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Reviewed, UniProtKB/Swiss-Prot Q9V3C0 (DDX41_DROME)

Last modified November 24, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP-dependent RNA helicase abstrakt
      Short name=DEAD box protein abstrakt
    EC=3.6.1.-
Gene names
Name: abs
ORF Names: CG14637
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

ATP-dependent RNA helicase. Is essential for the directed and fasciculated early outgrowth of the bolwig nerves, as well as for its navigation at later stages. Is required during post-transcriptional gene expression. Plays a role during morphogenetic process, apoptosis and the establishment of cell polarity.

Subcellular location

Nucleus Potential.

Sequence similarities

Belongs to the DEAD box helicase family. DDX41 subfamily.

Contains 1 CCHC-type zinc finger.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Cellular componentNucleus
   DomainZinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9VB741EBI-134927,EBI-169306

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 619619ATP-dependent RNA helicase abstrakt
PRO_0000054974

Regions

Domain208 – 392185Helicase ATP-binding
Domain403 – 563161Helicase C-terminal
Nucleotide binding221 – 2288ATP By similarity
Zinc finger577 – 59418CCHC-type
Motif177 – 20529Q motif
Motif340 – 3434DEAD box

Amino acid modifications

Modified residue111Phosphoserine Ref.6
Modified residue131Phosphoserine Ref.6
Modified residue141Phosphoserine Ref.6
Modified residue561Phosphoserine Ref.6
Modified residue571Phosphoserine Ref.6
Modified residue581Phosphoserine Ref.6
Modified residue661Phosphoserine Ref.6

Natural variations

Natural variant2411E → K in allele 14B; temperature sensitive.
Natural variant4311V → M in allele 33B; temperature sensitive.

Experimental info

Sequence conflict51K → Q in AAF04040. Ref.2
Sequence conflict26 – 305Missing Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9V3C0-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F148D277A1FD0BEC

FASTA61969,488
        10         20         30         40         50         60 
MAHVKRYRRS SKSSEEGDLD NEDYVPYVPV KERKKQHMIK LGRIVQLVSE TAQPKSSSEN 

        70         80         90        100        110        120 
ENEDDSQGAH DVETWGRKYN ISLLDQHTEL KKIAEAKKLS AVEKQLREEE KIMESIAQQK 

       130        140        150        160        170        180 
ALMGVAELAK GIQYEQPIKT AWKPPRYIRE MSEEEREAVR HELRILVEGE TPSPPIRSFR 

       190        200        210        220        230        240 
EMKFPKGILN GLAAKGIKNP TPIQVQGLPT VLAGRDLIGI AFTGSGKTLV FVLPVIMFAL 

       250        260        270        280        290        300 
EQEYSLPFER NEGPYGLIIC PSRELAKQTH EIIQHYSKHL QACGMPEIRS CLAMGGLPVS 

       310        320        330        340        350        360 
EALDVISRGV HIVVATPGRL MDMLDKKILT LDMCRYLCMD EADRMIDMGF EEDVRTIFSF 

       370        380        390        400        410        420 
FKGQRQTLLF SATMPKKIQN FARSALVKPV TINVGRAGAA SMNVTQQVEY VKQEAKVVYL 

       430        440        450        460        470        480 
LDCLQKTAPP VLIFAEKKQD VDCIHEYLLL KGVEAVAIHG GKDQEERSRA VDAYRVGKKD 

       490        500        510        520        530        540 
VLVATDVASK GLDFPNVQHV INYDMPDDIE NYVHRIGRTG RSNTKGLATT LINKTTEQSV 

       550        560        570        580        590        600 
LLDLKHLLIE GKQEVPDFLD ELAPETEHQH LDLGDSHGCT YCGGLGHRIT ECPKLEAVQN 

       610 
KQASNIGRRD YLSNTAADY 

« Hide

References

« Hide 'large scale' references
[1]"The Drosophila gene abstrakt, required for visual system development, encodes a putative RNA helicase of the DEAD box protein family."
Schmucker D., Vorbrueggen G., Yeghiayan P., Fan H.Q., Jaeckle H., Gaul U.
Mech. Dev. 91:189-196(2000) [PubMed: 10704843] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Developmental and cell biological functions of the Drosophila DEAD-box protein abstrakt."
Irion U., Leptin M.
Curr. Biol. 9:1373-1381(1999) [PubMed: 10607561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS 14B AND 33B.
[3]"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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[5]"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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[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: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; SER-14; SER-56; SER-57; SER-58 AND SER-66, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF212866 mRNA. Translation: AAF19985.1.
AF187729 Genomic DNA. Translation: AAF04040.1.
AE014297 Genomic DNA. Translation: AAF52165.1.
AY051752 mRNA. Translation: AAK93176.1.
RefSeqNP_524220.1.
UniGeneDm.3300

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:21861N.
IntActQ9V3C0. 5 interactions.
STRINGQ9V3C0.

Proteomic databases

PRIDEQ9V3C0.

Genome annotation databases

EnsemblFBtr0078967; FBpp0078606; FBgn0015331; Drosophila melanogaster. [Genome view]
GeneID40530.
KEGGdme:Dmel_CG14637.
UCSCCG14637-RA. d. melanogaster.

Organism-specific databases

CTD40530.
FlyBaseFBgn0015331. abs.

Phylogenomic databases

HOGENOMQ9V3C0.
OMAMGFEEDV
OrthoDBEOG98WC7V

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-009859-MON.

Gene expression databases

BgeeQ9V3C0.
GermOnlineCG14637. Drosophila melanogaster.

Family and domain databases

InterProIPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR014014. RNA_helicase_DEAD_Q_motif.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]
PROSITEPS00039. DEAD_ATP_HELICASE. False negative.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio819209.

Entry information

Entry nameDDX41_DROME
AccessionPrimary (citable) accession number: Q9V3C0
Secondary accession number(s): Q9U6D0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: November 24, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents