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- SASDF52: dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensat... -

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Basic information

Entry
Database: SASBDB / ID: SASDF52
SampledsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE
  • Dosage compensation regulator (protein), MLE, Drosophila melanogaster
Function / homology
Function and homology information


RIP-mediated NFkB activation via ZBP1 / X chromosome located dosage compensation complex, transcription activating / 3'-5' DNA/RNA helicase activity / DEx/H-box helicases activate type I IFN and inflammatory cytokines production / male courtship behavior, veined wing generated song production / regulation of cytoplasmic translation / regulatory region RNA binding / sex-chromosome dosage compensation / PKR-mediated signaling / MSL complex ...RIP-mediated NFkB activation via ZBP1 / X chromosome located dosage compensation complex, transcription activating / 3'-5' DNA/RNA helicase activity / DEx/H-box helicases activate type I IFN and inflammatory cytokines production / male courtship behavior, veined wing generated song production / regulation of cytoplasmic translation / regulatory region RNA binding / sex-chromosome dosage compensation / PKR-mediated signaling / MSL complex / dosage compensation by hyperactivation of X chromosome / positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity / polytene chromosome / 3'-5' RNA helicase activity / regulation of mRNA processing / axon extension / lncRNA binding / 3'-5' DNA helicase activity / DNA duplex unwinding / nuclear chromosome / positive regulation of heterochromatin formation / X chromosome / DNA helicase activity / helicase activity / determination of adult lifespan / double-stranded RNA binding / chromosome / double-stranded DNA binding / RNA helicase activity / RNA helicase / ribonucleoprotein complex / chromatin binding / chromatin / nucleolus / ATP hydrolysis activity / positive regulation of transcription by RNA polymerase II / RNA binding / ATP binding / nucleus / cytosol
Similarity search - Function
DHX9, first double-stranded RNA binding domain / DHX9, second double-stranded RNA binding domain / DHX9, DEXH-box helicase domain / : / Helicase associated domain (HA2), ratchet-like / DEAD-box helicase, OB fold / Oligonucleotide/oligosaccharide-binding (OB)-fold / Helicase-associated domain / Helicase associated domain (HA2), winged-helix / Helicase associated domain (HA2) Add an annotation ...DHX9, first double-stranded RNA binding domain / DHX9, second double-stranded RNA binding domain / DHX9, DEXH-box helicase domain / : / Helicase associated domain (HA2), ratchet-like / DEAD-box helicase, OB fold / Oligonucleotide/oligosaccharide-binding (OB)-fold / Helicase-associated domain / Helicase associated domain (HA2), winged-helix / Helicase associated domain (HA2) Add an annotation / Double-stranded RNA binding motif / Double-stranded RNA binding motif / DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site / DEAH-box subfamily ATP-dependent helicases signature. / Double stranded RNA-binding domain (dsRBD) profile. / Double-stranded RNA-binding domain / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / Helicase conserved C-terminal domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Dosage compensation regulator
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
Contact author
  • Po-chia Chen (EMBL, European Molecular Biology Laboratory (EMBL) - Heidelberg, Heidelberg, Germany)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #2736
Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 2.089
Search similar-shape structures of this assembly by Omokage search (details)
Model #2737
Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 2.089
Search similar-shape structures of this assembly by Omokage search (details)
Model #2738
Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 2.089
Search similar-shape structures of this assembly by Omokage search (details)
Model #2739
Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 2.089
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE
Specimen concentration: 5.00-5.00
BufferName: 20 mM NaPO4, 200 mM NaCl, 1 mM DTT / pH: 6.5
Entity #1422Name: MLE / Type: protein / Description: Dosage compensation regulator / Formula weight: 28.549 / Num. of mol.: 1 / Source: Drosophila melanogaster / References: UniProt: P24785
Sequence: GAMDIKSFLY QFCAKSQIEP KFDIRQTGPK NRQRFLCEVR VEPNTYIGVG NSTNKKDAEK NACRDFVNYL VRVGKLNTND VPADAGASGG GPRTGLEGAG MAGGSGQQKR VFDGQSGPQD LGEAYRPLNH DGGDGGNRYS VIDRIQEQRD MNEAEAFDVN AAIHGNWTIE ...Sequence:
GAMDIKSFLY QFCAKSQIEP KFDIRQTGPK NRQRFLCEVR VEPNTYIGVG NSTNKKDAEK NACRDFVNYL VRVGKLNTND VPADAGASGG GPRTGLEGAG MAGGSGQQKR VFDGQSGPQD LGEAYRPLNH DGGDGGNRYS VIDRIQEQRD MNEAEAFDVN AAIHGNWTIE NAKERLNIYK QTNNIRDDYK YTPVGPEHAR SFLAELSIYV PALNRTVTAR ESGSNKKSAS KSCALSLVRQ LFHLNVIEPF SGTLKKKKD

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Experimental information

BeamInstrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.09919 Å / Dist. spec. to detc.: 2.867 mm
DetectorName: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm
Scan
Title: dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE
Measurement date: Nov 29, 2016 / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/nm /
MinMax
Q0.0348 4.9439
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 414 /
MinMax
Q0.0583505 2.0041
P(R) point1 414
R0 12.5
Result
Type of curve: single_conc
Comments: Construct contains an additional two amino acids (Gly-Ala) at the N-terminus as a remaining product the TEV-protease cleavage. The data displayed in this entry consists of merged data from ...Comments: Construct contains an additional two amino acids (Gly-Ala) at the N-terminus as a remaining product the TEV-protease cleavage. The data displayed in this entry consists of merged data from three replicates of equal sample concentration (5.0 mg/ml). Thus, an effective total of 30 frames x 1s exposures is collated for this curve. The data were merged using Primus and datmerge of the ATSAS 2.8.4-1 package maintained by SBGrid.
ExperimentalPorod
MW14.8 kDa14 kDa
Volume-22 nm3

P(R)GuinierGuinier error
Forward scattering, I066.44 66.26 0.13
Radius of gyration, Rg3.337 nm3.23 nm0.13

MinMax
D-12.5
Guinier point6 60

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