ID M9PBB5_DROME Unreviewed; 661 AA. AC M9PBB5; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 16-JAN-2019, entry version 53. DE SubName: Full=Vasa, isoform B {ECO:0000313|EMBL:AGB92993.1}; DE SubName: Full=Vasa, isoform C {ECO:0000313|EMBL:ALI30207.1}; DE EC=2.7.7.- {ECO:0000313|EMBL:AGB92993.1, ECO:0000313|EMBL:ALI30207.1}; DE EC=3.6.1.3 {ECO:0000313|EMBL:AGB92993.1, ECO:0000313|EMBL:ALI30207.1}; GN Name=vas {ECO:0000313|EMBL:AGB92993.1, GN ECO:0000313|FlyBase:FBgn0283442}; GN Synonyms=BG:DS00929.14 {ECO:0000313|EMBL:AGB92993.1}, CG3506 GN {ECO:0000313|EMBL:AGB92993.1}, CG43081 {ECO:0000313|EMBL:AGB92993.1}, GN cgt {ECO:0000313|EMBL:AGB92993.1}, Dmel\CG46283 GN {ECO:0000313|EMBL:AGB92993.1}, DmRH25 {ECO:0000313|EMBL:AGB92993.1}, GN EP(2)0812 {ECO:0000313|EMBL:AGB92993.1}, fs(2)ltoRJ36 GN {ECO:0000313|EMBL:AGB92993.1}, VAS {ECO:0000313|EMBL:AGB92993.1}, Vas GN {ECO:0000313|EMBL:AGB92993.1}, VASA {ECO:0000313|EMBL:AGB92993.1}, GN Vasa {ECO:0000313|EMBL:AGB92993.1}; GN ORFNames=CG46283 {ECO:0000313|EMBL:AGB92993.1, GN ECO:0000313|FlyBase:FBgn0283442}, Dmel_CG46283 GN {ECO:0000313|EMBL:AGB92993.1}; 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:AGB92993.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AGB92993.1, 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:AGB92993.1, 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:AGB92993.1, 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:AGB92993.1, 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:AGB92993.1, 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:AGB92993.1, 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:AGB92993.1} 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:ALI30207.1} RP NUCLEOTIDE SEQUENCE. RA O'Boyle S.T.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:AGB92993.1} 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 [10] {ECO:0000313|EMBL:AGB92993.1, 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 [11] {ECO:0000313|EMBL:AGB92993.1, 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 [12] {ECO:0000313|EMBL:AGB92993.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109357; DOI=.1534/g3.115.018929; RG FlyBase Consortium; RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., RA St Pierre S.E., Gramates L.S., Zhou P., Schroeder A.J., Falls K., RA Strelets V., Russo S.M., Gelbart W.M.; RT "Gene Model Annotations for Drosophila melanogaster: Impact of High- RT Throughput Data."; RL G3 (Bethesda) 5:1721-1736(2015). RN [13] {ECO:0000313|EMBL:AGB92993.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109356; DOI=.1534/g3.115.018937; RG FlyBase Consortium; RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., RA St Pierre S.E., Zhou P., Schroeder A.J., Falls K., Emmert D.B., RA Russo S.M., Gelbart W.M.; RT "Gene Model Annotations for Drosophila melanogaster: The Rule- RT Benders."; RL G3 (Bethesda) 5:1737-1749(2015). RN [14] {ECO:0000313|EMBL:AGB92993.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000256|RuleBase:RU000492}. 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; AE014134; AGB92993.1; -; Genomic_DNA. DR EMBL; AE014134; ALI30207.1; -; Genomic_DNA. DR RefSeq; NP_001260458.1; NM_001273529.2. DR RefSeq; NP_001303322.1; NM_001316393.1. DR RefSeq; NP_723899.1; NM_165103.3. DR UniGene; Dm.4715; -. DR EnsemblMetazoa; FBtr0445185; FBpp0401445; FBgn0283442. DR EnsemblMetazoa; FBtr0445186; FBpp0401446; FBgn0283442. DR EnsemblMetazoa; FBtr0445187; FBpp0401447; FBgn0283442. DR GeneID; 26067080; -. DR KEGG; dme:Dmel_CG46283; -. DR CTD; 26067080; -. DR FlyBase; FBgn0283442; vas. DR KO; K13982; -. DR OMA; PMYNQLR; -. DR OrthoDB; 595675at2759; -. DR ChiTaRS; vas; fly. DR GenomeRNAi; 26067080; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0262526; Expressed in 10 organ(s), highest expression level in egg chamber. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:FlyBase. DR GO; GO:0043186; C:P granule; IDA:FlyBase. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase. DR GO; GO:0045495; C:pole plasm; IDA:FlyBase. DR GO; GO:0045170; C:spectrosome; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-EC. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IDA:FlyBase. DR GO; GO:0003724; F:RNA helicase activity; TAS:FlyBase. DR GO; GO:0046843; P:dorsal appendage formation; HMP:FlyBase. DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase. DR GO; GO:0008298; P:intracellular mRNA localization; TAS:FlyBase. DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase. DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; NAS:FlyBase. DR GO; GO:0030717; P:oocyte karyosome formation; NAS:FlyBase. DR GO; GO:0048477; P:oogenesis; HMP:FlyBase. DR GO; GO:0007315; P:pole plasm assembly; IMP:FlyBase. DR GO; GO:0007316; P:pole plasm RNA localization; IMP:FlyBase. DR GO; GO:0046012; P:positive regulation of oskar mRNA translation; NAS:FlyBase. DR GO; GO:0045727; P:positive regulation of translation; IMP:FlyBase. DR GO; GO:0008104; P:protein localization; IMP:FlyBase. DR GO; GO:0046011; P:regulation of oskar mRNA translation; TAS:FlyBase. DR GO; GO:0006417; P:regulation of translation; TAS:FlyBase. DR CDD; cd00079; HELICc; 1. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU000492}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Helicase {ECO:0000256|RuleBase:RU000492}; KW Hydrolase {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AGB92993.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000492}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AGB92993.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Transferase {ECO:0000313|EMBL:AGB92993.1}. FT DOMAIN 245 273 Q_MOTIF. {ECO:0000259|PROSITE:PS51195}. FT DOMAIN 276 453 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 477 624 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT MOTIF 245 273 Q motif. {ECO:0000256|PROSITE-ProRule: FT PRU00552}. SQ SEQUENCE 661 AA; 72331 MW; 8617C25CCB3130B9 CRC64; MSDDWDDEPI VDTRGARGGD WSDDEDTAKS FSGEAEGDGV GGSGGEGGGY QGGNRDVFGR IGGGRGGGAG GYRGGNRDGG GFHGGRREGE RDFRGGEGGF RGGQGGSRGG QGGSRGGQGG FRGGEGGFRG RLYENEDGDE RRGRLDREER GGERRGRLDR EERGGERGER GDGGFARRRR NEDDINNNNN IVEDVERKRE FYIPPEPSND AIEIFSSGIA SGIHFSKYNN IPVKVTGSDV PQPIQHFTSA DLRDIIIDNV NKSGYKIPTP IQKCSIPVIS SGRDLMACAQ TGSGKTAAFL LPILSKLLED PHELELGRPQ VVIVSPTREL AIQIFNEARK FAFESYLKIG IVYGGTSFRH QNECITRGCH VVIATPGRLL DFVDRTFITF EDTRFVVLDE ADRMLDMGFS EDMRRIMTHV TMRPEHQTLM FSATFPEEIQ RMAGEFLKNY VFVAIGIVGG ACSDVKQTIY EVNKYAKRSK LIEILSEQAD GTIVFVETKR GADFLASFLS EKEFPTTSIH GDRLQSQREQ ALRDFKNGSM KVLIATSVAS RGLDIKNIKH VINYDMPSKI DDYVHRIGRT GRVGNNGRAT SFFDPEKDRA IAADLVKILE GSGQTVPDFL RTCGAGGDGG YSNQNFGGVD VRGRGNYVGD ATNVEEEEQW D //