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Q9VCU9

- DCR1_DROME

UniProt

Q9VCU9 - DCR1_DROME

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Protein

Endoribonuclease Dcr-1

Gene
Dcr-1, CG4792
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Cofactori

Magnesium or manganese By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi2032 – 20321Magnesium or manganese By similarity
Sitei2132 – 21321Important for activity By similarity
Metal bindingi2136 – 21361Magnesium or manganese By similarity
Metal bindingi2139 – 21391Magnesium or manganese By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi37 – 448ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. bidentate ribonuclease III activity Source: FlyBase
  3. double-stranded RNA binding Source: FlyBase
  4. helicase activity Source: UniProtKB-KW
  5. metal ion binding Source: UniProtKB-KW
  6. pre-miRNA binding Source: FlyBase
  7. protein binding Source: UniProtKB
  8. ribonuclease III activity Source: MGI
  9. single-stranded RNA binding Source: FlyBase

GO - Biological processi

  1. dendrite morphogenesis Source: FlyBase
  2. dsRNA transport Source: FlyBase
  3. germarium-derived female germ-line cyst formation Source: FlyBase
  4. germarium-derived oocyte fate determination Source: FlyBase
  5. germ-line stem cell division Source: FlyBase
  6. mitotic cell cycle, embryonic Source: FlyBase
  7. pole cell formation Source: FlyBase
  8. pre-miRNA processing Source: FlyBase
  9. production of miRNAs involved in gene silencing by miRNA Source: FlyBase
  10. production of siRNA involved in RNA interference Source: UniProtKB
  11. RNA interference Source: FlyBase
  12. RNA phosphodiester bond hydrolysis Source: GOC
  13. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  14. segment polarity determination Source: FlyBase
  15. siRNA loading onto RISC involved in RNA interference Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Helicase, Hydrolase, Nuclease

Keywords - Biological processi

RNA-mediated gene silencing

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_181252. Small interfering RNA (siRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoribonuclease Dcr-1 (EC:3.1.26.-)
Short name:
Protein dicer-1
Gene namesi
Name:Dcr-1
ORF Names:CG4792
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0039016. Dcr-1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. RISC complex Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22492249Endoribonuclease Dcr-1PRO_0000180474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1423 – 14231Phosphoserine1 Publication
Modified residuei1877 – 18771Phosphoserine1 Publication
Modified residuei1880 – 18801Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VCU9.
PRIDEiQ9VCU9.

Expressioni

Gene expression databases

BgeeiQ9VCU9.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
loqsQ9VJY93EBI-112170,EBI-638074

Protein-protein interaction databases

BioGridi67642. 5 interactions.
DIPiDIP-23028N.
IntActiQ9VCU9. 4 interactions.
MINTiMINT-923321.

Structurei

3D structure databases

ProteinModelPortaliQ9VCU9.
SMRiQ9VCU9. Positions 549-615, 973-1266, 1981-2240.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini485 – 648164Helicase C-terminalAdd
BLAST
Domaini825 – 92096Dicer dsRNA-binding foldAdd
BLAST
Domaini1099 – 1246148PAZAdd
BLAST
Domaini1698 – 1919222RNase III 1Add
BLAST
Domaini1993 – 2150158RNase III 2Add
BLAST
Domaini2175 – 224167DRBMAdd
BLAST

Sequence similaritiesi

Contains 1 PAZ domain.
Contains 2 RNase III domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0571.
GeneTreeiENSGT00510000046789.
InParanoidiQ9VCU9.
KOiK11592.
OMAiKYAITTY.
OrthoDBiEOG78PV82.
PhylomeDBiQ9VCU9.

Family and domain databases

Gene3Di1.10.1520.10. 4 hits.
3.40.50.300. 1 hit.
InterProiIPR005034. Dicer_dimerisation_dom.
IPR014720. dsRNA-bd_dom.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR003100. PAZ_dom.
IPR000999. RNase_III_dom.
[Graphical view]
PfamiPF03368. Dicer_dimer. 1 hit.
PF00271. Helicase_C. 1 hit.
PF02170. PAZ. 1 hit.
PF00636. Ribonuclease_3. 2 hits.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
SM00490. HELICc. 1 hit.
SM00949. PAZ. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view]
SUPFAMiSSF101690. SSF101690. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF69065. SSF69065. 4 hits.
PROSITEiPS51327. 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]

Sequencei

Sequence statusi: Complete.

Q9VCU9-1 [UniParc]FASTAAdd to Basket

« Hide

MAFHWCDNNL HTTVFTPRDF QVELLATAYE RNTIICLGHR SSKEFIALKL     50
LQELSRRARR HGRVSVYLSC EVGTSTEPCS IYTMLTHLTD LRVWQEQPDM 100
QIPFDHCWTD YHVSILRPEG FLYLLETREL LLSSVELIVL EDCHDSAVYQ 150
RIRPLFENHI MPAPPADRPR ILGLAGPLHS AGCELQQLSA MLATLEQSVL 200
CQIETASDIV TVLRYCSRPH EYIVQCAPFE MDELSLVLAD VLNTHKSFLL 250
DHRYDPYEIY GTDQFMDELK DIPDPKVDPL NVINSLLVVL HEMGPWCTQR 300
AAHHFYQCNE KLKVKTPHER HYLLYCLVST ALIQLYSLCE HAFHRHLGSG 350
SDSRQTIERY SSPKVRRLLQ TLRCFKPEEV HTQADGLRRM RHQVDQADFN 400
RLSHTLESKC RMVDQMDQPP TETRALVATL EQILHTTEDR QTNRSAARVT 450
PTPTPAHAKP KPSSGANTAQ PRTRRRVYTR RHHRDHNDGS DTLCALIYCN 500
QNHTARVLFE LLAEISRRDP DLKFLRCQYT TDRVADPTTE PKEAELEHRR 550
QEEVLKRFRM HDCNVLIGTS VLEEGIDVPK CNLVVRWDPP TTYRSYVQCK 600
GRARAAPAYH VILVAPSYKS PTVGSVQLTD RSHRYICATG DTTEADSDSD 650
DSAMPNSSGS DPYTFGTARG TVKILNPEVF SKQPPTACDI KLQEIQDELP 700
AAAQLDTSNS SDEAVSMSNT SPSESSTEQK SRRFQCELSS LTEPEDTSDT 750
TAEIDTAHSL ASTTKDLVHQ MAQYREIEQM LLSKCANTEP PEQEQSEAER 800
FSACLAAYRP KPHLLTGASV DLGSAIALVN KYCARLPSDT FTKLTALWRC 850
TRNERAGVTL FQYTLRLPIN SPLKHDIVGL PMPTQTLARR LAALQACVEL 900
HRIGELDDQL QPIGKEGFRA LEPDWECFEL EPEDEQIVQL SDEPRPGTTK 950
RRQYYYKRIA SEFCDCRPVA GAPCYLYFIQ LTLQCPIPEE QNTRGRKIYP 1000
PEDAQQGFGI LTTKRIPKLS AFSIFTRSGE VKVSLELAKE RVILTSEQIV 1050
CINGFLNYTF TNVLRLQKFL MLFDPDSTEN CVFIVPTVKA PAGGKHIDWQ 1100
FLELIQANGN TMPRAVPDEE RQAQPFDPQR FQDAVVMPWY RNQDQPQYFY 1150
VAEICPHLSP LSCFPGDNYR TFKHYYLVKY GLTIQNTSQP LLDVDHTSAR 1200
LNFLTPRYVN RKGVALPTSS EETKRAKREN LEQKQILVPE LCTVHPFPAS 1250
LWRTAVCLPC ILYRINGLLL ADDIRKQVSA DLGLGRQQIE DEDFEWPMLD 1300
FGWSLSEVLK KSRESKQKES LKDDTINGKD LADVEKKPTS EETQLDKDSK 1350
DDKVEKSAIE LIIEGEEKLQ EADDFIEIGT WSNDMADDIA SFNQEDDDED 1400
DAFHLPVLPA NVKFCDQQTR YGSPTFWDVS NGESGFKGPK SSQNKQGGKG 1450
KAKGPAKPTF NYYDSDNSLG SSYDDDDNAG PLNYMHHNYS SDDDDVADDI 1500
DAGRIAFTSK NEAETIETAQ EVEKRQKQLS IIQATNANER QYQQTKNLLI 1550
GFNFKHEDQK EPATIRYEES IAKLKTEIES GGMLVPHDQQ LVLKRSDAAE 1600
AQVAKVSMME LLKQLLPYVN EDVLAKKLGD RRELLLSDLV ELNADWVARH 1650
EQETYNVMGC GDSFDNYNDH HRLNLDEKQL KLQYERIEIE PPTSTKAITS 1700
AILPAGFSFD RQPDLVGHPG PSPSIILQAL TMSNANDGIN LERLETIGDS 1750
FLKYAITTYL YITYENVHEG KLSHLRSKQV ANLNLYRLGR RKRLGEYMIA 1800
TKFEPHDNWL PPCYYVPKEL EKALIEAKIP THHWKLADLL DIKNLSSVQI 1850
CEMVREKADA LGLEQNGGAQ NGQLDDSNDS CNDFSCFIPY NLVSQHSIPD 1900
KSIADCVEAL IGAYLIECGP RGALLFMAWL GVRVLPITRQ LDGGNQEQRI 1950
PGSTKPNAEN VVTVYGAWPT PRSPLLHFAP NATEELDQLL SGFEEFEESL 2000
GYKFRDRSYL LQAMTHASYT PNRLTDCYQR LEFLGDAVLD YLITRHLYED 2050
PRQHSPGALT DLRSALVNNT IFASLAVRHG FHKFFRHLSP GLNDVIDRFV 2100
RIQQENGHCI SEEYYLLSEE ECDDAEDVEV PKALGDVFES IAGAIFLDSN 2150
MSLDVVWHVY SNMMSPEIEQ FSNSVPKSPI RELLELEPET AKFGKPEKLA 2200
DGRRVRVTVD VFCKGTFRGI GRNYRIAKCT AAKCALRQLK KQGLIAKKD 2249
Length:2,249
Mass (Da):255,330
Last modified:May 1, 2000 - v1
Checksum:iD693F0432AC8033D
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1338 – 13392PT → AI1 Publication
Sequence conflicti1345 – 13451L → I1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF56056.1.
AY050230 mRNA. Translation: AAK84929.1. Different initiation.
RefSeqiNP_524453.1. NM_079729.3.
UniGeneiDm.1283.

Genome annotation databases

EnsemblMetazoaiFBtr0084324; FBpp0083717; FBgn0039016.
GeneIDi42693.
KEGGidme:Dmel_CG4792.
UCSCiCG4792-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF56056.1 .
AY050230 mRNA. Translation: AAK84929.1 . Different initiation.
RefSeqi NP_524453.1. NM_079729.3.
UniGenei Dm.1283.

3D structure databases

ProteinModelPortali Q9VCU9.
SMRi Q9VCU9. Positions 549-615, 973-1266, 1981-2240.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 67642. 5 interactions.
DIPi DIP-23028N.
IntActi Q9VCU9. 4 interactions.
MINTi MINT-923321.

Proteomic databases

PaxDbi Q9VCU9.
PRIDEi Q9VCU9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0084324 ; FBpp0083717 ; FBgn0039016 .
GeneIDi 42693.
KEGGi dme:Dmel_CG4792.
UCSCi CG4792-RA. d. melanogaster.

Organism-specific databases

CTDi 42693.
FlyBasei FBgn0039016. Dcr-1.

Phylogenomic databases

eggNOGi COG0571.
GeneTreei ENSGT00510000046789.
InParanoidi Q9VCU9.
KOi K11592.
OMAi KYAITTY.
OrthoDBi EOG78PV82.
PhylomeDBi Q9VCU9.

Enzyme and pathway databases

Reactomei REACT_181252. Small interfering RNA (siRNA) biogenesis.

Miscellaneous databases

GenomeRNAii 42693.
NextBioi 830091.
PROi Q9VCU9.

Gene expression databases

Bgeei Q9VCU9.

Family and domain databases

Gene3Di 1.10.1520.10. 4 hits.
3.40.50.300. 1 hit.
InterProi IPR005034. Dicer_dimerisation_dom.
IPR014720. dsRNA-bd_dom.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR003100. PAZ_dom.
IPR000999. RNase_III_dom.
[Graphical view ]
Pfami PF03368. Dicer_dimer. 1 hit.
PF00271. Helicase_C. 1 hit.
PF02170. PAZ. 1 hit.
PF00636. Ribonuclease_3. 2 hits.
[Graphical view ]
SMARTi SM00358. DSRM. 1 hit.
SM00490. HELICc. 1 hit.
SM00949. PAZ. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view ]
SUPFAMi SSF101690. SSF101690. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF69065. SSF69065. 4 hits.
PROSITEi PS51327. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiDCR1_DROME
AccessioniPrimary (citable) accession number: Q9VCU9
Secondary accession number(s): Q961S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 108 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

External Data

Dasty 3

Similar proteinsi