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Protein

ATP-dependent RNA helicase bel

Gene

bel

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent RNA helicase that is essential and required for cellular function, larval growth, and for male and female fertility. Also required for RNA interference (RNAi), double-stranded RNA induces potent and specific gene silencing, by acting downstream of dsRNA internalization. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys or silences messenger RNAs homologous to the silencing trigger.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi315 – 3228ATPPROSITE-ProRule annotation
Nucleotide bindingi339 – 3468ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: UniProtKB
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • ecdysone-mediated induction of salivary gland cell autophagic cell death Source: FlyBase
  • instar larval development Source: FlyBase
  • mitotic sister chromatid segregation Source: FlyBase
  • oogenesis Source: FlyBase
  • regulation of gene expression Source: FlyBase
  • RNA interference Source: UniProtKB
  • spermatid development Source: FlyBase
  • spermatogenesis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Helicase, Hydrolase

Keywords - Biological processi

Differentiation, Oogenesis, RNA-mediated gene silencing, Spermatogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase bel (EC:3.6.4.13)
Alternative name(s):
Protein belle
Gene namesi
Name:belImported
ORF Names:CG9748
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0263231. bel.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: In nurse cells, follicle cells, and within the oocyte. Vas and bel colocalize in the perinuclear region of nurse cells.

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • cytosol Source: FlyBase
  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • neuronal cell body Source: FlyBase
  • P granule Source: UniProtKB
  • RISC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Flies are recessive lethal with a larval growth defect phenotype. Hypomorphic bel mutants are male-sterile due to defects in spermatogenesis and female sterile as oogenesis usually arrests around stages 8-9 and egg chambers completely degenerate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 798798ATP-dependent RNA helicase belPRO_0000270580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei177 – 1771Phosphoserine1 Publication
Modified residuei179 – 1791Phosphoserine1 Publication
Modified residuei214 – 2141Phosphoserine1 Publication
Modified residuei219 – 2191Phosphoserine1 Publication
Modified residuei638 – 6381Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VHP0.
PRIDEiQ9VHP0.

PTM databases

iPTMnetiQ9VHP0.

Expressioni

Tissue specificityi

Vas and bel colocalize in nuage (perinuclear, electron-dense granules in germline cells) and at the oocyte posterior during oogenesis.1 Publication

Developmental stagei

Expressed throughout development, highest expression in second larval instar and adult females.1 Publication

Gene expression databases

BgeeiQ9VHP0.
ExpressionAtlasiQ9VHP0. differential.
GenevisibleiQ9VHP0. DM.

Interactioni

Protein-protein interaction databases

IntActiQ9VHP0. 26 interactions.
STRINGi7227.FBpp0081374.

Structurei

3D structure databases

ProteinModelPortaliQ9VHP0.
SMRiQ9VHP0. Positions 250-693.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini326 – 515190Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini542 – 693152Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi295 – 32329Q motifSequence analysisAdd
BLAST
Motifi459 – 4624DEAD boxSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 246238Gly-richSequence analysisAdd
BLAST
Compositional biasi697 – 78488Gly-richSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the DEAD box helicase family. DDX3/DED1 subfamily.Sequence analysis
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0335. Eukaryota.
ENOG410XNTI. LUCA.
GeneTreeiENSGT00770000120531.
InParanoidiQ9VHP0.
KOiK11594.
OMAiNAPDWWA.
OrthoDBiEOG7B5WV8.
PhylomeDBiQ9VHP0.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]

Sequencei

Sequence statusi: Complete.

Q9VHP0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNAINQNGT GLEQQVAGLD LNGGSADYSG PITSKTSTNS VTGGVYVPPH
60 70 80 90 100
LRGGGGNNNA ADAESQGQGQ GQGQGFDSRS GNPRQETRDP QQSRGGGGEY
110 120 130 140 150
RRGGGGGGRG FNRQSGDYGY GSGGGGRRGG GGRFEDNYNG GEFDSRRGGD
160 170 180 190 200
WNRSGGGGGG GRGFGRGPSY RGGGGGSGSN LNEQTAEDGQ AQQQQQPRND
210 220 230 240 250
RWQEPERPAG FDGSEGGQSA GGNRSYNNRG ERGGGGYNSR WKEGGGSNVD
260 270 280 290 300
YTKLGARDER LEVELFGVGN TGINFDKYED IPVEATGQNV PPNITSFDDV
310 320 330 340 350
QLTEIIRNNV ALARYDKPTP VQKHAIPIII NGRDLMACAQ TGSGKTAAFL
360 370 380 390 400
VPILNQMYEL GHVPPPQSTR QYSRRKQYPL GLVLAPTREL ATQIFEEAKK
410 420 430 440 450
FAYRSRMRPA VLYGGNNTSE QMRELDRGCH LIVATPGRLE DMITRGKVGL
460 470 480 490 500
ENIRFLVLDE ADRMLDMGFE PQIRRIVEQL NMPPTGQRQT LMFSATFPKQ
510 520 530 540 550
IQELASDFLS NYIFLAVGRV GSTSENITQT ILWVYEPDKR SYLLDLLSSI
560 570 580 590 600
RDGPEYTKDS LTLIFVETKK GADSLEEFLY QCNHPVTSIH GDRTQKEREE
610 620 630 640 650
ALRCFRSGDC PILVATAVAA RGLDIPHVKH VINFDLPSDV EEYVHRIGRT
660 670 680 690 700
GRMGNLGVAT SFFNEKNRNI CSDLLELLIE TKQEIPSFME DMSSDRGHGG
710 720 730 740 750
AKRAGRGGGG RYGGGFGSRD YRQSSGGGGG GRSGPPPRSG GSGSGGGGGS
760 770 780 790
YRSNGNSYGG NSGGGGYYGG GAGGGSYGGS YGGGSASHSS NAPDWWAQ
Length:798
Mass (Da):85,081
Last modified:May 1, 2000 - v1
Checksum:i516A9C8BEF8F8017
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti513 – 5131I → T in AAL90351 (PubMed:12537569).Curated
Sequence conflicti709 – 7091G → S in AAL90351 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF54262.1.
AY089613 mRNA. Translation: AAL90351.1.
RefSeqiNP_536783.1. NM_080522.4.
UniGeneiDm.7823.

Genome annotation databases

EnsemblMetazoaiFBtr0081888; FBpp0081374; FBgn0263231.
GeneIDi45826.
KEGGidme:Dmel_CG9748.
UCSCiCG9748-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF54262.1.
AY089613 mRNA. Translation: AAL90351.1.
RefSeqiNP_536783.1. NM_080522.4.
UniGeneiDm.7823.

3D structure databases

ProteinModelPortaliQ9VHP0.
SMRiQ9VHP0. Positions 250-693.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9VHP0. 26 interactions.
STRINGi7227.FBpp0081374.

PTM databases

iPTMnetiQ9VHP0.

Proteomic databases

PaxDbiQ9VHP0.
PRIDEiQ9VHP0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081888; FBpp0081374; FBgn0263231.
GeneIDi45826.
KEGGidme:Dmel_CG9748.
UCSCiCG9748-RA. d. melanogaster.

Organism-specific databases

CTDi100035747.
FlyBaseiFBgn0263231. bel.

Phylogenomic databases

eggNOGiKOG0335. Eukaryota.
ENOG410XNTI. LUCA.
GeneTreeiENSGT00770000120531.
InParanoidiQ9VHP0.
KOiK11594.
OMAiNAPDWWA.
OrthoDBiEOG7B5WV8.
PhylomeDBiQ9VHP0.

Miscellaneous databases

GenomeRNAii45826.
PROiQ9VHP0.

Gene expression databases

BgeeiQ9VHP0.
ExpressionAtlasiQ9VHP0. differential.
GenevisibleiQ9VHP0. DM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Belle is a Drosophila DEAD-box protein required for viability and in the germ line."
    Johnstone O., Deuring R., Bock R., Linder P., Fuller M.T., Lasko P.
    Dev. Biol. 277:92-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  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: BerkeleyImported.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BerkeleyImported.
    Tissue: Embryo1 Publication.
  5. "Double-stranded RNA is internalized by scavenger receptor-mediated endocytosis in Drosophila S2 cells."
    Ulvila J., Parikka M., Kleino A., Sormunen R., Ezekowitz R.A., Kocks C., Ramet M.
    J. Biol. Chem. 281:14370-14375(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-179; SER-214; SER-219 AND SER-638, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiDDX3_DROME
AccessioniPrimary (citable) accession number: Q9VHP0
Secondary accession number(s): Q8SXI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 124 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.