeq; NP_001188729.1; NM_001201800.1. DR UniGene; Dm.357; -. DR EnsemblMetazoa; FBtr0303923; FBpp0292924; FBgn0262029. DR GeneID; 34179; -. DR KEGG; dme:Dmel_CG42840; -. DR CTD; 34179; -. DR FlyBase; FBgn0262029; d. DR eggNOG; KOG0160; Eukaryota. DR eggNOG; COG5022; LUCA. DR GeneTree; ENSGT00900000140778; -. DR KO; K16677; -. DR OMA; QAWKACL; -. DR OrthoDB; EOG091G01EG; -. DR GenomeRNAi; 34179; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0262029; -. DR ExpressionAtlas; B5RJR1; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW. DR GO; GO:0051015; F:actin filament binding; IDA:FlyBase. DR GO; GO:0008017; F:microtubule binding; IEA:InterPro. DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0032947; F:protein-containing complex scaffold activity; IC:FlyBase. DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:FlyBase. DR GO; GO:0001736; P:establishment of planar polarity; IMP:FlyBase. DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase. DR GO; GO:0035218; P:leg disc development; IMP:FlyBase. DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro. DR GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase. DR GO; GO:0045572; P:positive regulation of imaginal disc growth; IMP:FlyBase. DR GO; GO:0035220; P:wing disc development; IMP:FlyBase. DR CDD; cd14881; MYSc_Myo20; 1. DR Gene3D; 3.40.850.10; -; 3. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR036029; MYSc_Myo20. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00612; IQ; 1. DR Pfam; PF00063; Myosin_head; 2. DR PRINTS; PR00193; MYOSINHEAVY. DR SMART; SM00242; MYSc; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS50096; IQ; 1. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. PE 2: Evidence at transcript level; KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782}; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782, KW ECO:0000256|SAAS:SAAS00875240}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Hydrolase {ECO:0000313|EMBL:ADV36979.1}; KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782, KW ECO:0000256|SAAS:SAAS00874053}; KW Myosin {ECO:0000256|PROSITE-ProRule:PRU00782, KW ECO:0000256|SAAS:SAAS01033784}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782, KW ECO:0000256|SAAS:SAAS00874078}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}. FT DOMAIN 292 1036 Myosin motor. {ECO:0000259|PROSITE: FT PS51456}. FT NP_BIND 380 387 ATP. {ECO:0000256|PROSITE-ProRule: FT PRU00782}. FT REGION 905 927 Actin-binding. {ECO:0000256|PROSITE- FT ProRule:PRU00782}. FT COILED 38 58 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1244 AA; 135410 MW; 73B6008973C07230 CRC64; MATLGLSKVF ILDKYFTELQ KFWETEKKLQ DASSSNEAVH LQQRLKSLST ELVTLRNRLH VGHGPGQGQS QGNGAQPVAP APNAGPKANN FDLNASSPNL NLSSSGAGLS ASAVQQHTNG HHTTSKNHSF SHTLPANSGS GGGGGAGGGA VVSARNTSIP HPLPHQLAEK PGLSHQQSGS GHGQSTGTLP HMSGMGSILG QNSHSHAPVN NNSNNSNTLP MRTSNSGHLG INGGGVGHHL SHAHSQQLPF IPQSKHTNPC QSVKTLPFGF GFSESQQKMQ QQQQQGNSSP KDMQDLIHLS GPLTEHAVMR TLQARFNERR YFTNVGPILL SINPYLDVGN PLTLTSTRAM PLAPQLQKIV QEAVRQQSET GYPQAIILSG TSGAGKTANA MLMLRQLFAI AGGGPETDAF KHLAAAFTVL RSLGSAKTTT NSESSRIGQF IEVQVTDGAL YRTKIHCYFL DQTRVIRPLP KEKNYHIFYQ LLAGLSREER QKLHLDGYSP ANLRYLRGDI GQNEQEDAAR FQAWKTCLGI LGIPFLDVVR VLAAVLLLGN VQFIDGGGLE VDVKGETELN SVASLLGVPP AALFRGLTTR THNVRGQLVK SVCGDGDANM TRDCLAKALY CRTVATIVRR ANSLKRLGST LGTLSSDSNE SVHNQADVAS QHASTIGGGN AGSKSMAALN NAVRHATSDG FIGILDMFGF EEPSPHAHLE HLCINLCAET MQHFYNTHIF KSSVESCRDE GIVCDTEVDY VDNVPCIDLI SSLRTGLLSM LDAECSVRGT AESYVTKLKV QHRSSTRLET KPTAEPHDPR MFLIRHFAGR VEYDTTDFLD TNRDVVPDDL VGVFYKHTCN FGFATHLFGS ELKALYAQQQ APRGLSFRIS PTSHSDLLNG DEPVSTLTQD FHTRLDNLLR TLVHARPHFV RCIRSNGTEA ARSFDRATVV RQIRSLQVLE TVNLMASGFP HRMRFKQFNA RYRMLAPFRL LRRSEDKALE DCQLILKYAM EQPPVLDGSV TLAWAPGKRH VFLSEGIRQH LEHLRTEIRH KSATLMQATW RGWWWRKKMG NGGAKRSKIP GLQQAPLPNN KTTPNSAAQN KAASSTMAAL AAVAAAAPIS VPRLSAKTTS LGIGGTVARP RPQPIAGTPP PDPQEKCDQK IIQQTCNLFG LDLERPPPVP PSRSYTITGN SKISYPQNRV MKMNFPEEGQ SEAPQLKKGE AVTVVGASTV RGHLMVEHKG QSFHVPFQFM TLSK //