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Protein

ATP-dependent RNA helicase ROK1

Gene

ROK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA. May also have a gene-specific regulatory function since it affects nuclear fusion by regulating KAR4 expression and contributes with KEM1 to ISP-1 sensitivity.5 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: SGD
  • RNA binding Source: UniProtKB-KW
  • RNA-dependent ATPase activity Source: SGD

GO - Biological processi

  • endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • maturation of SSU-rRNA Source: SGD
  • snoRNA localization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30659-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase ROK1 (EC:3.6.4.13)
Alternative name(s):
Rescuer of KEM1 protein 1
Gene namesi
Name:ROK1
Ordered Locus Names:YGL171W
ORF Names:G1651
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL171w.
EuPathDBiFungiDB:YGL171W.
SGDiS000003139. ROK1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi166 – 1661G → D: No cell growth and 2-fold decrease in ATPase activity in vitro. 1 Publication
Mutagenesisi172 – 1721K → G, R, S or W: Slow cell growth. 1 Publication
Mutagenesisi172 – 1721K → L: No cell growth and drastic decrease in ATPase activity in vitro. 1 Publication
Mutagenesisi280 – 2801D → A or V: Slow cell growth. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 564564ATP-dependent RNA helicase ROK1PRO_0000055063Add
BLAST

Proteomic databases

MaxQBiP45818.
PaxDbiP45818.
PeptideAtlasiP45818.

Interactioni

Subunit structurei

Interacts with the U3 snoRNA and is associated with the 90S and 40S pre-ribosomes. This association requires the presence of RRP5. Interacts also with OSH3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OSH3P387133EBI-15686,EBI-12630

Protein-protein interaction databases

BioGridi33082. 34 interactions.
DIPiDIP-5111N.
IntActiP45818. 16 interactions.
MINTiMINT-483312.
STRINGi4932.YGL171W.

Structurei

3D structure databases

ProteinModelPortaliP45818.
SMRiP45818. Positions 91-511.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini153 – 333181Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini344 – 506163Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi122 – 15029Q motifAdd
BLAST
Motifi280 – 2834DEAD 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

eggNOGiCOG0513.
GeneTreeiENSGT00550000074863.
HOGENOMiHOG000242486.
InParanoidiP45818.
KOiK14779.
OMAiMDFKGVR.
OrthoDBiEOG74TX7R.

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. 2 hits.
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.

P45818-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIFRVLTRG ASVKKESGPK AKAADYSVIN GNDENHKEDN NESQIVKELD
60 70 80 90 100
FFRNKRIISK VEDDREKTTE NDSPNKEEKS GNDDGLIKPV ITNTVEASAL
110 120 130 140 150
RKSYKGNVSG IDIPLPIGSF EDLISRFSFD KRLLNNLIEN GFTEPTPIQC
160 170 180 190 200
ECIPVALNNR DVLACGPTGS GKTLAFLIPL VQQIIDDKQT AGLKGLIISP
210 220 230 240 250
TKELANQIFI ECFKLSYKIF LEKKRPLQVA LLSKSLGAKL KNKVVSDKKY
260 270 280 290 300
DIIISTPLRL IDVVKNEALD LSKVKHLIFD EADKLFDKTF VEQSDDILSA
310 320 330 340 350
CREPSLRKAM FSATIPSNVE EIAQSIMMDP VRVIIGHKEA ANTNIEQKLI
360 370 380 390 400
FCGNEEGKLI AIRQLVQEGE FKPPIIIFLE SITRAKALYH ELMYDRINVD
410 420 430 440 450
VIHAERTALQ RDRIIERFKT GELWCLICTD VLARGIDFKG VNLVINYDVP
460 470 480 490 500
GSSQAYVHRI GRTGRGGRSG KAITFYTKQD SVAIKPIINV MKQSGCEVSE
510 520 530 540 550
WMDKMAKMTR KEKESIKNGK AHKERKQITT VPKMDKAKRR RQQEMIAASK
560
RRKNEELSKK HFSK
Length:564
Mass (Da):63,653
Last modified:November 1, 1995 - v1
Checksum:iCACB950B8A15D5A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z34901 Genomic DNA. Translation: CAA84384.1.
X85757 Genomic DNA. Translation: CAA59758.1.
Z72693 Genomic DNA. Translation: CAA96883.1.
BK006941 Genomic DNA. Translation: DAA07942.1.
PIRiS59649.
RefSeqiNP_011344.1. NM_001181036.1.

Genome annotation databases

EnsemblFungiiYGL171W; YGL171W; YGL171W.
GeneIDi852704.
KEGGisce:YGL171W.

Cross-referencesi

Web resourcesi

RNA helicases from the baker's yeast Saccharomyces cerevisiae

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z34901 Genomic DNA. Translation: CAA84384.1.
X85757 Genomic DNA. Translation: CAA59758.1.
Z72693 Genomic DNA. Translation: CAA96883.1.
BK006941 Genomic DNA. Translation: DAA07942.1.
PIRiS59649.
RefSeqiNP_011344.1. NM_001181036.1.

3D structure databases

ProteinModelPortaliP45818.
SMRiP45818. Positions 91-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33082. 34 interactions.
DIPiDIP-5111N.
IntActiP45818. 16 interactions.
MINTiMINT-483312.
STRINGi4932.YGL171W.

Proteomic databases

MaxQBiP45818.
PaxDbiP45818.
PeptideAtlasiP45818.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL171W; YGL171W; YGL171W.
GeneIDi852704.
KEGGisce:YGL171W.

Organism-specific databases

CYGDiYGL171w.
EuPathDBiFungiDB:YGL171W.
SGDiS000003139. ROK1.

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00550000074863.
HOGENOMiHOG000242486.
InParanoidiP45818.
KOiK14779.
OMAiMDFKGVR.
OrthoDBiEOG74TX7R.

Enzyme and pathway databases

BioCyciYEAST:G3O-30659-MONOMER.

Miscellaneous databases

NextBioi972056.
PROiP45818.

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. 2 hits.
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. "ROK1, a high-copy-number plasmid suppressor of kem1, encodes a putative ATP-dependent RNA helicase in Saccharomyces cerevisiae."
    Song Y., Kim S., Kim J.
    Gene 166:151-154(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A putative helicase, the SUA5, PMR1, tRNALys1 genes and four open reading frames have been detected in the DNA sequence of an 8.8 kb fragment of the left arm of chromosome VII of Saccharomyces cerevisiae."
    Klima R., Coglievina M., Zaccaria P., Bertani I., Bruschi C.V.
    Yeast 12:1033-1040(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Rok1p is a putative RNA helicase required for rRNA processing."
    Venema J., Bousquet-Antonelli C., Gelugne J.-P., Caizergues-Ferrer M., Tollervey D.
    Mol. Cell. Biol. 17:3398-3407(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Two mutant forms of the S1/TPR-containing protein Rrp5p affect the 18S rRNA synthesis in Saccharomyces cerevisiae."
    Torchet C., Jacq C., Hermann-Le Denmat S.
    RNA 4:1636-1652(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "ATP hydrolysis activity of the DEAD box protein Rok1p is required for in vivo ROK1 function."
    Oh J.Y., Kim J.
    Nucleic Acids Res. 27:2753-2759(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-166; LYS-172 AND ASP-280.
  8. "Two-hybrid cloning and characterization of OSH3, a yeast oxysterol-binding protein homolog."
    Park Y.-U., Hwang O., Kim J.
    Biochem. Biophys. Res. Commun. 293:733-740(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OSH3.
  9. "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes."
    Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.
    EMBO J. 22:1370-1380(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE 90S AND 40S PRE-RIBOSOMES, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Deletion of OSH3 gene confers resistance against ISP-1 in Saccharomyces cerevisiae."
    Yano T., Inukai M., Isono F.
    Biochem. Biophys. Res. Commun. 315:228-234(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Posttranscriptional regulation of the karyogamy gene by Kem1p/Xrn1p exoribonuclease and Rok1p RNA helicase of Saccharomyces cerevisiae."
    Kim J., Jeon S., Yang Y.-S., Kim J.
    Biochem. Biophys. Res. Commun. 321:1032-1039(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "U3 snoRNP and Rrp5p associate independently with Saccharomyces cerevisiae 35S pre-rRNA, but Rrp5p is essential for association of Rok1p."
    Vos H.R., Bax R., Faber A.W., Vos J.C., Raue H.A.
    Nucleic Acids Res. 32:5827-5833(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE U3 SNORNA, ASSOCIATION WITH THE PRE-RIBOSOME.

Entry informationi

Entry nameiROK1_YEAST
AccessioniPrimary (citable) accession number: P45818
Secondary accession number(s): D6VTY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 138 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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 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.