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P19109

- DDX17_DROME

UniProt

P19109 - DDX17_DROME

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiP19109. differential.

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.
GeneTreeiENSGT00760000119219.
InParanoidiP19109.
KOiK12823.
OMAiCITQRRH.
OrthoDBiEOG7HTHGB.
PhylomeDBiP19109.

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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform A (identifier: P19109) [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

        10         20         30         40         50
MLKLVQYIAP RVGGATPRPT ACGWGNLLLI SPRSGASSEK CITQRRHFLF
60 70 80 90 100
SSASSSGTFA SSSSLCTEQR QQFHGSRRNR ETILFPSTYS SLQAQSQRAF
110 120 130 140 150
RDSSKPDSDD YVDSIPKAEQ RTRTRKSLFN DPDERTEEIK IEGVMAPHDR
160 170 180 190 200
DFGHSGRGGR GGDRGGDDRR GGGGGGNRFG GGGGGGDYHG IRNGRVEKRR
210 220 230 240 250
DDRGGGNRFG GGGGFGDRRG GGGGGSQDLP MRPVDFSNLA PFKKNFYQEH
260 270 280 290 300
PNVANRSPYE VQRYREEQEI TVRGQVPNPI QDFSEVHLPD YVMKEIRRQG
310 320 330 340 350
YKAPTAIQAQ GWPIAMSGSN FVGIAKTGSG KTLGYILPAI VHINNQQPLQ
360 370 380 390 400
RGDGPIALVL APTRELAQQI QQVATEFGSS SYVRNTCVFG GAPKGGQMRD
410 420 430 440 450
LQRGCEIVIA TPGRLIDFLS AGSTNLKRCT YLVLDEADRM LDMGFEPQIR
460 470 480 490 500
KIVSQIRPDR QTLMWSATWP KEVKQLAEDF LGNYIQINIG SLELSANHNI
510 520 530 540 550
RQVVDVCDEF SKEEKLKTLL SDIYDTSESP GKIIIFVETK RRVDNLVRFI
560 570 580 590 600
RSFGVRCGAI HGDKSQSERD FVLREFRSGK SNILVATDVA ARGLDVDGIK
610 620 630 640 650
YVINFDYPQN SEDYIHRIGR TGRSNTKGTS FAFFTKNNAK QAKALVDVLR
660 670 680 690 700
EANQEINPAL ENLARNSRYD GGGGRSRYGG GGGGGRFGGG GFKKGSLSNG
710
RGFGGGGGGG GEGRHSRFD

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_169121.2. [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_169121.2. [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 ENSGT00760000119219.
InParanoidi P19109.
KOi K12823.
OMAi CITQRRH.
OrthoDBi EOG7HTHGB.
PhylomeDBi P19109.

Miscellaneous databases

GenomeRNAii 40739.
NextBioi 820339.
PROi P19109.

Gene expression databases

Bgeei P19109.
ExpressionAtlasi P19109. differential.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. 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 ]
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

« Hide 'large scale' publications
  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 29, 2014
This is version 147 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