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Protein

ATP-dependent RNA helicase rok1

Gene

rok1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi90 – 978ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-SPO-6791226. Major pathway of rRNA processing in the nucleolus.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase rok1 (EC:3.6.4.13)
Gene namesi
Name:rok1
ORF Names:SPAC22F3.08c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC22F3.08c.
PomBaseiSPAC22F3.08c. rok1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481ATP-dependent RNA helicase rok1PRO_0000055085Add
BLAST

Proteomic databases

MaxQBiQ09775.

Interactioni

Subunit structurei

Interacts with the U3 snoRNA and is associated with the 90S and 40S pre-ribosomes.By similarity

Protein-protein interaction databases

BioGridi278278. 135 interactions.
MINTiMINT-4694971.

Structurei

3D structure databases

ProteinModelPortaliQ09775.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 249173Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini260 – 422163Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi65 – 739Q motif
Motifi196 – 1994DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi423 – 47149Lys-richAdd
BLAST

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

HOGENOMiHOG000242486.
InParanoidiQ09775.
KOiK14779.
OMAiNITECTT.
OrthoDBiEOG74TX7R.
PhylomeDBiQ09775.

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.
[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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDALKLLTTN VKFKNKVPQP SIKEKEAKKL QGITKGKAKV TGNNPVDPIE
60 70 80 90 100
EFPEGILCEN LKKQNITECT TIQRYAIPTI GSKRDLLACA PTGSGKTIAY
110 120 130 140 150
LFPILQKLQL HVPGGYRAII VAPTRELCEQ IYRQAEKLSF GTSLKIIELS
160 170 180 190 200
KSNEKIQEKA PKLREKYDMC IGTPMRLVQA IQTGLSFEKV EFFVMDEADR
210 220 230 240 250
LFEPGFIEQT DHILSACTSS NICKSLFSAT IPSRVEELAK VVTVDPIRII
260 270 280 290 300
VGLKDAATDS IDQRLLFVGS DTSKIVILRQ MISNGELKPR VVIFVQDIER
310 320 330 340 350
AKALYTELLF DEIHVGVIHG ELPQAKREEA LAKFRKGEIW VLIATDLLAR
360 370 380 390 400
GIDFHGVKMV INFDFPQSVH SYIHRIGRTG RAGNTGQAVT FFTKEDGEYI
410 420 430 440 450
KLIAGVMRSS GCEVPNWVMA LPKPSKEMKK KLKKSPPKRK RITTRASYDR
460 470 480
QKEQRKKEYI KKVKKEASIK KHNEATGDSG Q
Length:481
Mass (Da):54,026
Last modified:November 1, 1995 - v1
Checksum:i872ECAFC106E110A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91073.1.
PIRiT38183. S62423.
RefSeqiNP_593033.1. NM_001018432.2.

Genome annotation databases

EnsemblFungiiSPAC22F3.08c.1; SPAC22F3.08c.1:pep; SPAC22F3.08c.
GeneIDi2541786.
KEGGispo:SPAC22F3.08c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91073.1.
PIRiT38183. S62423.
RefSeqiNP_593033.1. NM_001018432.2.

3D structure databases

ProteinModelPortaliQ09775.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278278. 135 interactions.
MINTiMINT-4694971.

Proteomic databases

MaxQBiQ09775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC22F3.08c.1; SPAC22F3.08c.1:pep; SPAC22F3.08c.
GeneIDi2541786.
KEGGispo:SPAC22F3.08c.

Organism-specific databases

EuPathDBiFungiDB:SPAC22F3.08c.
PomBaseiSPAC22F3.08c. rok1.

Phylogenomic databases

HOGENOMiHOG000242486.
InParanoidiQ09775.
KOiK14779.
OMAiNITECTT.
OrthoDBiEOG74TX7R.
PhylomeDBiQ09775.

Enzyme and pathway databases

ReactomeiR-SPO-6791226. Major pathway of rRNA processing in the nucleolus.

Miscellaneous databases

PROiQ09775.

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.
[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.
[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 nameiROK1_SCHPO
AccessioniPrimary (citable) accession number: Q09775
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 117 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. 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.