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Protein

Putative ATP-dependent RNA helicase me31b

Gene

me31B

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

Functioni

Unwinds RNA in an ATP-dependent fashion (Potential). Involved in germ cell formation.Curated1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi102 – 1098ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: GO_Central
  • RNA binding Source: FlyBase

GO - Biological processi

  • cytoplasmic mRNA processing body assembly Source: FlyBase
  • gene silencing by miRNA Source: FlyBase
  • habituation Source: FlyBase
  • mitotic G2 DNA damage checkpoint Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • pole cell formation Source: FlyBase
  • regulation of defense response to virus Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • regulation of olfactory learning Source: FlyBase
  • RNA secondary structure unwinding Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-DME-430039. mRNA decay by 5' to 3' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative ATP-dependent RNA helicase me31b (EC:3.6.4.13)
Alternative name(s):
Maternal expression at 31B
Gene namesi
Name:me31B
ORF Names:CG4916
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0004419. me31B.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis.

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • cytoplasmic mRNA processing body Source: FlyBase
  • cytoplasmic stress granule Source: GO_Central
  • microtubule associated complex Source: FlyBase
  • P granule Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi281 – 2811Q → A: Abolishes interaction with EDC3; when associated with A-284; A-288 and A-292. 1 Publication
Mutagenesisi284 – 2841H → A: Abolishes interaction with EDC3; when associated with A-281; A-288 and A-292. 1 Publication
Mutagenesisi288 – 2881T → A: Abolishes interaction with EDC3; when associated with A-281; A-284 and A-292. 1 Publication
Mutagenesisi292 – 2921K → A: Abolishes interaction with EDC3; when associated with A-281; A-284 and A-288. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Putative ATP-dependent RNA helicase me31bPRO_0000054982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine1 Publication
Modified residuei29 – 291Phosphoserine1 Publication
Modified residuei450 – 4501Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP23128.
PRIDEiP23128.

PTM databases

iPTMnetiP23128.

Expressioni

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiP23128.
GenevisibleiP23128. DM.

Interactioni

Subunit structurei

Interacts with EDC3, TraI/LSM14A, tud and vas.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cupQ9VMA33EBI-300281,EBI-95398

Protein-protein interaction databases

BioGridi60455. 9 interactions.
IntActiP23128. 11 interactions.
MINTiMINT-769276.
STRINGi7227.FBpp0079565.

Structurei

3D structure databases

ProteinModelPortaliP23128.
SMRiP23128. Positions 28-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini89 – 259171Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini269 – 429161Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi58 – 8629Q motifAdd
BLAST
Motifi207 – 2104DEAD box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0326. Eukaryota.
ENOG410XRAZ. LUCA.
GeneTreeiENSGT00840000129900.
InParanoidiP23128.
KOiK12614.
OMAiGVQVMVT.
OrthoDBiEOG7D85W7.
PhylomeDBiP23128.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P23128-1) [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
MMTEKLNSGH TNLTSKGIIN DLQIAGNTSD DMGWKSKLKL PPKDNRFKTT
60 70 80 90 100
DVTDTRGNEF EEFCLKRELL MGIFEKGWER PSPIQEAAIP IALSGKDVLA
110 120 130 140 150
RAKNGTGKTG AYCIPVLEQI DPTKDYIQAL VMVPTRELAL QTSQICIELA
160 170 180 190 200
KHLDIRVMVT TGGTILKDDI LRIYQKVQLI IATPGRILDL MDKKVADMSH
210 220 230 240 250
CRILVLDEAD KLLSLDFQGM LDHVILKLPK DPQILLFSAT FPLTVKNFME
260 270 280 290 300
KHLREPYEIN LMEELTLKGV TQYYAFVQER QKVHCLNTLF SKLQINQSII
310 320 330 340 350
FCNSTQRVEL LAKKITELGY CCYYIHAKMA QAHRNRVFHD FRQGLCRNLV
360 370 380 390 400
CSDLFTRGID VQAVNVVINF DFPRMAETYL HRIGRSGRFG HLGIAINLIT
410 420 430 440 450
YEDRFDLHRI EKELGTEIKP IPKVIDPALY VANVGASVGD TCNNSDLNNS

ANEEGNVSK
Length:459
Mass (Da):51,945
Last modified:February 2, 2004 - v3
Checksum:iB783E8185EF11E86
GO
Isoform B (identifier: P23128-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Note: No experimental confirmation available.
Show »
Length:428
Mass (Da):48,644
Checksum:i34E61B3C97D11A2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 457KLPPKDN → NCRQRTT in AAA28603 (PubMed:1900936).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3131Missing in isoform B. CuratedVSP_019286Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59926 mRNA. Translation: AAA28603.1.
AE014134 Genomic DNA. Translation: AAF52881.2.
AE014134 Genomic DNA. Translation: AAN10728.1.
AY051663 mRNA. Translation: AAK93087.1.
PIRiA39157.
RefSeqiNP_523533.2. NM_078809.4. [P23128-1]
NP_723539.1. NM_164898.2. [P23128-2]
UniGeneiDm.2770.

Genome annotation databases

EnsemblMetazoaiFBtr0079975; FBpp0079565; FBgn0004419. [P23128-1]
GeneIDi34364.
KEGGidme:Dmel_CG4916.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59926 mRNA. Translation: AAA28603.1.
AE014134 Genomic DNA. Translation: AAF52881.2.
AE014134 Genomic DNA. Translation: AAN10728.1.
AY051663 mRNA. Translation: AAK93087.1.
PIRiA39157.
RefSeqiNP_523533.2. NM_078809.4. [P23128-1]
NP_723539.1. NM_164898.2. [P23128-2]
UniGeneiDm.2770.

3D structure databases

ProteinModelPortaliP23128.
SMRiP23128. Positions 28-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60455. 9 interactions.
IntActiP23128. 11 interactions.
MINTiMINT-769276.
STRINGi7227.FBpp0079565.

PTM databases

iPTMnetiP23128.

Proteomic databases

PaxDbiP23128.
PRIDEiP23128.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079975; FBpp0079565; FBgn0004419. [P23128-1]
GeneIDi34364.
KEGGidme:Dmel_CG4916.

Organism-specific databases

CTDi34364.
FlyBaseiFBgn0004419. me31B.

Phylogenomic databases

eggNOGiKOG0326. Eukaryota.
ENOG410XRAZ. LUCA.
GeneTreeiENSGT00840000129900.
InParanoidiP23128.
KOiK12614.
OMAiGVQVMVT.
OrthoDBiEOG7D85W7.
PhylomeDBiP23128.

Enzyme and pathway databases

ReactomeiR-DME-430039. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

ChiTaRSime31B. fly.
GenomeRNAii34364.
PROiP23128.

Gene expression databases

BgeeiP23128.
GenevisibleiP23128. DM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A second maternally expressed Drosophila gene encodes a putative RNA helicase of the 'DEAD box' family."
    de Valoir T., Tucker M.A., Belikoff E.J., Camp L.A., Bolduc C., Beckingham K.
    Proc. Natl. Acad. Sci. U.S.A. 88:2113-2117(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), DEVELOPMENTAL STAGE.
  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 A).
    Strain: Berkeley.
    Tissue: Embryo.
  5. "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-8; SER-29 AND SER-450, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  6. "Similar modes of interaction enable Trailer Hitch and EDC3 to associate with DCP1 and Me31B in distinct protein complexes."
    Tritschler F., Eulalio A., Helms S., Schmidt S., Coles M., Weichenrieder O., Izaurralde E., Truffault V.
    Mol. Cell. Biol. 28:6695-6708(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EDC3 AND TRAI/LSM14A.
  7. "Isolation of new polar granule components in Drosophila reveals P body and ER associated proteins."
    Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.
    Mech. Dev. 125:865-873(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TUD AND VAS, SUBCELLULAR LOCATION.
  8. "Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B."
    Tritschler F., Braun J.E., Eulalio A., Truffault V., Izaurralde E., Weichenrieder O.
    Mol. Cell 33:661-668(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EDC3, MUTAGENESIS OF GLN-281; HIS-284; THR-288 AND LYS-292.

Entry informationi

Entry nameiDDX6_DROME
AccessioniPrimary (citable) accession number: P23128
Secondary accession number(s): Q8IPC9, Q961D2, Q9VL17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: February 2, 2004
Last modified: July 6, 2016
This is version 155 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.