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Protein

ATP-dependent RNA helicase DBP5

Gene

DBP5

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi145 – 152ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, RNA-binding
Biological processmRNA transport, Protein transport, Translocation, Transport
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DBP5 (EC:3.6.4.13)
Gene namesi
Name:DBP5
Ordered Locus Names:YALI0E31427g
OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic identifieri284591 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
Proteomesi
  • UP000001300 Componenti: Chromosome E

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002322281 – 488ATP-dependent RNA helicase DBP5Add BLAST488

Proteomic databases

PRIDEiQ6C3X7.

Interactioni

Subunit structurei

Associates with the nuclear pore complex.By similarity

Protein-protein interaction databases

STRINGi4952.XP_504635.1.

Structurei

3D structure databases

ProteinModelPortaliQ6C3X7.
SMRiQ6C3X7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini132 – 298Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST167
Domaini326 – 477Helicase C-terminalPROSITE-ProRule annotationAdd BLAST152

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi99 – 127Q motifAdd BLAST29
Motifi246 – 249DEAD box4

Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000268797.
InParanoidiQ6C3X7.
KOiK18655.
OMAiPPRNMIA.
OrthoDBiEOG092C2B1L.

Family and domain databases

InterProiView protein in InterPro
IPR011545. 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.
PfamiView protein in Pfam
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiView protein in PROSITE
PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6C3X7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDQVSDMLE KLELQKEKNQ AAATEAKVEE VKEDDKKDVK EELNEDDKKV
60 70 80 90 100
AKEDDKKEDA KEESKEDAEE NNLIQTEYEV RVKLADLQAD PNSPLYSAKR
110 120 130 140 150
FEDLGLDENL LKGLYAMKFN KPSKIQEKAL PLLLSDPPHN MIGQSQSGTG
160 170 180 190 200
KTGAFSLTML SRVDPNLKAV QCICLAPSRE LARQTLDVVD EMKKFTDITT
210 220 230 240 250
HLIVPESTER GQKVTSQILV GTPGSVAGLL QKKQIDAKHV KVFVLDEADN
260 270 280 290 300
MVDSSMGSTC ARIKKYLPSS TQVVLFSATF PESVLDLAGK MCPNPNEIRL
310 320 330 340 350
KANELNVDAI TQLYMDCEDG EEKFKMLEEL YSMLTIASSV IFVAQRSTAN
360 370 380 390 400
ALYQRMSKNG HKVSLLHSDL SVDERDRLMD DFRFGRSKVL ISTNVIARGI
410 420 430 440 450
DIATVSMVVN YDLPTDKNGK PDPETYLHRI GRTGRFGRSG VSISFVHDEA
460 470 480
SFEVLDSIQQ SLGMTLTQVP TDDIDEVEEI IKKAIKGK
Length:488
Mass (Da):54,389
Last modified:August 16, 2004 - v1
Checksum:i54BD916D85DE2A99
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382131 Genomic DNA. Translation: CAG80239.1.
RefSeqiXP_504635.1. XM_504635.1.

Genome annotation databases

EnsemblFungiiCAG80239; CAG80239; YALI0_E31427g.
GeneIDi2911469.
KEGGiyli:YALI0E31427g.

Similar proteinsi

Entry informationi

Entry nameiDBP5_YARLI
AccessioniPrimary (citable) accession number: Q6C3X7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 16, 2004
Last modified: July 5, 2017
This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families