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P19109 (DDX17_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent RNA helicase p62
EC=3.6.4.13
Gene names
Name:Rm62
Synonyms:Dmp68, p62
ORF Names:CG10279
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length719 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.6

Subcellular location

Nucleus Potential.

Sequence similarities

Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processRNA-mediated gene silencing
Translation regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA interference

Inferred from mutant phenotype Ref.6. Source: FlyBase

antimicrobial humoral response

Inferred from mutant phenotype PubMed 16163390. Source: FlyBase

mRNA splicing, via spliceosome

Inferred by curator PubMed 18981222. Source: FlyBase

neurogenesis

Inferred from mutant phenotype PubMed 21549331. Source: FlyBase

regulation of alternative mRNA splicing, via spliceosome

Inferred from mutant phenotype PubMed 15492211. Source: FlyBase

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay PubMed 18981222. Source: FlyBase

microtubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

polytene chromosome puff

Inferred from direct assay PubMed 16598038. Source: FlyBase

precatalytic spliceosome

Inferred from direct assay PubMed 18981222. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

mRNA binding

Inferred from sequence or structural similarity PubMed 10908586. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Fmr1Q9NFU04EBI-200734,EBI-422631

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P19109-1)

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.
Note: No experimental confirmation available.
Isoform C (identifier: P19109-2)

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.
Isoform D (identifier: P19109-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-144: Missing.
Isoform E (identifier: P19109-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-141: Missing.
     142-145: EGVM → MRAK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 719719ATP-dependent RNA helicase p62
PRO_0000055007

Regions

Domain312 – 487176Helicase ATP-binding
Domain519 – 664146Helicase C-terminal
Nucleotide binding325 – 3328ATP By similarity
Motif281 – 30929Q motif
Motif435 – 4384DEAD box
Compositional bias153 – 22573Gly-rich
Compositional bias671 – 71343Gly-rich

Natural variations

Alternative sequence1 – 144144Missing in isoform D.
VSP_007414
Alternative sequence1 – 141141Missing in isoform C and isoform E.
VSP_007413
Alternative sequence142 – 1454EGVM → MRAK in isoform E.
VSP_007416
Alternative sequence142 – 1443EGV → MMM in isoform C.
VSP_007415

Experimental info

Sequence conflict1951R → A in CAA37037. Ref.1
Sequence conflict6751R → P in CAA37037. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified May 16, 2003. Version 3.
Checksum: A70A071A920B24FC

FASTA71978,548
        10         20         30         40         50         60 
MLKLVQYIAP RVGGATPRPT ACGWGNLLLI SPRSGASSEK CITQRRHFLF SSASSSGTFA 

        70         80         90        100        110        120 
SSSSLCTEQR QQFHGSRRNR ETILFPSTYS SLQAQSQRAF RDSSKPDSDD YVDSIPKAEQ 

       130        140        150        160        170        180 
RTRTRKSLFN DPDERTEEIK IEGVMAPHDR DFGHSGRGGR GGDRGGDDRR GGGGGGNRFG 

       190        200        210        220        230        240 
GGGGGGDYHG IRNGRVEKRR DDRGGGNRFG GGGGFGDRRG GGGGGSQDLP MRPVDFSNLA 

       250        260        270        280        290        300 
PFKKNFYQEH PNVANRSPYE VQRYREEQEI TVRGQVPNPI QDFSEVHLPD YVMKEIRRQG 

       310        320        330        340        350        360 
YKAPTAIQAQ GWPIAMSGSN FVGIAKTGSG KTLGYILPAI VHINNQQPLQ RGDGPIALVL 

       370        380        390        400        410        420 
APTRELAQQI QQVATEFGSS SYVRNTCVFG GAPKGGQMRD LQRGCEIVIA TPGRLIDFLS 

       430        440        450        460        470        480 
AGSTNLKRCT YLVLDEADRM LDMGFEPQIR KIVSQIRPDR QTLMWSATWP KEVKQLAEDF 

       490        500        510        520        530        540 
LGNYIQINIG SLELSANHNI RQVVDVCDEF SKEEKLKTLL SDIYDTSESP GKIIIFVETK 

       550        560        570        580        590        600 
RRVDNLVRFI RSFGVRCGAI HGDKSQSERD FVLREFRSGK SNILVATDVA ARGLDVDGIK 

       610        620        630        640        650        660 
YVINFDYPQN SEDYIHRIGR TGRSNTKGTS FAFFTKNNAK QAKALVDVLR EANQEINPAL 

       670        680        690        700        710 
ENLARNSRYD GGGGRSRYGG GGGGGRFGGG GFKKGSLSNG RGFGGGGGGG GEGRHSRFD

« Hide

Isoform C (B) (F) [UniParc].

Checksum: 2A948C1A9D7ED561
Show »

FASTA57862,867
Isoform D [UniParc].

Checksum: 77007C1A9D6E51E9
Show »

FASTA57562,474
Isoform E [UniParc].

Checksum: 7B4A17CFD243D0E9
Show »

FASTA57862,829

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
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] (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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIRS11485.
RefSeqNP_001163528.1. NM_001170057.1.
NP_001189182.1. NM_001202253.2.
NP_524243.2. NM_079519.2.
NP_731031.1. NM_169118.1.
NP_731032.1. NM_169119.3.
NP_731033.1. NM_169120.1.
NP_731034.1. NM_169121.1.
NP_731035.2. NM_169122.1.
UniGeneDm.1520.

3D structure databases

ProteinModelPortalP19109.
SMRP19109. Positions 260-669.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-17867N.
IntActP19109. 5 interactions.
MINTMINT-301207.

Proteomic databases

PaxDbP19109.
PRIDEP19109.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0078652; FBpp0078301; FBgn0003261.
GeneID40739.
KEGGdme:Dmel_CG10279.

Organism-specific databases

CTD40739.
FlyBaseFBgn0003261. Rm62.

Phylogenomic databases

eggNOGCOG0513.
GeneTreeENSGT00660000095174.
InParanoidP19109.
KOK12823.
OMAHISNQPR.
OrthoDBEOG4QBZMP.
PhylomeDBP19109.

Gene expression databases

BgeeP19109.
GermOnlineCG10279. Drosophila melanogaster.

Family and domain databases

InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi40739.
NextBio820339.

Entry information

Entry nameDDX17_DROME
AccessionPrimary (citable) accession number: P19109
Secondary accession number(s): A4V2H1 expand/collapse secondary AC list , Q6AWN9, Q8IGL7, Q95TB8, Q9I7P5, Q9VNK4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 16, 2003
Last modified: May 1, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents