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Protein

ATP-dependent RNA helicase dbp5

Gene

dbp5

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

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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi160 – 1678ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase dbp5 (EC:3.6.4.13)
Gene namesi
Name:dbp5
ORF Names:SPBC12C2.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC12C2.06.
PomBaseiSPBC12C2.06. dbp5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nuclear envelope Source: PomBase
  • nuclear membrane Source: UniProtKB-SubCell
  • nuclear pore Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503ATP-dependent RNA helicase dbp5PRO_0000055020Add
BLAST

Proteomic databases

MaxQBiQ09747.

Interactioni

Subunit structurei

Associates with the nuclear pore complex.By similarity

Protein-protein interaction databases

BioGridi276519. 8 interactions.
MINTiMINT-4694662.

Structurei

Secondary structure

1
503
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi142 – 1443Combined sources
Helixi145 – 1495Combined sources
Beta strandi156 – 1594Combined sources
Helixi167 – 17711Combined sources
Beta strandi187 – 1904Combined sources
Helixi194 – 20714Combined sources
Beta strandi232 – 2365Combined sources
Helixi238 – 2469Combined sources
Beta strandi257 – 2604Combined sources
Helixi263 – 2664Combined sources
Helixi273 – 28210Combined sources
Beta strandi288 – 2947Combined sources
Helixi299 – 3079Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi329 – 3357Combined sources
Helixi337 – 34711Combined sources
Beta strandi355 – 3584Combined sources
Turni362 – 3665Combined sources
Helixi367 – 3726Combined sources
Turni373 – 3764Combined sources
Helixi392 – 3943Combined sources
Helixi396 – 3994Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi423 – 4253Combined sources
Helixi440 – 4445Combined sources
Beta strandi457 – 4637Combined sources
Turni464 – 4663Combined sources
Beta strandi467 – 4704Combined sources
Helixi471 – 4777Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FHOX-ray2.80A/B139-503[»]
ProteinModelPortaliQ09747.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ09747.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 314168Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini325 – 493169Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi114 – 14229Q motifAdd
BLAST
Motifi261 – 2644DEAD 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

HOGENOMiHOG000268797.
InParanoidiQ09747.
KOiK18655.
OMAiNKLDTDD.
OrthoDBiEOG7FNCJ0.
PhylomeDBiQ09747.

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.

Q09747-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTLGQESK TDWASLDSDE EVQRISDKVN QLNTSENKNE DQKATNLSDR
60 70 80 90 100
LGPKITENVD AKSEQDKATN TIAEDANTKQ SENDESNLIP NKNEVRVKLA
110 120 130 140 150
DLQADPNSPL FSVKSFEELE LKPELLKGIY SMKFQKPSKI QEKALPLLLS
160 170 180 190 200
NPPRNMIGQS QSGTGKTAAF ALTMLSRVDA SVPKPQAICL APSRELARQI
210 220 230 240 250
MDVVTEMGKY TEVKTAFGIK DSVPKGAKID AQIVIGTPGT VMDLMKRRQL
260 270 280 290 300
DARDIKVFVL DEADNMLDQQ GLGDQSMRIK HLLPRNTQIV LFSATFSERV
310 320 330 340 350
EKYAERFAPN ANEIRLKTEE LSVEGIKQLY MDCQSEEHKY NVLVELYGLL
360 370 380 390 400
TIGQSIIFCK KKDTAEEIAR RMTADGHTVA CLTGNLEGAQ RDAIMDSFRV
410 420 430 440 450
GTSKVLVTTN VIARGIDVSQ VNLVVNYDMP LDQAGRPDPQ TYLHRIGRTG
460 470 480 490 500
RFGRVGVSIN FVHDKKSWEE MNAIQEYFQR PITRVPTDDY EELEKVVKNA

LKM
Length:503
Mass (Da):56,305
Last modified:November 1, 1995 - v1
Checksum:i68C7C8BD6AED252F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA90819.1.
PIRiT39375.
RefSeqiNP_596016.1. NM_001021924.2.

Genome annotation databases

EnsemblFungiiSPBC12C2.06.1; SPBC12C2.06.1:pep; SPBC12C2.06.
GeneIDi2539975.
KEGGispo:SPBC12C2.06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA90819.1.
PIRiT39375.
RefSeqiNP_596016.1. NM_001021924.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FHOX-ray2.80A/B139-503[»]
ProteinModelPortaliQ09747.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276519. 8 interactions.
MINTiMINT-4694662.

Proteomic databases

MaxQBiQ09747.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC12C2.06.1; SPBC12C2.06.1:pep; SPBC12C2.06.
GeneIDi2539975.
KEGGispo:SPBC12C2.06.

Organism-specific databases

EuPathDBiFungiDB:SPBC12C2.06.
PomBaseiSPBC12C2.06. dbp5.

Phylogenomic databases

HOGENOMiHOG000268797.
InParanoidiQ09747.
KOiK18655.
OMAiNKLDTDD.
OrthoDBiEOG7FNCJ0.
PhylomeDBiQ09747.

Miscellaneous databases

EvolutionaryTraceiQ09747.
PROiQ09747.

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

  1. "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 nameiDBP5_SCHPO
AccessioniPrimary (citable) accession number: Q09747
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.