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P19109

- DDX17_DROME

UniProt

P19109 - DDX17_DROME

Protein

ATP-dependent RNA helicase p62

Gene

Rm62

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (16 May 2003)
      Previous versions | rss
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    Functioni

    Involved in RNA interference (RNAi); double-stranded RNA induces potent and specific gene silencing. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys messenger RNAs homologous to the silencing trigger.1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi325 – 3328ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. mRNA binding Source: FlyBase
    4. protein binding Source: IntAct

    GO - Biological processi

    1. antimicrobial humoral response Source: FlyBase
    2. mRNA splicing, via spliceosome Source: FlyBase
    3. neurogenesis Source: FlyBase
    4. regulation of alternative mRNA splicing, via spliceosome Source: FlyBase
    5. regulation of translation Source: UniProtKB-KW
    6. RNA interference Source: FlyBase

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    RNA-mediated gene silencing, Translation regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent RNA helicase p62 (EC:3.6.4.13)
    Gene namesi
    Name:Rm62
    Synonyms:Dmp68, p62
    ORF Names:CG10279
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0003261. Rm62.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: FlyBase
    2. microtubule associated complex Source: FlyBase
    3. nucleus Source: FlyBase
    4. polytene chromosome Source: FlyBase
    5. polytene chromosome puff Source: FlyBase
    6. precatalytic spliceosome Source: FlyBase

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 719719ATP-dependent RNA helicase p62PRO_0000055007Add
    BLAST

    Proteomic databases

    PaxDbiP19109.
    PRIDEiP19109.

    Expressioni

    Gene expression databases

    BgeeiP19109.

    Interactioni

    Subunit structurei

    Interacts with Fmr1 to form a ribonucleoprotein (RNP) complex involved in translation regulation, other components of the complex are mRpL5, mRpL11, AGO2 and Dcr-1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Fmr1Q9NFU04EBI-200734,EBI-422631

    Protein-protein interaction databases

    BioGridi65943. 24 interactions.
    DIPiDIP-17867N.
    IntActiP19109. 5 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP19109.
    SMRiP19109. Positions 239-669.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini312 – 487176Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini519 – 664146Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi281 – 30929Q motifAdd
    BLAST
    Motifi435 – 4384DEAD box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi153 – 22573Gly-richAdd
    BLAST
    Compositional biasi671 – 71343Gly-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0513.
    GeneTreeiENSGT00750000117262.
    InParanoidiP19109.
    KOiK12823.
    OMAiCITQRRH.
    OrthoDBiEOG7HTHGB.
    PhylomeDBiP19109.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: P19109-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLKLVQYIAP RVGGATPRPT ACGWGNLLLI SPRSGASSEK CITQRRHFLF    50
    SSASSSGTFA SSSSLCTEQR QQFHGSRRNR ETILFPSTYS SLQAQSQRAF 100
    RDSSKPDSDD YVDSIPKAEQ RTRTRKSLFN DPDERTEEIK IEGVMAPHDR 150
    DFGHSGRGGR GGDRGGDDRR GGGGGGNRFG GGGGGGDYHG IRNGRVEKRR 200
    DDRGGGNRFG GGGGFGDRRG GGGGGSQDLP MRPVDFSNLA PFKKNFYQEH 250
    PNVANRSPYE VQRYREEQEI TVRGQVPNPI QDFSEVHLPD YVMKEIRRQG 300
    YKAPTAIQAQ GWPIAMSGSN FVGIAKTGSG KTLGYILPAI VHINNQQPLQ 350
    RGDGPIALVL APTRELAQQI QQVATEFGSS SYVRNTCVFG GAPKGGQMRD 400
    LQRGCEIVIA TPGRLIDFLS AGSTNLKRCT YLVLDEADRM LDMGFEPQIR 450
    KIVSQIRPDR QTLMWSATWP KEVKQLAEDF LGNYIQINIG SLELSANHNI 500
    RQVVDVCDEF SKEEKLKTLL SDIYDTSESP GKIIIFVETK RRVDNLVRFI 550
    RSFGVRCGAI HGDKSQSERD FVLREFRSGK SNILVATDVA ARGLDVDGIK 600
    YVINFDYPQN SEDYIHRIGR TGRSNTKGTS FAFFTKNNAK QAKALVDVLR 650
    EANQEINPAL ENLARNSRYD GGGGRSRYGG GGGGGRFGGG GFKKGSLSNG 700
    RGFGGGGGGG GEGRHSRFD 719

    Note: No experimental confirmation available.

    Length:719
    Mass (Da):78,548
    Last modified:May 16, 2003 - v3
    Checksum:iA70A071A920B24FC
    GO
    Isoform C (identifier: P19109-2) [UniParc]FASTAAdd to Basket

    Also known as: B, F

    The sequence of this isoform differs from the canonical sequence as follows:
         1-141: Missing.
         142-144: EGV → MMM

    Note: No experimental confirmation available.

    Show »
    Length:578
    Mass (Da):62,867
    Checksum:i2A948C1A9D7ED561
    GO
    Isoform D (identifier: P19109-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-144: Missing.

    Show »
    Length:575
    Mass (Da):62,474
    Checksum:i77007C1A9D6E51E9
    GO
    Isoform E (identifier: P19109-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-141: Missing.
         142-145: EGVM → MRAK

    Note: No experimental confirmation available.

    Show »
    Length:578
    Mass (Da):62,829
    Checksum:i7B4A17CFD243D0E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti195 – 1951R → A in CAA37037. (PubMed:2170937)Curated
    Sequence conflicti675 – 6751R → P in CAA37037. (PubMed:2170937)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 144144Missing in isoform D. 2 PublicationsVSP_007414Add
    BLAST
    Alternative sequencei1 – 141141Missing in isoform C and isoform E. 1 PublicationVSP_007413Add
    BLAST
    Alternative sequencei142 – 1454EGVM → MRAK in isoform E. CuratedVSP_007416
    Alternative sequencei142 – 1443EGV → MMM in isoform C. 1 PublicationVSP_007415

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52846 mRNA. Translation: CAA37037.1.
    AE014297 Genomic DNA. Translation: AAF51926.2.
    AE014297 Genomic DNA. Translation: AAF51927.2.
    AE014297 Genomic DNA. Translation: AAG22212.1.
    AE014297 Genomic DNA. Translation: AAG22213.2.
    AE014297 Genomic DNA. Translation: AAN14331.1.
    AE014297 Genomic DNA. Translation: AAN14332.1.
    BT001716 mRNA. Translation: AAN71471.1.
    BT011476 mRNA. Translation: AAR99134.1.
    BT015209 mRNA. Translation: AAT94438.1.
    PIRiS11485.
    RefSeqiNP_001163528.1. NM_001170057.1. [P19109-3]
    NP_001189182.1. NM_001202253.2. [P19109-4]
    NP_524243.2. NM_079519.2. [P19109-1]
    NP_731031.1. NM_169118.1. [P19109-3]
    NP_731032.1. NM_169119.3. [P19109-4]
    NP_731033.1. NM_169120.1. [P19109-2]
    NP_731034.1. NM_169121.1. [P19109-2]
    NP_731035.2. NM_169122.1. [P19109-2]
    UniGeneiDm.1520.

    Genome annotation databases

    EnsemblMetazoaiFBtr0078652; FBpp0078301; FBgn0003261. [P19109-1]
    GeneIDi40739.
    KEGGidme:Dmel_CG10279.
    UCSCiCG10279-RC. d. melanogaster.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52846 mRNA. Translation: CAA37037.1 .
    AE014297 Genomic DNA. Translation: AAF51926.2 .
    AE014297 Genomic DNA. Translation: AAF51927.2 .
    AE014297 Genomic DNA. Translation: AAG22212.1 .
    AE014297 Genomic DNA. Translation: AAG22213.2 .
    AE014297 Genomic DNA. Translation: AAN14331.1 .
    AE014297 Genomic DNA. Translation: AAN14332.1 .
    BT001716 mRNA. Translation: AAN71471.1 .
    BT011476 mRNA. Translation: AAR99134.1 .
    BT015209 mRNA. Translation: AAT94438.1 .
    PIRi S11485.
    RefSeqi NP_001163528.1. NM_001170057.1. [P19109-3 ]
    NP_001189182.1. NM_001202253.2. [P19109-4 ]
    NP_524243.2. NM_079519.2. [P19109-1 ]
    NP_731031.1. NM_169118.1. [P19109-3 ]
    NP_731032.1. NM_169119.3. [P19109-4 ]
    NP_731033.1. NM_169120.1. [P19109-2 ]
    NP_731034.1. NM_169121.1. [P19109-2 ]
    NP_731035.2. NM_169122.1. [P19109-2 ]
    UniGenei Dm.1520.

    3D structure databases

    ProteinModelPortali P19109.
    SMRi P19109. Positions 239-669.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65943. 24 interactions.
    DIPi DIP-17867N.
    IntActi P19109. 5 interactions.

    Proteomic databases

    PaxDbi P19109.
    PRIDEi P19109.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0078652 ; FBpp0078301 ; FBgn0003261 . [P19109-1 ]
    GeneIDi 40739.
    KEGGi dme:Dmel_CG10279.
    UCSCi CG10279-RC. d. melanogaster.

    Organism-specific databases

    CTDi 40739.
    FlyBasei FBgn0003261. Rm62.

    Phylogenomic databases

    eggNOGi COG0513.
    GeneTreei ENSGT00750000117262.
    InParanoidi P19109.
    KOi K12823.
    OMAi CITQRRH.
    OrthoDBi EOG7HTHGB.
    PhylomeDBi P19109.

    Miscellaneous databases

    GenomeRNAii 40739.
    NextBioi 820339.
    PROi P19109.

    Gene expression databases

    Bgeei P19109.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel RNA helicase gene tightly linked to the Triplo-lethal locus of Drosophila."
      Dorer D.R., Christensen A.C., Johnson D.H.
      Nucleic Acids Res. 18:5489-5494(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
      Tissue: Embryo.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
      Strain: Berkeley.
      Tissue: Embryo.
    5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND D).
      Strain: Berkeley.
      Tissue: Embryo.
    6. "A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins."
      Ishizuka A., Siomi M.C., Siomi H.
      Genes Dev. 16:2497-2508(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FMR1.

    Entry informationi

    Entry nameiDDX17_DROME
    AccessioniPrimary (citable) accession number: P19109
    Secondary accession number(s): A4V2H1
    , Q6AWN9, Q8IGL7, Q95TB8, Q9I7P5, Q9VNK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: May 16, 2003
    Last modified: October 1, 2014
    This is version 146 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3