Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9VCU9 (DCR1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoribonuclease Dcr-1

Short name=Protein dicer-1
EC=3.1.26.-
Gene names
Name:Dcr-1
ORF Names:CG4792
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length2249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for RNA interference (RNAi); double-stranded RNA (dsRNA) induces potent and specific gene silencing. 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. May carry out the initiation step of RNAi by cleaving dsRNA to produce 22 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs. During embryogenesis, involved in germline fate determination. Ref.4 Ref.5 Ref.7

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Interacts with AGO2 to form components of the RISC. Interacts with Fmr1 to form a ribonucleoprotein (RNP) complex involved in translation regulation, other components of the complex are mRpL5, mRpL11, AGO2 and Rm62. Interacts with piwi and vas; these interactions occur in the polar granules. Ref.5 Ref.6 Ref.7

Sequence similarities

Belongs to the helicase family. Dicer subfamily.

Contains 1 Dicer dsRNA-binding fold domain.

Contains 1 DRBM (double-stranded RNA-binding) domain.

Contains 1 helicase C-terminal domain.

Contains 1 PAZ domain.

Contains 2 RNase III domains.

Sequence caution

The sequence AAK84929.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processRNA-mediated gene silencing
   DomainRepeat
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionEndonuclease
Helicase
Hydrolase
Nuclease
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA interference

Inferred from direct assay PubMed 15066284. Source: FlyBase

RNA phosphodiester bond hydrolysis

Inferred from direct assay Ref.4PubMed 11889553. Source: GOC

RNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay Ref.4PubMed 11889553. Source: GOC

dendrite morphogenesis

Inferred from mutant phenotype PubMed 19013069. Source: FlyBase

dsRNA transport

Inferred from mutant phenotype PubMed 16862146. Source: FlyBase

germ-line stem cell division

Inferred from mutant phenotype PubMed 15944714. Source: FlyBase

germarium-derived female germ-line cyst formation

Inferred from mutant phenotype PubMed 22445511. Source: FlyBase

germarium-derived oocyte fate determination

Inferred from mutant phenotype PubMed 22445511. Source: FlyBase

mitotic cell cycle, embryonic

Inferred from mutant phenotype Ref.7. Source: FlyBase

pole cell formation

Inferred from mutant phenotype Ref.7. Source: FlyBase

pre-miRNA processing

Inferred from direct assay PubMed 17666393PubMed 21926993. Source: FlyBase

production of miRNAs involved in gene silencing by miRNA

Inferred from mutant phenotype PubMed 15066283. Source: FlyBase

production of siRNA involved in RNA interference

Inferred from direct assay Ref.6. Source: UniProtKB

segment polarity determination

Inferred from genetic interaction PubMed 16934003. Source: FlyBase

siRNA loading onto RISC involved in RNA interference

Inferred from mutant phenotype PubMed 15066283. Source: FlyBase

   Cellular_componentRISC complex

Inferred from direct assay PubMed 15066284. Source: FlyBase

cytoplasm

Inferred from direct assay PubMed 15918769PubMed 16530043. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

bidentate ribonuclease III activity

Inferred from direct assay Ref.4. Source: FlyBase

double-stranded RNA binding

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

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pre-miRNA binding

Inferred from direct assay PubMed 21926993. Source: FlyBase

protein binding

Inferred from physical interaction Ref.5Ref.6. Source: UniProtKB

ribonuclease III activity

Inferred from direct assay PubMed 11889553. Source: MGI

single-stranded RNA binding

Inferred from direct assay PubMed 21926993. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

loqsQ9VJY93EBI-112170,EBI-638074

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22492249Endoribonuclease Dcr-1
PRO_0000180474

Regions

Domain485 – 648164Helicase C-terminal
Domain825 – 92096Dicer dsRNA-binding fold
Domain1099 – 1246148PAZ
Domain1698 – 1919222RNase III 1
Domain1993 – 2150158RNase III 2
Domain2175 – 224167DRBM
Nucleotide binding37 – 448ATP Potential

Sites

Metal binding20321Magnesium or manganese By similarity
Metal binding21361Magnesium or manganese By similarity
Metal binding21391Magnesium or manganese By similarity
Site21321Important for activity By similarity

Amino acid modifications

Modified residue14231Phosphoserine Ref.8
Modified residue18771Phosphoserine Ref.8
Modified residue18801Phosphoserine Ref.8

Experimental info

Sequence conflict1338 – 13392PT → AI Ref.3
Sequence conflict13451L → I Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9VCU9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D693F0432AC8033D

FASTA2,249255,330
        10         20         30         40         50         60 
MAFHWCDNNL HTTVFTPRDF QVELLATAYE RNTIICLGHR SSKEFIALKL LQELSRRARR 

        70         80         90        100        110        120 
HGRVSVYLSC EVGTSTEPCS IYTMLTHLTD LRVWQEQPDM QIPFDHCWTD YHVSILRPEG 

       130        140        150        160        170        180 
FLYLLETREL LLSSVELIVL EDCHDSAVYQ RIRPLFENHI MPAPPADRPR ILGLAGPLHS 

       190        200        210        220        230        240 
AGCELQQLSA MLATLEQSVL CQIETASDIV TVLRYCSRPH EYIVQCAPFE MDELSLVLAD 

       250        260        270        280        290        300 
VLNTHKSFLL DHRYDPYEIY GTDQFMDELK DIPDPKVDPL NVINSLLVVL HEMGPWCTQR 

       310        320        330        340        350        360 
AAHHFYQCNE KLKVKTPHER HYLLYCLVST ALIQLYSLCE HAFHRHLGSG SDSRQTIERY 

       370        380        390        400        410        420 
SSPKVRRLLQ TLRCFKPEEV HTQADGLRRM RHQVDQADFN RLSHTLESKC RMVDQMDQPP 

       430        440        450        460        470        480 
TETRALVATL EQILHTTEDR QTNRSAARVT PTPTPAHAKP KPSSGANTAQ PRTRRRVYTR 

       490        500        510        520        530        540 
RHHRDHNDGS DTLCALIYCN QNHTARVLFE LLAEISRRDP DLKFLRCQYT TDRVADPTTE 

       550        560        570        580        590        600 
PKEAELEHRR QEEVLKRFRM HDCNVLIGTS VLEEGIDVPK CNLVVRWDPP TTYRSYVQCK 

       610        620        630        640        650        660 
GRARAAPAYH VILVAPSYKS PTVGSVQLTD RSHRYICATG DTTEADSDSD DSAMPNSSGS 

       670        680        690        700        710        720 
DPYTFGTARG TVKILNPEVF SKQPPTACDI KLQEIQDELP AAAQLDTSNS SDEAVSMSNT 

       730        740        750        760        770        780 
SPSESSTEQK SRRFQCELSS LTEPEDTSDT TAEIDTAHSL ASTTKDLVHQ MAQYREIEQM 

       790        800        810        820        830        840 
LLSKCANTEP PEQEQSEAER FSACLAAYRP KPHLLTGASV DLGSAIALVN KYCARLPSDT 

       850        860        870        880        890        900 
FTKLTALWRC TRNERAGVTL FQYTLRLPIN SPLKHDIVGL PMPTQTLARR LAALQACVEL 

       910        920        930        940        950        960 
HRIGELDDQL QPIGKEGFRA LEPDWECFEL EPEDEQIVQL SDEPRPGTTK RRQYYYKRIA 

       970        980        990       1000       1010       1020 
SEFCDCRPVA GAPCYLYFIQ LTLQCPIPEE QNTRGRKIYP PEDAQQGFGI LTTKRIPKLS 

      1030       1040       1050       1060       1070       1080 
AFSIFTRSGE VKVSLELAKE RVILTSEQIV CINGFLNYTF TNVLRLQKFL MLFDPDSTEN 

      1090       1100       1110       1120       1130       1140 
CVFIVPTVKA PAGGKHIDWQ FLELIQANGN TMPRAVPDEE RQAQPFDPQR FQDAVVMPWY 

      1150       1160       1170       1180       1190       1200 
RNQDQPQYFY VAEICPHLSP LSCFPGDNYR TFKHYYLVKY GLTIQNTSQP LLDVDHTSAR 

      1210       1220       1230       1240       1250       1260 
LNFLTPRYVN RKGVALPTSS EETKRAKREN LEQKQILVPE LCTVHPFPAS LWRTAVCLPC 

      1270       1280       1290       1300       1310       1320 
ILYRINGLLL ADDIRKQVSA DLGLGRQQIE DEDFEWPMLD FGWSLSEVLK KSRESKQKES 

      1330       1340       1350       1360       1370       1380 
LKDDTINGKD LADVEKKPTS EETQLDKDSK DDKVEKSAIE LIIEGEEKLQ EADDFIEIGT 

      1390       1400       1410       1420       1430       1440 
WSNDMADDIA SFNQEDDDED DAFHLPVLPA NVKFCDQQTR YGSPTFWDVS NGESGFKGPK 

      1450       1460       1470       1480       1490       1500 
SSQNKQGGKG KAKGPAKPTF NYYDSDNSLG SSYDDDDNAG PLNYMHHNYS SDDDDVADDI 

      1510       1520       1530       1540       1550       1560 
DAGRIAFTSK NEAETIETAQ EVEKRQKQLS IIQATNANER QYQQTKNLLI GFNFKHEDQK 

      1570       1580       1590       1600       1610       1620 
EPATIRYEES IAKLKTEIES GGMLVPHDQQ LVLKRSDAAE AQVAKVSMME LLKQLLPYVN 

      1630       1640       1650       1660       1670       1680 
EDVLAKKLGD RRELLLSDLV ELNADWVARH EQETYNVMGC GDSFDNYNDH HRLNLDEKQL 

      1690       1700       1710       1720       1730       1740 
KLQYERIEIE PPTSTKAITS AILPAGFSFD RQPDLVGHPG PSPSIILQAL TMSNANDGIN 

      1750       1760       1770       1780       1790       1800 
LERLETIGDS FLKYAITTYL YITYENVHEG KLSHLRSKQV ANLNLYRLGR RKRLGEYMIA 

      1810       1820       1830       1840       1850       1860 
TKFEPHDNWL PPCYYVPKEL EKALIEAKIP THHWKLADLL DIKNLSSVQI CEMVREKADA 

      1870       1880       1890       1900       1910       1920 
LGLEQNGGAQ NGQLDDSNDS CNDFSCFIPY NLVSQHSIPD KSIADCVEAL IGAYLIECGP 

      1930       1940       1950       1960       1970       1980 
RGALLFMAWL GVRVLPITRQ LDGGNQEQRI PGSTKPNAEN VVTVYGAWPT PRSPLLHFAP 

      1990       2000       2010       2020       2030       2040 
NATEELDQLL SGFEEFEESL GYKFRDRSYL LQAMTHASYT PNRLTDCYQR LEFLGDAVLD 

      2050       2060       2070       2080       2090       2100 
YLITRHLYED PRQHSPGALT DLRSALVNNT IFASLAVRHG FHKFFRHLSP GLNDVIDRFV 

      2110       2120       2130       2140       2150       2160 
RIQQENGHCI SEEYYLLSEE ECDDAEDVEV PKALGDVFES IAGAIFLDSN MSLDVVWHVY 

      2170       2180       2190       2200       2210       2220 
SNMMSPEIEQ FSNSVPKSPI RELLELEPET AKFGKPEKLA DGRRVRVTVD VFCKGTFRGI 

      2230       2240 
GRNYRIAKCT AAKCALRQLK KQGLIAKKD 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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.
Strain: Berkeley.
[3]"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] OF 1338-2249.
Strain: Berkeley.
Tissue: Embryo.
[4]"Role for a bidentate ribonuclease in the initiation step of RNA interference."
Bernstein E., Caudy A.A., Hammond S.M., Hannon G.J.
Nature 409:363-366(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Argonaute2, a link between genetic and biochemical analyses of RNAi."
Hammond S.M., Boettcher S., Caudy A.A., Kobayashi R., Hannon G.J.
Science 293:1146-1150(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AGO2.
[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: INTERACTION WITH FMR1.
[7]"The role of PIWI and the miRNA machinery in Drosophila germline determination."
Megosh H.B., Cox D.N., Campbell C., Lin H.
Curr. Biol. 16:1884-1894(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PIWI AND VAS.
[8]"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-1423; SER-1877 AND SER-1880, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014297 Genomic DNA. Translation: AAF56056.1.
AY050230 mRNA. Translation: AAK84929.1. Different initiation.
RefSeqNP_524453.1. NM_079729.3.
UniGeneDm.1283.

3D structure databases

ProteinModelPortalQ9VCU9.
SMRQ9VCU9. Positions 549-615, 973-1266, 1981-2240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67642. 5 interactions.
DIPDIP-23028N.
IntActQ9VCU9. 4 interactions.
MINTMINT-923321.

Proteomic databases

PaxDbQ9VCU9.
PRIDEQ9VCU9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0084324; FBpp0083717; FBgn0039016.
GeneID42693.
KEGGdme:Dmel_CG4792.
UCSCCG4792-RA. d. melanogaster.

Organism-specific databases

CTD42693.
FlyBaseFBgn0039016. Dcr-1.

Phylogenomic databases

eggNOGCOG0571.
GeneTreeENSGT00510000046789.
InParanoidQ9VCU9.
KOK11592.
OMAKYAITTY.
OrthoDBEOG78PV82.
PhylomeDBQ9VCU9.

Gene expression databases

BgeeQ9VCU9.

Family and domain databases

Gene3D1.10.1520.10. 4 hits.
3.40.50.300. 1 hit.
InterProIPR005034. Dicer_dimerisation_dom.
IPR014720. dsRNA-bd_dom.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR003100. PAZ_dom.
IPR000999. RNase_III_dom.
[Graphical view]
PfamPF03368. Dicer_dimer. 1 hit.
PF00271. Helicase_C. 1 hit.
PF02170. PAZ. 1 hit.
PF00636. Ribonuclease_3. 2 hits.
[Graphical view]
SMARTSM00358. DSRM. 1 hit.
SM00490. HELICc. 1 hit.
SM00949. PAZ. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view]
SUPFAMSSF101690. SSF101690. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF69065. SSF69065. 4 hits.
PROSITEPS51327. DICER_DSRBF. 1 hit.
PS50137. DS_RBD. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50821. PAZ. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi42693.
NextBio830091.
PROQ9VCU9.

Entry information

Entry nameDCR1_DROME
AccessionPrimary (citable) accession number: Q9VCU9
Secondary accession number(s): Q961S7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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