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Protein

ATP-dependent RNA helicase dbp2

Gene

dbp2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi166 – 1738ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Nonsense-mediated mRNA decay, Ribosome biogenesis, rRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase dbp2 (EC:3.6.4.13)
Alternative name(s):
p68-like protein
Gene namesi
Name:dbp2
ORF Names:SPBP8B7.16c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBP8B7.16c.
PomBaseiSPBP8B7.16c. dbp2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleolus Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 550550ATP-dependent RNA helicase dbp2PRO_0000054998Add
BLAST

Proteomic databases

MaxQBiP24782.
PRIDEiP24782.

Interactioni

Subunit structurei

Associates with polysomes.By similarity

Protein-protein interaction databases

BioGridi277894. 6 interactions.
IntActiP24782. 1 interaction.
MINTiMINT-4687851.

Structurei

3D structure databases

ProteinModelPortaliP24782.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini153 – 328176Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini340 – 503164Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni510 – 53324RNA-binding RGG-boxAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi122 – 15029Q motifAdd
BLAST
Motifi276 – 2794DEAD box

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

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

Phylogenomic databases

HOGENOMiHOG000268804.
InParanoidiP24782.
KOiK12823.
OMAiGSNVANM.
OrthoDBiEOG7TJ3T2.
PhylomeDBiP24782.

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]

Sequencei

Sequence statusi: Complete.

P24782-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYRDNEYSG NYNGKEDGYN SRGRYGGGYR NNYSRGGGRG GFNDGASYGY
60 70 80 90 100
DQRGQGRNFY ESDGPGANLV KKDWKNETLI PFQKDFYKEH ENVRNRSDAE
110 120 130 140 150
VTEYRKEKEI VVHGLNVPKP VTTFEEAGFP NYVLKEVKQL GFEAPTPIQQ
160 170 180 190 200
QAWPMAMSGR DMVGISATGS GKTLSYCLPA IVHINAQPLL SPGDGPIVLV
210 220 230 240 250
LAPTRELAVQ IQQECTKFGK SSRIRNTCVY GGVPRGPQIR DLIRGVEICI
260 270 280 290 300
ATPGRLLDML DSNKTNLRRV TYLVLDEADR MLDMGFEPQI RKIVDQIRPD
310 320 330 340 350
RQTVMFSATW PKEVQRLARD YLNDYIQVTV GSLDLAASHN IKQIVEVVDN
360 370 380 390 400
ADKRARLGKD IEEVLKDRDN KVLIFTGTKR VADDITRFLR QDGWPALAIH
410 420 430 440 450
GDKAQDERDW VLNEFRTGKS PIMVATDVAS RGIDVKGITH VFNYDFPGNT
460 470 480 490 500
EDYVHRIGRT GRAGAKGTAY TYFTSDNAKQ ARELVSILSE AKQDIDPKLE
510 520 530 540 550
EMARYSSGGR GGNYRRGGYG RGGFRRGGGY GNRNRGFTGS NSAPLARSRW
Length:550
Mass (Da):61,548
Last modified:December 1, 2000 - v2
Checksum:i3BD1636D14275451
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351R → L in CAA36873 (PubMed:1996094).Curated
Sequence conflicti240 – 2401R → L in CAA36873 (PubMed:1996094).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52648 Genomic DNA. Translation: CAA36873.1.
L11574 mRNA. Translation: AAA35319.1.
CU329671 Genomic DNA. Translation: CAA21801.1.
PIRiT40810. S14048.
RefSeqiNP_596523.1. NM_001022444.2.

Genome annotation databases

EnsemblFungiiSPBP8B7.16c.1; SPBP8B7.16c.1:pep; SPBP8B7.16c.
GeneIDi2541383.
KEGGispo:SPBP8B7.16c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52648 Genomic DNA. Translation: CAA36873.1.
L11574 mRNA. Translation: AAA35319.1.
CU329671 Genomic DNA. Translation: CAA21801.1.
PIRiT40810. S14048.
RefSeqiNP_596523.1. NM_001022444.2.

3D structure databases

ProteinModelPortaliP24782.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277894. 6 interactions.
IntActiP24782. 1 interaction.
MINTiMINT-4687851.

Proteomic databases

MaxQBiP24782.
PRIDEiP24782.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBP8B7.16c.1; SPBP8B7.16c.1:pep; SPBP8B7.16c.
GeneIDi2541383.
KEGGispo:SPBP8B7.16c.

Organism-specific databases

EuPathDBiFungiDB:SPBP8B7.16c.
PomBaseiSPBP8B7.16c. dbp2.

Phylogenomic databases

HOGENOMiHOG000268804.
InParanoidiP24782.
KOiK12823.
OMAiGSNVANM.
OrthoDBiEOG7TJ3T2.
PhylomeDBiP24782.

Miscellaneous databases

NextBioi20802492.
PROiP24782.

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. "p68 RNA helicase: identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts."
    Iggo R.D., Jamieson D.J., McNeill S.A., Southgate J., McPheat J., Lane D.P.
    Mol. Cell. Biol. 11:1326-1333(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiDBP2_SCHPO
AccessioniPrimary (citable) accession number: P24782
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: December 1, 2000
Last modified: May 11, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.