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Database: UniProt
Entry: Q09775
LinkDB: Q09775
Original site: Q09775 
ID   ROK1_SCHPO              Reviewed;         481 AA.
AC   Q09775;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-OCT-2019, entry version 136.
DE   RecName: Full=ATP-dependent RNA helicase rok1;
DE            EC=3.6.4.13;
GN   Name=rok1; ORFNames=SPAC22F3.08c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal
CC       subunit biogenesis. Required for the processing and cleavage of
CC       35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Interacts with the U3 snoRNA and is associated with the
CC       90S and 40S pre-ribosomes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX52/ROK1
CC       subfamily. {ECO:0000305}.
DR   EMBL; CU329670; CAA91073.1; -; Genomic_DNA.
DR   PIR; T38183; S62423.
DR   RefSeq; NP_593033.1; NM_001018432.2.
DR   SMR; Q09775; -.
DR   BioGrid; 278278; 138.
DR   STRING; 4896.SPAC22F3.08c.1; -.
DR   MaxQB; Q09775; -.
DR   PaxDb; Q09775; -.
DR   PRIDE; Q09775; -.
DR   EnsemblFungi; SPAC22F3.08c.1; SPAC22F3.08c.1:pep; SPAC22F3.08c.
DR   GeneID; 2541786; -.
DR   KEGG; spo:SPAC22F3.08c; -.
DR   EuPathDB; FungiDB:SPAC22F3.08c; -.
DR   PomBase; SPAC22F3.08c; rok1.
DR   HOGENOM; HOG000242486; -.
DR   InParanoid; Q09775; -.
DR   KO; K14779; -.
DR   OMA; KSSKKFX; -.
DR   PhylomeDB; Q09775; -.
DR   Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q09775; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; ISO:PomBase.
DR   GO; GO:0005524; F:ATP binding; IC:PomBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; ISO:PomBase.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    481       ATP-dependent RNA helicase rok1.
FT                                /FTId=PRO_0000055085.
FT   DOMAIN       77    249       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      260    422       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      90     97       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        65     73       Q motif.
FT   MOTIF       196    199       DEAD box.
FT   COMPBIAS    423    471       Lys-rich.
SQ   SEQUENCE   481 AA;  54026 MW;  872ECAFC106E110A CRC64;
     MDALKLLTTN VKFKNKVPQP SIKEKEAKKL QGITKGKAKV TGNNPVDPIE EFPEGILCEN
     LKKQNITECT TIQRYAIPTI GSKRDLLACA PTGSGKTIAY LFPILQKLQL HVPGGYRAII
     VAPTRELCEQ IYRQAEKLSF GTSLKIIELS KSNEKIQEKA PKLREKYDMC IGTPMRLVQA
     IQTGLSFEKV EFFVMDEADR LFEPGFIEQT DHILSACTSS NICKSLFSAT IPSRVEELAK
     VVTVDPIRII VGLKDAATDS IDQRLLFVGS DTSKIVILRQ MISNGELKPR VVIFVQDIER
     AKALYTELLF DEIHVGVIHG ELPQAKREEA LAKFRKGEIW VLIATDLLAR GIDFHGVKMV
     INFDFPQSVH SYIHRIGRTG RAGNTGQAVT FFTKEDGEYI KLIAGVMRSS GCEVPNWVMA
     LPKPSKEMKK KLKKSPPKRK RITTRASYDR QKEQRKKEYI KKVKKEASIK KHNEATGDSG
     Q
//
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